Primary structure of the heparin-binding site of type V collagen

• Published in: Biochimica et biophysica acta Vol. 1035; no. 2; pp. 139 - 145
• Main Authors: Yaoi, Yoshihito, Hashimoto, Kahoko, Koitabashi, Hiroyuki, Takahara, Kazuhiko, Ito, Manabu, Kato, Ikunoshin
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 17.08.1990; Elsevier; North-Holland
• Subjects: Amino Acid Sequence; Animals; Binding Sites; Biological and medical sciences; Cattle; Chromatography, Affinity; Chromatography, High Pressure Liquid; Collagen - genetics; Collagen - isolation & purification; Collagen - metabolism; Collagen V; Fundamental and applied biological sciences. Psychology; Heparin - metabolism; Heparin binding site; Humans; Interactions. Associations; Intermolecular phenomena; Molecular biophysics; Molecular Sequence Data; Peptide Fragments - isolation & purification; Peptide Hydrolases; Peptide Mapping; Primary structure; Collagen V; Primary structure; Heparin binding site; Human; Affinity chromatography; Peptide fragment; Collagen; HPLC chromatography; Molecular interaction; Anticoagulant; Binding site; Heparin; Aminoacid sequence
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(90)90108-9

The abilities of collagens, type I, II, III, IV, and V, to bind heparin were examined by heparin-affinity chromatography and binding studies with [ 35S]heparin. At a physiological pH and ionic strength, only type V collagen bound to heparin. Collagens type I and II showed higher affinities than types III and IV for heparin, but did not bind to a heparin column at a physiological ionic strength. The heparin binding site of type V collagen was located in a 30 kDa CNBr fragment of the α 1(V) chain, and the amino acid sequence of this fragment was determined. The 30 kDa fragment contained a cluster of basic amino acid residues, and enzymatic cleavage within this basic domain greatly reduced the heparin-binding activities of the resulting peptides. Thus this basic region is probably teh heparin-binding site of type V collagen.