FUNCTION Integral component of basement membranes. Component of the glomerular basement membrane (GBM), responsible for the fixed negative electrostatic membrane charge, and which provides a barrier which is both size- and charge-selective. It serves as an attachment substrate for cells. Plays essential roles in vascularization. Critical for normal heart development and for regulating the vascular response to injury. Also required for avascular cartilage development (PubMed:12435733, PubMed:15591058, PubMed:19789387). In muscle, it is essential for localizing acetylcholinesterase (AChE) at the neuromuscular junctions (NMJ), most probably acting as an adapter that links the acetylcholinesterase collagenic tail peptide (COLQ) to alpha-dystroglycan, and is therefore involved in the down-regulation of colinergic synaptic transmission (By similarity).FUNCTION Anti-angiogenic and anti-tumor peptide that inhibits endothelial cell migration, collagen-induced endothelial tube morphogenesis and blood vessel growth in the chorioallantoic membrane. Blocks endothelial cell adhesion to fibronectin and type I collagen. Anti-tumor agent in neovascularization. Interaction with its ligand, integrin alpha2/beta1, is required for the anti-angiogenic properties. Evokes a reduction in phosphorylation of receptor tyrosine kinases via alpha2/beta1 integrin-mediated activation of the tyrosine phosphatase, PTPN6.FUNCTION Has anti-angiogenic properties that require binding of calcium ions for full activity.SUBUNIT Has a strong tendency to aggregate in dimers or stellate structures. Interacts with other basement membrane components such as laminin, prolargin and collagen type IV. Interacts with COL13A1 (PubMed:11956183). Interacts with FGFBP1 (PubMed:11148217). Interacts with VWA1 (By similarity). Interacts (via C-terminus) with ECM1 (via C-terminus) (PubMed:12604605). Interacts with SVEP1 (By similarity). Interacts (via C-terminus) with alpha-dystroglycan; the interaction is required for acetylcholinesterase (AChE) localization at the neuromuscular junctions (NMJ) (By similarity). Interacts with the acetylcholinesterase collagenic tail peptide (COLQ) (PubMed:14702351).INTERACTION Detected in cerebrospinal fluid, fibroblasts and urine (at protein level).PTM Proteolytic processing produces the C-terminal angiogenic peptide, endorepellin. This peptide can be further processed to produce the LG3 peptide.PTM O-glycosylated with core 1 or possibly core 8 glycans. Contains three heparan sulfate chains. Also contains chondroitin sulfate.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS Has been found in the urine of patients with end-stage renal disease and in the amniotic fluid of pregnant women with premature rupture of fetal membranes.ONLINE INFORMATION Perlecan entry
This website requires cookies and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
