Decorin collagen binding

Decorin-binding sites for collagen type I are mainly located in. Lumican-binding site Rada et al., 19Svens. Here we have made use of these structural similarities and affinity differences in studies of the collagen binding properties of decorin.

Decorin-binding Sites for Collagen Type I Are Mainly Located in. Platelet adhesion to decorin but not collagen I correlates with the. Decorin consists of a collagen-binding core protein and a. Estimation of the binding force of the collagen molecule-decorin.

Although the general features of the structure of type I collagen have. Decorin-binding sites for collagen type I are mainly located in leucine-rich repeats 4-5. (a) Quantitative RT-PCR of calvarial bone of Pmice for the small leucine-rich proteoglycans decorin (Dcn biglycan (Bgn) and asporin (Aspn).

Decorin - , the free encyclopedia

Overexpression of Decorin by Rat Arterial Smooth Muscle Cells. The binding of collagen by other ECM macromolecules such as decorin. Consequently, we have designed a synthetic peptidoglycan based on decorin, a collagen-binding PG. The 44-kDa core protein of decorin contains long repetitive leucine repeats that are thought to play an important role in the collagen-binding. Key words: collagen fibrillogenesis tendon development decorin biglycan extracellular matrix.

This review will concentrate on decorin s function in collagen fibrillogenesis as determined through the study of mice with a disrupted decorin gene. Asporin competes with decorin for collagen binding, binds calcium. In this role, it promotes muscle hypertrophy by binding with myostatin.

Decorincollagen binding interactions that influence the size. In this study, interactions between decoron (the decorin core protein) and binding sites in the d and e bands of the type I collagen fibril were. Quantification of the binding strength of type i collagen and decorin. Microfibrillar structure of type I collagen in situ Jun 1 2006.

Decorin) bind collagen and it is likely that asporin also shares this property 113. Design of a Synthetic Collagen-Binding Peptidoglycan that. Binding of decorin to collagen would interfere with further lateral. Targeted Disruption of Decorin Leads to Abnormal Collagen Fibril.

This study used a nanomechanical optical tweezer to test the binding strength between collagen and both the protein and GAG sides of decorin. Native and GAG-depleted decorin enhanced the association of snpPLAto collagen types I and VI in a solid-phase binding assay. 2004.) Key Words: extracellular matrix decorin collagen, type I muscle, smooth integrin. Biochemical analysis of collagen binding by invertebrate SPARC and engineered monomeric decorin. We report that mice harboring a targeted disruption of the decorin gene are.

Interactions of the Extracellular Matrix Proteoglycans Decorin and. Biochemical analysis of collagen binding by invertebrate SPARC.

Decorin - , the free encyclopedia Decorin s name is a derivative of both the fact that it decorates collagen type I, and that. Decorin Core Protein (Decoron) Shape Complements Collagen. The decorin binding site of DbpA has been mapped to a conserved peptide motif (EAKVRA ) 17. We have demonstrated that decorin binds collagen type I. Decorin regulates assembly of collagen fibrils and acquisition of.

The role of decorin in collagen fibrillogenesis and skin homeostasis. Decorin Binding by DbpA and B of Borrelia garinii, Borrelia afzelii. Colocalization of the collagen-binding proteoglycans decorin, biglycan, fibromodulin and lumican with different cells in).

Design of a Synthetic Collagen-Binding Peptidoglycan that

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