The transport of iron between cells is mediated by transferrin. However, iron can also enter and leave cells not only by itself, but also in the form of heme and siderophores. When entering the cell via the main path (by transferrin endocytosis), its goal is not the (still elusive) chelated iron pool in the cytosol nor the lysosomes but the mitochondria, where heme is synthesized and iron-sulfur clusters are assembled (Kurz et al,2008, Hower et al 2009, Richardson et al 2010).Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=917937
This pathway was inferred from Homo sapiens pathway [http://wikipathways.org/instance/WP2670_r76854 WP2670(76854)] with a 88.0% conversion rate.
a38
b79
c84
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9Y5Y0
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8WZ55
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P54709
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02787
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P36543
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q86UD5
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9NY37
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P78348
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P58549
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P47870
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P20648
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q70Z44
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8NEY4
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02786
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51800
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51170
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8N8Y2
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51168
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P28472
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P14415
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q13061
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P21817
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P49281
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96LB4
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P47869
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P27449
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q13488
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9Y5K8
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51164
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O15342
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O00476
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51172
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O75185
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02787
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O95264
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P04049
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51172
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P34903
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q15413
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q86WC4
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9Y487
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O43307
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02787
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q99576
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P18505
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P18507
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51798
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96PU5
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P98194
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q13733
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P05026
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O00168
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9UI12
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8NHE4
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q04656
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O00476
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P38606
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q658P3
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P48169
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P05023
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O95670
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P28476
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96A05
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q53TN4
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P61421
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9NP59
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96NT5
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q16445
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9UHC3
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51168
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51790
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9HBY8
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02792
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O00141
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9HBG4
aae
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P15313
The ferritin complex is an oligomer of 24 subunits with light and heavy chains. The major chain can be light or heavy, depending on the tissue type. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited. Iron metabolism provides a useful example of gene expression translational control. Increased iron levels stimulate the synthesis of the iron-binding protein, ferritin, without any corresponding increase in the amount of ferritin mRNA. The 5?-UTR of both ferritin heavy chain mRNA and light chain mRNA contain a single iron-response element (IRE), a specific cis-acting regulatory sequence which forms a hairpin structure.
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9H0Q3
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:A5X5Y0
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P35670
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P24046
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02786
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P21281
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P13637
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O75348
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02787
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P37088
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02787
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51801
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P50993
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q4G0N8
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51170
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:O15247
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P14867
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02786
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P21283
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02786
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9NP59
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9P2D8
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q92736
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P48167
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P46098
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q96FT7
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q14802
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02787
HomologyConvert: Multiple homologues found: En:ENSBTAG00000013284;En:ENSBTAG00000013284;
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P51788
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P35523
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P37088
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P31644
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P54710
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q16864
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8N2C7
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P54707
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9H0M0
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q8IZF0
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9GZU1
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q99437
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9BQS7
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q9UNQ0
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P00450
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q93050
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:P02786
HomologyConvert: Homo sapiens to Bos taurus: Original ID = S:Q86UD5
The sodium leak channel non-selective protein NALCN, a nonselective cation channel, forms the background Na+ leak conductance and controls neuronal excitability (Lu et al. 2007). Mice with mutant NALCN have a severely disrupted respiratory rhythm and die within 24 hours of birth. Calcium (Ca2+) influences neuronal excitability via the NALCN:UNC79:UNC80 complex, with high Ca2+ concentrations inhibiting transport of Na+ (Lu et al. 2010).
b24
de7
Intracellular pools of Ca2+ serve as the source for inositol 1,4,5-trisphosphate (IP3) -induced alterations in cytoplasmic free Ca2+. In most human cells Ca2+ is stored in the lumen of the sarco/endoplastic reticulum by ATPases known as SERCAs (ATP2As). In platelets, ATP2As transport Ca2+ into the platelet dense tubular network. ATP2As are P-type ATPases, similar to the plasma membrane Na+ and Ca+-ATPases. Humans have three genes for SERCA pumps; ATP2A1-3. Studies on ATP2A1 suggest that it binds two Ca2+ ions from the cytoplasm and is subsequently phosphorylated at Asp351 before translocating Ca2+ into the SR lumen. There is a counter transport of two or possibly three protons ensuring partial charge balancing.
c88
efa
Cytochrome b reductase 1 not only reduces ferrous iron in the brush-border membrane but also in the airways. It is upregulated on iron starvation. However, its electron donor molecule is still unknown (Oakhill et al, 2007; Turi et al, 2006).
afc
f53
Mitochondrial sodium/hydrogen exchanger 9B2 (SLC9B2, aka NHA2) is ubiquitously expressed and mediates the electrogenic exchange of 1 Na+ (or 1 Li+) for 2 H+ across the inner mitochondrial membrane (Xiang et al. 2007, Taglicht et al. 1993). This transport is thought to play a role in salt homeostasis and pH regulation in humans.
d2c
c50
Human serum urate levels are largely maintained by its reabsorption and secretion in the kidney. Loss of this maintenance can elevate urate levels leading to gout, hypertension, and various cardiovascular diseases. Renal urate reabsorption is controlled via two proximal tubular urate transporters; apical SLC22A12 (URAT1) and basolateral SLC2A9 (URATv1, GLUT9). On the other hand, urate secretion is mediated by the orphan sodium phosphate transporter 4 isoform 2 (SLC17A3, NPT4 isoform 2). It is mainly expressed at the apical side of renal tubules and functions as a voltage-driven urate transporter (Jutabha et al. 2010).<br><br>Genetic variations in SLC17A3 influence the variance in serum uric acid concentrations and define the serum uric acid concentration quantitative trait locus 4 (UAQTL4; MIM:612671). Excess serum urate (hyperuricemia) can lead to the development of gout, characterized by tissue deposition of monosodium urate crystals.
d2b
The potassium-transporting ATPase heterodimer (ATP4A/12A:ATP4B) catalyzes the hydrolysis of ATP coupled with the exchange of H+ and K+ ions across the plasma membrane. It is composed of alpha and beta chains. Two human genes encode the catalytic alpha subunit, ATP4A and ATP12A (Maeda et al, 1990; Grishin et al, 1994). ATP4A is responsible for acid production in the stomach. ATP12A is responsible for potassium absorption in various tissues. One human gene encodes the beta subunit, ATP4B (Ma et al, 1991).
e6a
b10
e64
Amiloride-sensitive sodium channels (SCNNs, aka ENaCs, epithelial Na+ channels, non voltage-gated sodium channels) comprises three subunits (alpha, beta and gamma) and plays an essential role in Na+ and fluid absorption in the kidney, colon and lung. The number of channels at the cell's surface (consequently its function) can be regulated. This is achieved by ubiquitination of SCNN via E3 ubiquitin-protein ligases (NED4L and WPP1) (Staub et al. 2000, Farr et al. 2000). NED4L/WPP1 is found in a signaling complex including Raf1 (RAF proto-oncogene serine/threonine-protein kinase), SGK (serum/glucocorticoid-regulated kinase) and GILZ (glucocorticoid-induced leucine zipper protein, TSC22D3) (Soundararajan et al. 2009). Ubiquitinated SCNN (Ub-SCNN) is targeted for degradation so a lesser number of channels are present at the cell surface, reducing the amount of Na+ absorption. Proline-rich sequences at the C-terminus of SCNNs include the PY motif containing a PPxY sequence. PY motifs bind WW domains of NED4L/WPP1. Protein kinases with no lysine K (WNKs) can activate SCNN activity by interacting non-enzymatically with the signaling complex, specifically SGK although the mechanism is unknown (Heise et al. 2010).
d34
bcd
f63
ae4
Intracellular pools of Ca2+ serve as the source for inositol 1,4,5-trisphosphate (IP3) -induced alterations in cytoplasmic free Ca2+. In most human cells Ca2+ is stored in the lumen of the sarco/endoplastic reticulum by ATPases known as SERCAs (ATP2As). In platelets, ATP2As transport Ca2+ into the platelet dense tubular network. ATP2As are P-type ATPases, similar to the plasma membrane Na+ and Ca+-ATPases. Humans have three genes for SERCA pumps; ATP2A1-3. Studies on ATP2A1 suggest that it binds two Ca2+ ions from the cytoplasm and is subsequently phosphorylated at Asp351 before translocating Ca2+ into the SR lumen. There is a counter transport of two or possibly three protons ensuring partial charge balancing.
c88
efa
Transferrin receptor 1 molecules can be found on the outside of any cell. Transferrin transports two iron ions through the blood and two transferrins bind to a TfR1 dimer (West et al, 2001).
d85
The iron ions that are no longer bound to transferrin are reduced by the metalloreductase STEAP3, an endosomal membrane protein. The electron donor partner of the enzyme is unknown (Ohgami et al, 2005; Ohgami et al, 2006).
a92
c0f
Hephaestin oxidizes ferrous iron after export from duodenal cells to enable its transport via transferrin (Griffiths et al, 2005).
b1c
Acid-sensing ion channels 1, 2, 3 and 5 (ASIC1, 2, 3 and 5, aka amiloride-sensitive cation channels) are homotrimeric, multi-pass membrane proteins which can transport sodium (Na+) when activated by extracellular protons. Members of the ASIC family are sensitive to amiloride and function in neurotransmission. The encoded proteins function in learning, pain transduction, touch sensation, and development of memory and fear. Many neuronal diseases cause acidosis, accompanied by pain and neuronal damage; ASICs can mediate the pathophysiological effects seen in acidiosis (Wang & Xu 2011, Qadri et al. 2012). The diuretic drug amiloride inhibits these channels, resulting in analgesic effects. NSAIDs (Nonsteroidal anti-inflammatory drugs) can also inhibit ASICs to produce analgesia (Voilley et al. 2001). ASICs are also partially permeable to Ca2+, Li+ and K+ (not shown here). ASIC1 and 2 are expressed mostly in brain (Garcia-Anoveros et al. 1997, Price et al. 1996), ASIC3 is strongly expressed in testis (de Weille et al. 1998, Ishibashi & Marumo 1998) and ASIC5 is found mainly in intestine (Schaefer et al. 2000). ASIC4 subunits do not form functional channels and it's activity is unknown. It could play a part in regulating other ASIC activity (Donier et al. 2008).
b5c
f05
b2b
a70
b08
fd5
b99
The glycine receptor (GLR) is a ligand-gated ion channel. It is functional as a heteropentamer, consisting of alpha (GLRA) and beta (GLRB) subunits. With no ligand bound, the receptor complex is closed to chloride ions. Binding of the inhibitory neurotransmitter glycine (Gly) to this receptor complex increases chloride conductance into neurons and thus produces hyperpolarization (inhibition of neuronal firing) (Grenningloh et al. 1990, Nikolic et al. 1998, Handford et al. 1996).
d1e
bfb
a57
The transferrin/receptor complex is internalized as a clathrin-coated vesicle (Willingham et al, 1984; Harding et al, 1983).
f94
ca9
The H+/Cl- exchange transporters CLCN4 (Kawasaki et al. 1999, Zdebik et al. 2008), CLCN5 (Zdebik et al. 2008) and CLCN6 (Neagoe et al. 2010) mediate the exchange of endosomal Cl- for cytosolic H+ across endosomal membranes, contributing to the acidification of endosomes.
bdf
ef1
f27
After about 15 minutes on the cell surface, the equilibrium favors dissociation of transferrin, and the transferrin receptor 1 dimer is available again for binding (Hemadi et al., 2006).
e3a
The GABA(A)-rho receptor (GABRR) is expressed in many areas of the brain, but in contrast to other GABA(A) receptors, has especially high expression in the retina. It is functional as a homopentamer and is permeable to chloride ions when GABA binds to it (Cutting et al. 1991, Cutting et al. 1992, Bailey et al. 1990).
f11
b49
fa2
b57
Acidification of the endosome does not continue further, and the endosome fuses again with the plasma membrane (Willingham et al, 1984; Harding et al, 1983).
ca9
f94
Chloride channel 7 comprises H+/Cl- exchange transporter 7 (CLCN7) and osteopetrosis-associated transmembrane protein 1 (OSTM1) (Leisle et al. 2011). This complex localises to the lysosomal membrane where it mediates the exchange of Cl- and H+ ions, perhaps playing a role in the acidification of the lysosome (Graves et al. 2008).<br><br>Defects in CLCN7 cause osteopetrosis autosomal recessive types 2 and 4 (OPTB2, MIM:166600 and OPTB4, MIM:611490) (Frattini et al. 2003, Pangrazio et al. 2010). Defects in OSTM1 cause osteopetrosis autosomal recessive type 5 (OPTB5, MIM:259720) (Pangrazio et al. 2006).
d7a
dff
b6f
cb7
da2
The primary site for absorption of dietary iron is the duodenum. Ferrous iron (Fe2+) is taken up from the gut lumen across the apical membranes of enterocytes and released into the portal vein circulation across basolateral membranes.<br>The human gene SLC11A2 encodes the divalent cation transporter DCT1 (NRAMP2, Natural resistance-associated macrophage protein 2). NRAMP2 resides on the apical membrane of enterocytes and mediates the uptake of ferrous iron into these cells (Tandy S et al, 2000). DCT1 can also accept a broad range of transition metal ions.
b00
Mucolipin-1 is an iron ion channel specifically expressed in endosome and lysosome membranes. It catalyzes the diffusion of Fe2+ ions into the cytosol (Dong et al, 2008).
bb8
Heme oxygenase (HO) cleaves the heme ring at the alpha-methene bridge to form bilverdin. This reaction forms the only endogenous source of carbon monoxide. HO-1 is inducible and is thought to have an antioxidant role as it's activated in virtually all cell types and by many types of "oxidative stress" (Poss and Tonegawa, 1997). HO-2 is non-inducible.
The primary site for absorption of dietary iron is the duodenum. Ferrous iron (Fe2+) is taken up from the gut lumen across the apical membranes of enterocytes and released into the portal vein circulation across basolateral membranes.<br>The human gene SLC40A1 encodes a metal transporter protein MTP1 (also called ferroportin or IREG1). This protein resides on the basolateral membrane of enterocytes and mediates ferrous iron efflux into the portal vein (Schimanski LM et al, 2005). MTP1 colocalizes with hephaestin (HEPH) which stablizes MTP1 and is necessary for the efflux reaction to occur (Han O and Kim EY, 2007; Chen H et al, 2009). As well as the dudenum, MTP1 is also highly expressed on macrophages (where it mediates iron efflux from the breakdown of haem) and the placenta (where it may mediate the transport of iron from maternal to foetal circulation). It is also expressed in muscle and spleen.
c12
ac7
e2a
The efflux pump ABCG2 can relieve cells from toxic heme concentrations even against a concentration gradient. It is expressed in placenta, liver, and small intestine (Krishnamurthy et al, 2004; Doyle & Ross, 2003; Zhang et al, 2003).
dfb
a33
cce
The GABA(A) receptor (GABR) family belongs to the ligand-gated ion channel superfamily (LGIC). Its endogenous ligand is gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the central nervous system. There are six alpha subunits (GABRA) (Garrett et al. 1988, Schofield et al. 1989, Hadingham et al. 1993, Edenberg et al. 2004, Hadingham et al. 1993, Yang et al. 1995, Wingrove et al. 1992, Hadingham et al. 1996), three beta subunits (GABRB) (Schofield et al. 1989, Hadingham et al. 1993, Wagstaff et al. 1991) and 2 gamma subunits (GABRG) (Khan et al. 1993, Hadingham et al. 1995) characterized. GABA(A) functions as a heteropentamer, the most common structure being 2 alpha subunits, 2 beta subunits and a gamma subunit (2GABRA:2GABRB:GABRG). Upon binding of GABA, this complex conducts chloride ions through its pore, resulting in hyperpolarization of the neuron. This causes an inhibitory effect on neurotransmission by reducing the chances of a successful action potential occurring.
eff
c52
e10
c83
e8d
b4c
eec
f5a
ab9
fa7
b3b
Amiloride-sensitive sodium channels (SCNNs, aka ENaCs, epithelial Na+ channels, non voltage-gated sodium channels) belong to the epithelial Na+ channel/degenerin (ENaC/DEG) protein family and mediate the transport of Na+ (and associated water) through the apical membrane of epithelial cells in kidney, colon and lungs. This makes SCNNs important determinants of systemic blood pressure. The physiological activator for SCNNs is unknown but as they belong in the same family as acid-sensitive ion channels (ASICs, which are mediated by protons), these may also be the activating ligands for SCNNs. SCNNs are probable heterotrimers comprising an alpha (or interchangeable delta subunit), beta and gamma subunit (Horisberger 1998).
e83
Protein tweety homolog 1 (TTYH1) has 5 isoforms. Isoform 3 (Campbell et al. 2000) mediates the Ca+-independent efflux of Cl- across plasma membranes (Suzuki & Mizuno 2004, Suzuki 2006).
f1d
f32
c80
The heme transporter FLVCR is expressed in intestine and liver tissue, but also in developing erythroid cells where it is required to protect them from heme toxicity (Quigley et al, 2004; Rey et al, 2008).
c6f
ea2
MTP1 is also highly expressed on macrophages where it mediates iron efflux from the breakdown of haem.<br>The human gene SLC40A1 encodes a metal transporter protein MTP1 (also called ferroportin or IREG1) (Schimanski LM et al, 2005). MTP1 colocalizes with ceruloplasmin (CP) which stablizes MTP1 and is necessary for the efflux reaction to occur (Texel SJ et al, 2008). Ceruloplasmin also catalyzes the conversion of iron from ferrous (Fe2+) to ferric form (Fe3+), therefore assisting in its transport in the plasma in association with transferrin, which can only carry iron in the ferric state. As well as on macrophages, MTP1 is also highly expressed in the duodenum, placenta (where it may mediate the transport of iron from maternal to foetal circulation), in muscle and the spleen.
e1f
c12
The plasma membrane Ca-ATPases 1-4 (ATP2B1-4, PMCAs) are P-type Ca2+-ATPases regulated by calmodulin. The PMCA also counter-transports a proton. PMCA is important for Ca2+ homeostasis and function.
dd6
bc7
The 5-hydroxytryptamine receptor (HTR3) family are members of the superfamily of ligand-gated ion channels (LGICs). Five receptors (HTR3A-E) form a heteropentamer. Binding of the neurotransmitter 5-hydroxytryptamine (5HT, serotonin) to the HTR3 complex opens the channel, which in turn, leads to an excitatory response in neurons and is permeable to sodium, potassium, and calcium ions (Miyake et al. 1995, Davies et al. 1999, Niesler et al. 2007).
baa
bf6
fa0
The H+/Cl- exchange transporter CLCN3 (Borsani et al. 1995) mediates the exchange of endosomal Cl- for cytosolic H+ across late endosomal membranes, contributing to the acidification of endosomes. The activity of CLCN3 is inferred from experiments in mice (Stobrawa et al. 2001, Hara-Chikuma et al. 2005).
e7d
b5d
c2d
Calcium-activated chloride channels (CaCCs) are ubiquitously expressed and implicated in physiological processes such as sensory transduction, fertilization, epithelial secretion, and smooth muscle contraction. The anoctamin family of transmembrane proteins (ANO, TMEM16) belong to CaCCs and have been shown to transport Cl- ions when activated by intracellular Ca2+ (Galietta 2009, Huang et al. 2012). There are currently 10 members, ANO1-10, all having a similar structure, with eight putative transmembrane domains and cytosolic amino- and carboxy-termini. ANO1 and 2 possess Ca2+ activated Cl- transport activity (Yang et al. 2008, Scudieri et al. 2012) while the remaining members also show some demonstrable activity (Tian et al. 2012).
f4e
d47
c32
Uptake of iron from meat happens in the form of ferriheme, and via the same transporter that is used for folate. The process is more effective than taking up iron ions (Shayeghi M et al, 2005).
d6f
Transferrin is the main transporter of iron in the blood. It can take up two ferric iron ions (Wally et al, 2006).
b63
Calcium (Ca2+) can be mobilised from intracellular stores by the presence of nicotinic acid adenine dinucleotide phosphate (NAADP). Two pore calcium channel proteins 1 and 2 (TPCN1 and 2) are expressed on endosomal (not shown here) and lysosomal membranes and mediate the mobilization of Ca2+ from these organelles when activated by NAADP (Brailoiu et al. 2009, Calcraft et al. 2009).
fdc
dce
When endosomal pH reaches 6,0, protons replace the iron ions in the transferrin/receptor complex (Hemadi et al, 2006).
e3a
Human homologues 2 and 3 (TTYH2 and 3) mediate the efflux of Cl- from cells in response to the increase in intracellular Ca2+ levels (Suzuki & Mizuno 2004, Suzuki 2006).
c80
f1d
Chloride channel proteins 1, 2, Ka and Kb (CLCN1, 2, KA, KB) can mediate Cl- influx across the plasma membrane of almost all cells. CLCN1 is expressed mainly on skeletal muscle where it is involved in the electrical stability of the muscle. CLCN1 is thought to function in a homotetrameric form (Steimeyer et al. 1994). CLCN2 is ubiquitously expressed, playing a role in the regulation of cell volume (Cid et al. 1995, Niemeyer et al. 2009). Defects in CLCN1 cause myotonia congenita, an autosomal dominant disease (MCD aka Thomsen disease, MIM:160800). It is characterized by muscle stiffness due to delayed relaxation, resulting from membrane hyperexcitability (Meyer-Kleine et al. 1995, Steimeyer et al. 1994). Defects in CLCN1 also cause autosomal recessive myotonia congenita (MCR aka Becker disease, MIM:255700) (Koch et al. 1992, Meyer-Kleine et al. 1995), a nondystrophic skeletal muscle disorder characterized by muscle stiffness and an inability of the muscle to relax after voluntary contraction. Becker disease is more common and more severe than Thomsen disease.<br><br>CLCNKA and B (Kieferle et al. 1994) are predominantly expressed in distal nephron segments of the kidney (Takeuchi et al. 1995) and the inner ear (Estevez et al. 2001, Schlingmann et al. 2004). They are tightly associated with their essential beta subunit barttin (BSND), requiring it to be fully functional channels (Fischer et al. 2010, Scholl et al. 2006). These channels bound to BSND are essential for renal Cl- reabsorption (Waldegger & Jentsch 2000) and K+ recycling in the inner ear (Estevez et al. 2001). Defects in CLCNKA and B cause Bartter syndrome type 4B (BS4B; MIM:613090) characterized by impaired salt reabsorption and sensorineural deafness (Schlingmann et al. 2004, Nozu et al. 2008). Defects in BSND cause Bartter syndrome type 4A (BS4A aka infantile Bartter syndrome with sensorineural deafness; MIM:602522) characterized by impaired salt reabsorption in the thick ascending loop of Henle and sensorineural deafness (Birkenhager et al. 2001, Nozu et al. 2008).
c98
b5f
ab5
f42
faf
de6
dfe
ee1
d88
c1e
a85
f43
c91
fd4
The sodium/potassium-transporting ATPase (ATP1A:ATP1B:FXYD) is composed of three subunits - alpha (catalytic part), beta and gamma. The trimer catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane, creating the electrochemical gradient which provides energy for the active transport of various nutrients.<br>Four human genes encode the catalytic alpha subunits, ATP1A1-4 (Kawakami et al, 1986; Shull et al, 1989; Ovchinnikov et al, 1988; Keryanov and Gardner, 2002). Defects in ATP1A2 cause alternating hemiplegia of childhood (AHC) (Swoboda et al, 2004). Another defect in ATP1A2 causes familial hemiplegic migraine type 2 (FHM2) (Vanmolkot et al, 2003). Defects in ATP1A3 are the cause of dystonia type 12 (DYT12) (de Carvalho Aguiar et al, 2004).<br><br>Three human genes encode the non-catalytic beta subunits, ATP1B1-3. The beta subunits are thought to mediate the number of sodium pumps transported to the plasma membrane (Lane et al, 1989; Ruiz et al, 1996; Malik et al, 1996). FXYD proteins belong to a family of small membrane proteins that are auxiliary gamma subunits of Na-K-ATPase. At least six members of this family, FYD1-4, 6 and 7, have been shown to regulate Na-K-ATPase activity (Geering 2006, Choudhury et al. 2007). Defects in FXYD2 are the cause of hypomagnesemia type 2 (HOMG2) (Meij et al, 2000).
f84
a71
ec4
ebc
ed6
ada
cd4
fa5
b78
c0a
ed0
b7e
The human gene ATP7A (MNK) encodes the copper-transporting ATPase 1 (ATP7A, ATPase1, Menkes protein) which is expressed in most tissues except the liver (Vulpe et al, 1993; Chelly et al, 1993). Normally, ATP7A resides on the trans-Golgi membrane (Dierick et al, 1997). When cells are exposed to excessive copper levels, it is rapidly relocalized to the plasma membrane where it functions in copper efflux (Petris and Mercer, 1999). Defects in ATP7A are the cause of Menkes disease (MNKD), an X-linked recessive disorder of copper metabolism characterized by generalized copper deficiency (Ambrosini and Mercer, 1999).
fdd
ca3
af0
f18
a5f
The function of V-type proton pumping ATPases is basically the same as that of F-type ATPases, except that V-ATPases cannot synthesize ATP from the proton motive force, the reverse reaction of pumping. When pumping, ATP hydrolysis drives a 120 degree rotation of the rotor which leads to movement of three protons into the phagosome (Adachi et al. 2007).
d4b
The plasma membrane contains a broad range of lipids making up the bilayer. Aminophospholipids (APLs) such as phosphatidylserine (PS) and phosphatidylethanolamine (PE) are distributed in this bilayer and their arrangement is mediated by the P-type ATPases type IV family (Paulusma and Oude Elferink, 2005).
eaf
Accumulation of calcium into the Golgi apparatus is mediated by sarco(endo)plasmic reticulum calcium-ATPases (SERCAs) and by secretory pathway calcium-ATPases (SPCAs). There are two human genes which encode SPCAs; ATP2C1 and ATP2C2 which encode magnesium-dependent calcium-transporting ATPase type 2C members 1 and 2 (ATP2C1 and 2) respectively (Sudbrak et al, 2000; Vanoevelen et al, 2005). Defects in ATP2C1 are the cause of Hailey-Hailey disease (HHD), an autosomal dominant disease characterized by persistent blisters and erosions of the skin (Hu et al, 2000).
fdb
ded
d7c
The plasma membrane contains a broad range of lipids making up the bilayer. Aminophospholipids such as phosphatidylserine (PS) and phosphatidylethanolamine (PE) are distributed in this bilayer and their arrangement is mediated by the P-type ATPases type IV family (Paulusma and Oude Elferink, 2005).
eaf
Many Cl- channels such as CFTR, ClC, CaCC, and ligand-gated anion channels are permeable to bicarbonate (HCO3-) which is an important anion in the regulation of pH. Many tissues, including retinal pigment epithelium (RPE), utilize HCO3- transporters to mediate transport of HCO3-. Bestrophns 1-4 (BEST1-4, aka vitelliform macular dystrophy proteins) have high permeability to HCO3- (Hu & Hartzell 2008). Defective BEST1 may play a role in macular degeneration in the eye due to impaired HCO3- and Cl- conductance (Hu & Hartzell 2008).
ab4
The sodium/hydrogen exchanger 9B1 (SLC9B1 aka Na+/H+ exchanger like domain containing 1, NHEDC1) is specifically expressed on the plasma membrane of the testis and may be implicated in infertility (Ye et al. 2006). Sodium/hydrogen exchanger 9C2 (SLC9C2), also localized to the plasma membrane, may be involved in pH regulation although this protein has not been fully characterized.
ae5
The microsomal Na+/(PO4)3- transporter isoform 1 (SLC17A3, NPT4 isoform 1) is a member of the anion-cation symporter family. It is expressed in liver, kidney and intestine and may function as a cotransporter of sodium (Na+) and phosphate ((PO4)3- or Pi) across the ER membrane (Melis et al. 2004).
e06
Bestrophins 1-4 (BEST1-4, aka vitelliform macular dystrophy proteins) mediate cytosolic Cl- efflux across plasma membranes. This transport is sensitive to intracellular Ca2+ concentrations (Sun et al. 2002, Tsunenari et al. 2003). Mutations in bestrophins that impair their function are implicated in macular degeneration in the eye. Defects in BEST1 cause vitelliform macular dystrophy (BVMD, Best's disease, MIM:153700), an autosomal dominant form of macular degeneration that usually begins in childhood and is characterized lesions due to abnormal accumulation of lipofuscin within and beneath retinal pigment epithelium (RPE) cells (Marquardt et al. 1998, Petrukhin et al. 1998).
d45
b93
a30
c63
The human gene ATP7B encodes the copper-transporting ATPase 2 (ATP7B, ATPase2, Wilson's protein) which is expressed mainly in the liver, brain and kidneys (Bull et al, 1993). ATP7B resides on the trans-Golgi membrane where it it thought to sequester copper from the cytosol into the golgi (Yang et al, 1997). Defects in ATP7B are the cause of Wilson disease (WD), an autosomal recessive disorder of copper metabolism characterized by the toxic accumulation of copper in a number of organs, particularly the liver and brain (Thomas et al, 1995).
c7c
b45
ac2
Ryanodine receptors (RYRs) are located in the sarcoplasmic reticulum (SR) membrane and mediate the release of Ca2+ from intracellular stores during excitation-contraction (EC) coupling in both cardiac and skeletal muscle. RYRs are the largest known ion channels (>2MDa) and are functional in their homotetrameric forms. There are three mammalian isoforms (RYR1-3); RYR1 is prominent in skeletal muscle (Zorzato et al. 1990), RYR2 in cardiac muscle (Tunwell et al. 1996) and RYR3 is found in the brain (Nakashima et al. 1997). For review see Lanner et al. 2010. The function of RYRs are controlled by intracellular Ca2+-binding proteins calsequestrin 1 and 2 (CASQ1 and 2) and the anchoring proteins triadin (TRDN) and junctin. Together, they make up the Ca2+-release complex. CASQ1 and 2 buffer intra-SR Ca2+ stores in skeletal muscle and cardiac muscle respectively (Fujii et al. 1990, Kim et al. 2007). When Ca2+ concentrations reach 1mM, CASQs polymerize (Kim et al. 2007) and can attach to one end of RYRs, mediated by anchoring proteins TRDN and junctin (Taske et al. 1995). By sequestering Ca2+ ions, CASQs can inhibit RYRs function. For reviews see Beard et al. 2004, Beard et al. 2009a, Beard et al. 2009b.<br><br>A member of the intracellular Cl- channel protein family, CLIC2, has also been determined to inhibit RYR-mediated Ca2+ transport (Board et al. 2004), potentially playing a role in the homeostasis of Ca2+ release from intracellular stores. Inhibition is thought to be via reducing activation of the channels by their primary endogenous cytoplasmic ligands, ATP and Ca2+ (Dulhunty et al. 2005).
fe8
a37
bb4
b60
a7a
e99
e50
def
Ferritin oxidises Fe(II) ions to Fe(III), migrates them to its centre, and collects thousands of them as FeO(OH) in the central mineral core from which they can be later remobilised (Harrison & Arrosio 1996).
bf3
In tissues other than the duodenum, ceruloplasmin oxidizes ferrous iron after it is exported from the cell (Sato et al, 1990).
bd7
The sperm-specific Na+/H+ exchanger SLC9C1 (aka sodium/hydrogen exchanger 10, NHE10) is localized to the flagellar membrane and is involved in pH regulation of spermatozoa required for sperm motility and fertility. The activity of human SLC9C1 is inferred from experiments using mouse Slc9c1 (Wang et al. 2003).
dbf
d2c
c50
iron transport pathway
PW:0000591
Pathway Ontology
18259769
PubMed
Lysosomes in iron metabolism, ageing and apoptosis.
Kurz T, Terman A, Gustafsson B, Brunk UT.
19381358
PubMed
A general map of iron metabolism and tissue-specific subnetworks.
Hower V, Mendes P, Torti FM, Laubenbacher R, Akman S, Shulaev V, Torti SV.
20495089
PubMed
Mitochondrial iron trafficking and the integration of iron metabolism between the mitochondrion and cytosol.
Richardson DR, Lane DJ, Becker EM, Huang ML, Whitnall M, Suryo Rahmanto Y, Sheftel AD, Ponka P.
17686774
PubMed
Intramolecular disulfide bond is a critical check point determining degradative fates of ATP-binding cassette (ABC) transporter ABCG2 protein.
Wakabayashi K, Nakagawa H, Tamura A, Koshiba S, Hoshijima K, Komada M, Ishikawa T.
21040849
PubMed
Extracellular calcium controls background current and neuronal excitability via an UNC79-UNC80-NALCN cation channel complex.
Lu B, Zhang Q, Wang H, Wang Y, Nakayama M, Ren D.
17448995
PubMed
The neuronal channel NALCN contributes resting sodium permeability and is required for normal respiratory rhythm.
Lu B, Su Y, Das S, Liu J, Xia J, Ren D.
2953725
PubMed
Ca2+-activated ATPase in microsomes from human liver.
Spamer C, Heilmann C, Gerok W.
7702581
PubMed
Localization and identification of Ca2+ATPases in highly purified human platelet plasma and intracellular membranes. Evidence that the monoclonal antibody PL/IM 430 recognizes the SERCA 3 Ca2+ATPase in human platelets.
Bokkala S, el-Daher SS, Kakkar VV, Wuytack F, Authi KS.
18194661
PubMed
Functional characterization of human duodenal cytochrome b (Cybrd1): Redox properties in relation to iron and ascorbate metabolism.
Oakhill JS, Marritt SJ, Gareta EG, Cammack R, McKie AT.
16510471
PubMed
Duodenal cytochrome b: a novel ferrireductase in airway epithelial cells.
Turi JL, Wang X, McKie AT, Nozik-Grayck E, Mamo LB, Crissman K, Piantadosi CA, Ghio AJ.
18000046
PubMed
A human Na+/H+ antiporter sharing evolutionary origins with bacterial NhaA may be a candidate gene for essential hypertension.
Xiang M, Feng M, Muend S, Rao R.
8383669
PubMed
Proton-sodium stoichiometry of NhaA, an electrogenic antiporter from Escherichia coli.
Taglicht D, Padan E, Schuldiner S.
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PubMed
Human sodium phosphate transporter 4 (hNPT4/SLC17A3) as a common renal secretory pathway for drugs and urate.
Jutabha P, Anzai N, Kitamura K, Taniguchi A, Kaneko S, Yan K, Yamada H, Shimada H, Kimura T, Katada T, Fukutomi T, Tomita K, Urano W, Yamanaka H, Seki G, Fujita T, Moriyama Y, Yamada A, Uchida S, Wempe MF, Endou H, Sakurai H.
2160952
PubMed
Human gastric (H+ + K+)-ATPase gene. Similarity to (Na+ + K+)-ATPase genes in exon/intron organization but difference in control region.
Maeda M, Oshiman K, Tamura S, Futai M.
8045293
PubMed
Cloning and characterization of the entire cDNA encoded by ATP1AL1--a member of the human Na,K/H,K-ATPase gene family.
Grishin AV, Sverdlov VE, Kostina MB, Modyanov NN.
1656976
PubMed
cDNA cloning of the beta-subunit of the human gastric H,K-ATPase.
Ma JY, Song YH, Sjöstrand SE, Rask L, Mårdh S.
10720933
PubMed
Regulation of the epithelial Na+ channel by Nedd4 and ubiquitination.
Staub O, Abriel H, Plant P, Ishikawa T, Kanelis V, Saleki R, Horisberger JD, Schild L, Rotin D.
10642508
PubMed
Human Nedd4 interacts with the human epithelial Na+ channel: WW3 but not WW1 binds to Na+-channel subunits.
Farr TJ, Coddington-Lawson SJ, Snyder PM, McDonald FJ.
19380724
PubMed
Epithelial sodium channel regulated by differential composition of a signaling complex.
Soundararajan R, Melters D, Shih IC, Wang J, Pearce D.
20525693
PubMed
Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium channel are regulated by multiple with no lysine (WNK) family members.
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11800564
PubMed
Mutational analysis of the transferrin receptor reveals overlapping HFE and transferrin binding sites.
West AP Jr, Giannetti AM, Herr AB, Bennett MJ, Nangiana JS, Pierce JR, Weiner LP, Snow PM, Bjorkman PJ.
16227996
PubMed
Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells.
Ohgami RS, Campagna DR, Greer EL, Antiochos B, McDonald A, Chen J, Sharp JJ, Fujiwara Y, Barker JE, Fleming MD.
16609065
PubMed
The Steap proteins are metalloreductases.
Ohgami RS, Campagna DR, McDonald A, Fleming MD.
16274220
PubMed
Recombinant expression and functional characterization of human hephaestin: a multicopper oxidase with ferroxidase activity.
Griffiths TA, Mauk AG, MacGillivray RT.
9037075
PubMed
BNaC1 and BNaC2 constitute a new family of human neuronal sodium channels related to degenerins and epithelial sodium channels.
GarcÃa-Añoveros J, Derfler B, Neville-Golden J, Hyman BT, Corey DP.
8626462
PubMed
Cloning and expression of a novel human brain Na+ channel.
Price MP, Snyder PM, Welsh MJ.
9571199
PubMed
Molecular cloning of a DEG/ENaC sodium channel cDNA from human testis.
Ishibashi K, Marumo F.
9744806
PubMed
Identification, functional expression and chromosomal localisation of a sustained human proton-gated cation channel.
de Weille JR, Bassilana F, Lazdunski M, Waldmann R.
10767424
PubMed
Molecular cloning, functional expression and chromosomal localization of an amiloride-sensitive Na(+) channel from human small intestine.
Schaefer L, Sakai H, Mattei M, Lazdunski M, Lingueglia E.
11588175
PubMed
Nonsteroid anti-inflammatory drugs inhibit both the activity and the inflammation-induced expression of acid-sensing ion channels in nociceptors.
Voilley N, de Weille J, Mamet J, Lazdunski M.
18662336
PubMed
Regulation of ASIC activity by ASIC4--new insights into ASIC channel function revealed by a yeast two-hybrid assay.
Donier E, Rugiero F, Jacob C, Wood JN.
2155780
PubMed
Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes.
Grenningloh G, Schmieden V, Schofield PR, Seeburg PH, Siddique T, Mohandas TK, Becker CM, Betz H.
9677400
PubMed
The human glycine receptor subunit alpha3. Glra3 gene structure, chromosomal localization, and functional characterization of alternative transcripts.
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8717357
PubMed
The human glycine receptor beta subunit: primary structure, functional characterisation and chromosomal localisation of the human and murine genes.
Handford CA, Lynch JW, Baker E, Webb GC, Ford JH, Sutherland GR, Schofield PR.
6141558
PubMed
Morphologic characterization of the pathway of transferrin endocytosis and recycling in human KB cells.
Willingham MC, Hanover JA, Dickson RB, Pastan I.
6309857
PubMed
Receptor-mediated endocytosis of transferrin and recycling of the transferrin receptor in rat reticulocytes.
Harding C, Heuser J, Stahl P.
20466723
PubMed
The late endosomal ClC-6 mediates proton/chloride countertransport in heterologous plasma membrane expression.
Neagoe I, Stauber T, Fidzinski P, Bergsdorf EY, Jentsch TJ.
18063579
PubMed
Determinants of anion-proton coupling in mammalian endosomal CLC proteins.
Zdebik AA, Zifarelli G, Bergsdorf EY, Soliani P, Scheel O, Jentsch TJ, Pusch M.
10564087
PubMed
Identification of an acid-activated Cl(-) channel from human skeletal muscles.
Kawasaki M, Fukuma T, Yamauchi K, Sakamoto H, Marumo F, Sasaki S.
16564538
PubMed
The mechanism of iron release from the transferrin-receptor 1 adduct.
Hémadi M, Ha-Duong NT, El Hage Chahine JM.
1849271
PubMed
Cloning of the gamma-aminobutyric acid (GABA) rho 1 cDNA: a GABA receptor subunit highly expressed in the retina.
Cutting GR, Lu L, O'Hara BF, Kasch LM, Montrose-Rafizadeh C, Donovan DM, Shimada S, Antonarakis SE, Guggino WB, Uhl GR.
1315307
PubMed
Identification of a putative gamma-aminobutyric acid (GABA) receptor subunit rho2 cDNA and colocalization of the genes encoding rho2 (GABRR2) and rho1 (GABRR1) to human chromosome 6q14-q21 and mouse chromosome 4.
Cutting GR, Curristin S, Zoghbi H, O'Hara B, Seldin MF, Uhl GR.
10542332
PubMed
Genetic linkage and radiation hybrid mapping of the three human GABA(C) receptor rho subunit genes: GABRR1, GABRR2 and GABRR3.
Bailey ME, Albrecht BE, Johnson KJ, Darlison MG.
17398006
PubMed
A single amino acid in the second transmembrane domain of GABA rho receptors regulates channel conductance.
Zhu Y, Ripps H, Qian H.
18449189
PubMed
The Cl-/H+ antiporter ClC-7 is the primary chloride permeation pathway in lysosomes.
Graves AR, Curran PK, Smith CL, Mindell JA.
21527911
PubMed
ClC-7 is a slowly voltage-gated 2Cl(-)/1H(+)-exchanger and requires Ostm1 for transport activity.
Leisle L, Ludwig CF, Wagner FA, Jentsch TJ, Stauber T.
14584882
PubMed
Chloride channel ClCN7 mutations are responsible for severe recessive, dominant, and intermediate osteopetrosis.
Frattini A, Pangrazio A, Susani L, Sobacchi C, Mirolo M, Abinun M, Andolina M, Flanagan A, Horwitz EM, Mihci E, Notarangelo LD, Ramenghi U, Teti A, Van Hove J, Vujic D, Young T, Albertini A, Orchard PJ, Vezzoni P, Villa A.
19953639
PubMed
Molecular and clinical heterogeneity in CLCN7-dependent osteopetrosis: report of 20 novel mutations.
Pangrazio A, Pusch M, Caldana E, Frattini A, Lanino E, Tamhankar PM, Phadke S, Lopez AG, Orchard P, Mihci E, Abinun M, Wright M, Vettenranta K, Bariae I, Melis D, Tezcan I, Baumann C, Locatelli F, Zecca M, Horwitz E, Mansour LS, Van Roij M, Vezzoni P, Villa A, Sobacchi C.
16813530
PubMed
Mutations in OSTM1 (grey lethal) define a particularly severe form of autosomal recessive osteopetrosis with neural involvement.
Pangrazio A, Poliani PL, Megarbane A, Lefranc G, Lanino E, Di Rocco M, Rucci F, Lucchini F, Ravanini M, Facchetti F, Abinun M, Vezzoni P, Villa A, Frattini A.
10625641
PubMed
Nramp2 expression is associated with pH-dependent iron uptake across the apical membrane of human intestinal Caco-2 cells.
Tandy S, Williams M, Leggett A, Lopez-Jimenez M, Dedes M, Ramesh B, Srai SK, Sharp P.
18794901
PubMed
The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel.
Dong XP, Cheng X, Mills E, Delling M, Wang F, Kurz T, Xu H.
15692071
PubMed
In vitro functional analysis of human ferroportin (FPN) and hemochromatosis-associated FPN mutations.
Schimanski LM, Drakesmith H, Merryweather-Clarke AT, Viprakasit V, Edwards JP, Sweetland E, Bastin JM, Cowley D, Chinthammitr Y, Robson KJ, Townsend AR.
17486601
PubMed
Colocalization of ferroportin-1 with hephaestin on the basolateral membrane of human intestinal absorptive cells.
Han O, Kim EY.
19452451
PubMed
Decreased hephaestin expression and activity leads to decreased iron efflux from differentiated Caco2 cells.
Chen H, Attieh ZK, Dang T, Huang G, van der Hee RM, Vulpe C.
15044468
PubMed
The stem cell marker Bcrp/ABCG2 enhances hypoxic cell survival through interactions with heme.
Krishnamurthy P, Ross DD, Nakanishi T, Bailey-Dell K, Zhou S, Mercer KE, Sarkadi B, Sorrentino BP, Schuetz JD.
14576842
PubMed
Multidrug resistance mediated by the breast cancer resistance protein BCRP (ABCG2).
Doyle L, Ross DD.
12958161
PubMed
The expression and functional characterization of ABCG2 in brain endothelial cells and vessels.
Zhang W, Mojsilovic-Petrovic J, Andrade MF, Zhang H, Ball M, Stanimirovic DB.
2847710
PubMed
Isolation of a cDNA clone for the alpha subunit of the human GABA-A receptor.
Garrett KM, Duman RS, Saito N, Blume AJ, Vitek MP, Tallman JF.
2465923
PubMed
Sequence and expression of human GABAA receptor alpha 1 and beta 1 subunits.
Schofield PR, Pritchett DB, Sontheimer H, Kettenmann H, Seeburg PH.
8391122
PubMed
Cloning of cDNA sequences encoding human alpha 2 and alpha 3 gamma-aminobutyric acidA receptor subunits and characterization of the benzodiazepine pharmacology of recombinant alpha 1-, alpha 2-, alpha 3-, and alpha 5-containing human gamma-aminobutyric acidA receptors.
Hadingham KL, Wingrove P, Le Bourdelles B, Palmer KJ, Ragan CI, Whiting PJ.
15024690
PubMed
Variations in GABRA2, encoding the alpha 2 subunit of the GABA(A) receptor, are associated with alcohol dependence and with brain oscillations.
Edenberg HJ, Dick DM, Xuei X, Tian H, Almasy L, Bauer LO, Crowe RR, Goate A, Hesselbrock V, Jones K, Kwon J, Li TK, Nurnberger JI Jr, O'Connor SJ, Reich T, Rice J, Schuckit MA, Porjesz B, Foroud T, Begleiter H.
8719416
PubMed
Cloning and characterization of the human GABAA receptor alpha 4 subunit: identification of a unique diazepam-insensitive binding site.
Yang W, Drewe JA, Lan NC.
1321750
PubMed
Cloning and expression of a cDNA encoding the human GABA-A receptor alpha 5 subunit.
Wingrove P, Hadingham K, Wafford K, Kemp JA, Ragan CI, Whiting P.
8632757
PubMed
Cloning of cDNAs encoding the human gamma-aminobutyric acid type A receptor alpha 6 subunit and characterization of the pharmacology of alpha 6-containing receptors.
Hadingham KL, Garrett EM, Wafford KA, Bain C, Heavens RP, Sirinathsinghji DJ, Whiting PJ.
8264558
PubMed
Role of the beta subunit in determining the pharmacology of human gamma-aminobutyric acid type A receptors.
Hadingham KL, Wingrove PB, Wafford KA, Bain C, Kemp JA, Palmer KJ, Wilson AW, Wilcox AS, Sikela JM, Ragan CI.
1664410
PubMed
The GABAA receptor beta 3 subunit gene: characterization of a human cDNA from chromosome 15q11q13 and mapping to a region of conserved synteny on mouse chromosome 7.
Wagstaff J, Chaillet JR, Lalande M.
8382267
PubMed
Antibodies to the human gamma 2 subunit of the gamma-aminobutyric acidA/benzodiazepine receptor.
Khan ZU, Fernando LP, Escribá P, Busquets X, Mallet J, Miralles CP, Filla M, De Blas AL.
8719414
PubMed
Expression and pharmacology of human GABAA receptors containing gamma 3 subunits.
Hadingham KL, Wafford KA, Thompson SA, Palmer KJ, Whiting PJ.
9719863
PubMed
Amiloride-sensitive Na channels.
Horisberger JD.
16219661
PubMed
The Drosophila tweety family: molecular candidates for large-conductance Ca2+-activated Cl- channels.
Suzuki M.
10950931
PubMed
Human and mouse homologues of the Drosophila melanogaster tweety (tty) gene: a novel gene family encoding predicted transmembrane proteins.
Campbell HD, Kamei M, Claudianos C, Woollatt E, Sutherland GR, Suzuki Y, Hida M, Sugano S, Young IG.
15010458
PubMed
A novel human Cl(-) channel family related to Drosophila flightless locus.
Suzuki M, Mizuno A.
15369674
PubMed
Identification of a human heme exporter that is essential for erythropoiesis.
Quigley JG, Yang Z, Worthington MT, Phillips JD, Sabo KM, Sabath DE, Berg CL, Sassa S, Wood BL, Abkowitz JL.
18815190
PubMed
Enhanced alternative splicing of the FLVCR1 gene in Diamond Blackfan anemia disrupts FLVCR1 expression and function that are critical for erythropoiesis.
Rey MA, Duffy SP, Brown JK, Kennedy JA, Dick JE, Dror Y, Tailor CS.
19021540
PubMed
Ceruloplasmin in neurodegenerative diseases.
Texel SJ, Xu X, Harris ZL.
5961668
PubMed
ATP-dependent Ca++-extrusion from human red cells.
Schatzmann HJ.
2844759
PubMed
Complete primary structure of a human plasma membrane Ca2+ pump.
Verma AK, Filoteo AG, Stanford DR, Wieben ED, Penniston JT, Strehler EE, Fischer R, Heim R, Vogel G, Mathews S.
7565620
PubMed
Molecular cloning of human 5-hydroxytryptamine3 receptor: heterogeneity in distribution and function among species.
Miyake A, Mochizuki S, Takemoto Y, Akuzawa S.
9950429
PubMed
The 5-HT3B subunit is a major determinant of serotonin-receptor function.
Davies PA, Pistis M, Hanna MC, Peters JA, Lambert JJ, Hales TG, Kirkness EF.
17392525
PubMed
Characterization of the novel human serotonin receptor subunits 5-HT3C,5-HT3D, and 5-HT3E.
Niesler B, Walstab J, Combrink S, Möller D, Kapeller J, Rietdorf J, Bönisch H, Göthert M, Rappold G, Brüss M.
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Characterization of a human and murine gene (CLCN3) sharing similarities to voltage-gated chloride channels and to a yeast integral membrane protein.
Borsani G, Rugarli EI, Taglialatela M, Wong C, Ballabio A.
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ClC-3 chloride channels facilitate endosomal acidification and chloride accumulation.
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Disruption of ClC-3, a chloride channel expressed on synaptic vesicles, leads to a loss of the hippocampus.
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The anoctamin family: TMEM16A and TMEM16B as calcium-activated chloride channels.
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TMEM16A confers receptor-activated calcium-dependent chloride conductance.
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Anoctamins are a family of Ca2+-activated Cl- channels.
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Identification of an intestinal heme transporter.
Shayeghi M, Latunde-Dada GO, Oakhill JS, Laftah AH, Takeuchi K, Halliday N, Khan Y, Warley A, McCann FE, Hider RC, Frazer DM, Anderson GJ, Vulpe CD, Simpson RJ, McKie AT.
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The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding.
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Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling.
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NAADP mobilizes calcium from acidic organelles through two-pore channels.
Calcraft PJ, Ruas M, Pan Z, Cheng X, Arredouani A, Hao X, Tang J, Rietdorf K, Teboul L, Chuang KT, Lin P, Xiao R, Wang C, Zhu Y, Lin Y, Wyatt CN, Parrington J, Ma J, Evans AM, Galione A, Zhu MX.
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Voltage-dependent and -independent titration of specific residues accounts for complex gating of a ClC chloride channel by extracellular protons.
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Multimeric structure of ClC-1 chloride channel revealed by mutations in dominant myotonia congenita (Thomsen).
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PubMed
Cloning of a putative human voltage-gated chloride channel (CIC-2) cDNA widely expressed in human tissues.
Cid LP, Montrose-Rafizadeh C, Smith DI, Guggino WB, Cutting GR.
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Spectrum of mutations in the major human skeletal muscle chloride channel gene (CLCN1) leading to myotonia.
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PubMed
The skeletal muscle chloride channel in dominant and recessive human myotonia.
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PubMed
Cloning, tissue distribution, and intrarenal localization of ClC chloride channels in human kidney.
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Barttin activates ClC-K channel function by modulating gating.
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Functional and structural analysis of ClC-K chloride channels involved in renal disease.
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Two highly homologous members of the ClC chloride channel family in both rat and human kidney.
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Barttin is a Cl- channel beta-subunit crucial for renal Cl- reabsorption and inner ear K+ secretion.
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Molecular analysis of digenic inheritance in Bartter syndrome with sensorineural deafness.
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PubMed
Salt wasting and deafness resulting from mutations in two chloride channels.
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Mutation of BSND causes Bartter syndrome with sensorineural deafness and kidney failure.
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Barttin modulates trafficking and function of ClC-K channels.
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Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence.
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Characterization of the human Na,K-ATPase alpha 2 gene and identification of intragenic restriction fragment length polymorphisms.
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Family of human Na+, K+-ATPase genes. Structure of the gene for the catalytic subunit (alpha III-form) and its relationship with structural features of the protein.
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Physical mapping and characterization of the human Na,K-ATPase isoform, ATP1A4.
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Characterization of two genes for the human Na,K-ATPase beta subunit.
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Expression and synthesis of the Na,K-ATPase beta 2 subunit in human retinal pigment epithelium.
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Identification of the mammalian Na,K-ATPase 3 subunit.
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Dominant isolated renal magnesium loss is caused by misrouting of the Na(+),K(+)-ATPase gamma-subunit.
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Alternating hemiplegia of childhood or familial hemiplegic migraine? A novel ATP1A2 mutation.
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Novel mutations in the Na+, K+-ATPase pump gene ATP1A2 associated with familial hemiplegic migraine and benign familial infantile convulsions.
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Mutations in the Na+/K+ -ATPase alpha3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism.
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A genetic association study of chromosome 11q22-24 in two different samples implicates the FXYD6 gene, encoding phosphohippolin, in susceptibility to schizophrenia.
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Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase.
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Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein.
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Immunocytochemical localization of the Menkes copper transport protein (ATP7A) to the trans-Golgi network.
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The Menkes protein (ATP7A; MNK) cycles via the plasma membrane both in basal and elevated extracellular copper using a C-terminal di-leucine endocytic signal.
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Defective copper-induced trafficking and localization of the Menkes protein in patients with mild and copper-treated classical Menkes disease.
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Coupling of rotation and catalysis in F(1)-ATPase revealed by single-molecule imaging and manipulation.
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The type 4 subfamily of P-type ATPases, putative aminophospholipid translocases with a role in human disease.
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Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump.
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Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease.
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The secretory pathway Ca2+/Mn2+-ATPase 2 is a Golgi-localized pump with high affinity for Ca2+ ions.
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Bestrophin Cl- channels are highly permeable to HCO3-.
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Cloning of a novel human NHEDC1 (Na+/H+ exchanger like domain containing 1) gene expressed specifically in testis.
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NPT4, a new microsomal phosphate transporter: mutation analysis in glycogen storage disease type Ic.
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The vitelliform macular dystrophy protein defines a new family of chloride channels.
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Structure-function analysis of the bestrophin family of anion channels.
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Mutations in a novel gene, VMD2, encoding a protein of unknown properties cause juvenile-onset vitelliform macular dystrophy (Best's disease).
Marquardt A, Stöhr H, Passmore LA, Krämer F, Rivera A, Weber BH.
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Identification of the gene responsible for Best macular dystrophy.
Petrukhin K, Koisti MJ, Bakall B, Li W, Xie G, Marknell T, Sandgren O, Forsman K, Holmgren G, Andreasson S, Vujic M, Bergen AA, McGarty-Dugan V, Figueroa D, Austin CP, Metzker ML, Caskey CT, Wadelius C.
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The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene.
Bull PC, Thomas GR, Rommens JM, Forbes JR, Cox DW.
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Two forms of Wilson disease protein produced by alternative splicing are localized in distinct cellular compartments.
Yang XL, Miura N, Kawarada Y, Terada K, Petrukhin K, Gilliam T, Sugiyama T.
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The Wilson disease gene: spectrum of mutations and their consequences.
Thomas GR, Forbes JR, Roberts EA, Walshe JM, Cox DW.
2298749
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Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum.
Zorzato F, Fujii J, Otsu K, Phillips M, Green NM, Lai FA, Meissner G, MacLennan DH.
9395096
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Molecular cloning and characterization of a human brain ryanodine receptor.
Nakashima Y, Nishimura S, Maeda A, Barsoumian EL, Hakamata Y, Nakai J, Allen PD, Imoto K, Kita T.
8809036
PubMed
The human cardiac muscle ryanodine receptor-calcium release channel: identification, primary structure and topological analysis.
Tunwell RE, Wickenden C, Bertrand BM, Shevchenko VI, Walsh MB, Allen PD, Lai FA.
7588753
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Molecular cloning of the cDNA encoding human skeletal muscle triadin and its localisation to chromosome 6q22-6q23.
Taske NL, Eyre HJ, O'Brien RO, Sutherland GR, Denborough MA, Foster PS.
2321095
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Characterization and localization to human chromosome 1 of human fast-twitch skeletal muscle calsequestrin gene.
Fujii J, Willard HF, MacLennan DH.
17881003
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Characterization of human cardiac calsequestrin and its deleterious mutants.
Kim E, Youn B, Kemper L, Campbell C, Milting H, Varsanyi M, Kang C.
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CLIC-2 modulates cardiac ryanodine receptor Ca2+ release channels.
Board PG, Coggan M, Watson S, Gage PW, Dulhunty AF.
15916532
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A recently identified member of the glutathione transferase structural family modifies cardiac RyR2 substate activity, coupled gating and activation by Ca2+ and ATP.
Dulhunty AF, Pouliquin P, Coggan M, Gage PW, Board PG.
8695634
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The ferritins: molecular properties, iron storage function and cellular regulation.
Harrison PM, Arosio P.
2154449
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Detection of multiple forms of human ceruloplasmin. A novel Mr 200,000 form.
Sato M, Schilsky ML, Stockert RJ, Morell AG, Sternlieb I.
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A new sperm-specific Na+/H+ exchanger required for sperm motility and fertility.
Wang D, King SM, Quill TA, Doolittle LK, Garbers DL.