Probably plays a major role in determining the retinal structure as well as in the closure of the neural tube.
Non-collagenous domain 1
May regulate extracellular matrix-dependent motility and morphogenesis of endothelial and non-endothelial cells; the function requires homotrimerization and implicates MAPK signaling.
Endostatin
Potently inhibits endothelial cell proliferation and angiogenesis. May inhibit angiogenesis by binding to the heparan sulfate proteoglycans involved in growth factor signaling (PubMed:9008168). Inhibits VEGFA isoform VEGF165-induced endothelial cell proliferation and migration. Seems to inhibit VEGFA-mediated signaling by blocking the interaction of VEGFA to its receptor KDR/VEGFR2 (PubMed:12029087). Modulates endothelial cell migration in an integrin-dependent manner implicating integrin ITGA5:ITGB1 and to a lesser extent ITGAV:ITGB3 and ITGAV:ITGB5 (PubMed:11158588). May negatively regulate the activity of homotrimeric non-collagenous domain 1 (By similarity).
Prolines at the third position of the tripeptide repeating unit (G-X-Y) of the triple-helical regions are hydroxylated.
Undergoes proteolytic processing by CTSL/cathepsin-L and elastase-like proteases to generate both non-collagenous domain 1 trimers and endostatin monomers (PubMed:10716919). In tissue extracts (brain, skeletal muscle, heart, kidney, testis and liver) predominantly bands of approximately 38 kDa are detected; recombinant non-collagenous domain 1 shows similar mobility. In vitro, several proteolytic cleavage sites in the non-collagenous domain 1 hinge region generating different endostatin-like peptides are reported.
Belongs to the multiplexin collagen family.
Expressed in liver, kidney, lung, skeletal muscle and testis.
Collagen alpha-1(XVIII) chain, Col18a1
Proteins
Cardiovascular
182172Da
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