Adapted from: Genetic mouse models for the functional analysis of the perifibrillar components collagen IX, COMP and matrilin-3: Implications for growth cartilage differentiation and endochondral ossification by Frank Zaucke and Susanne Grässel [https://www.ncbi.nlm.nih.gov/pubmed/19554514]. Model for supramolecular assembly of cartilage fibrils and filaments into fibrillar networks: Matrilin-3 and COMP act as adaptor molecules to interconnect D-periodically banded fibrils with each other and/or with collagen VI beaded filaments to generate a heterotypic fibrillar network. The interaction may be mediated either by matrilin-1 / -3 binding directly to collagen IX or via COMP, which associates with the NC domains of collagen IX. Linked with a dotted arrow to the GeneProduct nodes are diseases caused by mutation in the respective gene.

Authors

Ritchie Lee , Kristina Hanspers , Friederike Ehrhart , Andreas Zankl , and Eric Weitz

Cited In

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Organism

Homo sapiens

Communities

Skeletal Dysplasia

Annotations

Pathway Ontology: disease pathway

Disease Ontology: pseudoachondroplasia

Participants

References

1. Genetic mouse models for the functional analysis of the perifibrillar components collagen IX, COMP and matrilin-3: Implications for growth cartilage differentiation and endochondral ossification. Zaucke F, Grässel S. Histol Histopathol. 2009 Aug;24(8):1067–79. PubMed Europe PMC Scholia