Literature DB >> 8688414

Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen.

J E Scott1.   

Abstract

The small proteoglycans proteodermatan and proteokeratan sulfates organize collagen fibrils in extracellular matrix [Scott, J. E. (1992) FASEB J. 6, 2639-2645], thus helping to maintain tissue shape. Their interaction with fibrils is probably via the protein. They have been examined by rotary shadowing-electron microscopy, which showed that these leucine-rich-repeat proteins are horseshoe shaped. Morphometry and comparison with polypeptide sequences suggest ways in which decorin could interact with tissue collagen fibrils. It is proposed that decorin is a bidentate ligand attached to two parallel neighboring collagen molecules in the fibril, helping to stabilize fibrils and orient fibrillogenesis.

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Year:  1996        PMID: 8688414     DOI: 10.1021/bi960773t

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  50 in total

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4.  Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties.

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Review 7.  The role of decorin in collagen fibrillogenesis and skin homeostasis.

Authors:  Charles C Reed; Renato V Iozzo
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Review 9.  Decorin interacting network: A comprehensive analysis of decorin-binding partners and their versatile functions.

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