The interaction of decorin core protein fragments with type I collagen.
To further define the molecular interaction between decorin and type I collagen we generated a 20 kD fragment containing the N-terminal half of the core protein by Endoproteinase Arg C digestion and a 40 kD fragment including all leucine-rich repeats in the central part of decorin core by cleavage with 2-nitro-5-thiocyanobenzoate. The fragments did not influence collagen fibril formation, even at high concentration, and radioactive fragments showed little binding to collagen fibrils. Our observations suggest that neither the N-terminal half nor the central leucine-rich repeats of the decorin core protein can, by itself, interact fully with fibrillar collagen.
Pogány
G
G
Department of Biology, University of New Mexico, Albuquerque 87131.
Vogel
K G
KG
D000818:Animals; D002417:Cattle; D002478:Cells, Cultured; D002852:Chromatography, Ion Exchange; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D058575:Decorin; D016326:Extracellular Matrix Proteins; D005347:Fibroblasts / Q000378:metabolism; D006868:Hydrolysis; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011509:Proteoglycans / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000378:metabolism*; D013710:Tendons / Q000378:metabolism; D013861:Thiocyanates
D058575:Decorin; D016326:Extracellular Matrix Proteins; D010446:Peptide Fragments; D011509:Proteoglycans; D013861:Thiocyanates; D003094:Collagen; C044499:submandibular proteinase A; D012697:Serine Endopeptidases; C008658:2-nitro-5-thiocyanobenzoic acid