PDGF binds to extracellular matrix proteins (R-HSA-382054) [Homo sapiens]


The long splice version of the PDGF-A chain as well as the COOH-terminal part of the PDGF-B precursor contain C-terminal protein motifs that confer retention of the secreted factors. In both the PDGF A- and B-chains, exon 6 encodes a basic sequence that mediates interaction with components of the extracellular matrix. PDGF binds to various types of collagens, thrombospondin and osteopontin; however, the major component of the matrix involved in PDGF binding is likely to be haparan sulphate. The negatively charged sulfate groups on the disaccharide building blocks of heparan sulfate (HS) polysaccharide chains provide binding sites for positively charged amino acid sequence motifs.
The precursor of the B-chain may be retained in the matrix; after maturation when the COOH-terminal retention sequence has been cleaved off, the molecule may become more diffusible.

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Compartment extracellular region
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Literature References
pubMedId Title Journal Year
10508235 Mechanism of action and in vivo role of platelet-derived growth factor Physiol Rev 1999
8900172 Type I, II, III, IV, V, and VI collagens serve as extracellular ligands for the isoforms of platelet-derived growth factor (AA, BB, and AB) J Biol Chem 1996
1311092 The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors Proc Natl Acad Sci U S A 1992
9334164 Interaction of platelet-derived growth factor with thrombospondin 1 Biochem J 1997
Inferred Entries
Orthologous events