The interaction of decorin core protein fragments with type I collagen
1992; Elsevier BV; Volume: 189; Issue: 1 Linguagem: Inglês
10.1016/0006-291x(92)91539-3
ISSN1090-2104
AutoresGábor Pogány, Kathryn G. Vogel,
Tópico(s)Veterinary Equine Medical Research
ResumoTo 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.
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