Matricellular Hevin Regulates Decorin Production and Collagen Assembly

Matricellular proteins such as SPARC, thrombospondin 1 and 2, and tenascin C and X subserve important functions in extracellular matrix synthesis and cellular adhesion to extracellular matrix. By virtue of its reported interaction with collagen I and deadhesive activity on cells, we hypothesized tha...

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Bibliographic Details
Published in:The Journal of biological chemistry 2006-09, Vol.281 (37), p.27621-27632
Main Authors: Sullivan, Millicent M., Barker, Thomas H., Funk, Sarah E., Karchin, Ari, Seo, Neung S., Höök, Magnus, Sanders, Joan, Starcher, Barry, Wight, Thomas N., Puolakkainen, Pauli, Sage, E. Helene
Format: Article
Language:English
Subjects:
Animals
Calcium-Binding Proteins - chemistry
Cell Adhesion
Collagen - chemistry
Decorin
Extracellular Matrix - metabolism
Extracellular Matrix Proteins - chemistry
Fibroblasts - metabolism
Gene Expression Regulation
Humans
Kinetics
Mice
Proteoglycans - chemistry
Skin - metabolism
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Summary:Matricellular proteins such as SPARC, thrombospondin 1 and 2, and tenascin C and X subserve important functions in extracellular matrix synthesis and cellular adhesion to extracellular matrix. By virtue of its reported interaction with collagen I and deadhesive activity on cells, we hypothesized that hevin, a member of the SPARC gene family, regulates dermal extracellular matrix and collagen fibril formation. We present evidence for an altered collagen matrix and levels of the proteoglycan decorin in the normal dermis and dermal wound bed of hevin-null mice. The dermal elastic modulus was also enhanced in hevin-null animals. The levels of decorin protein secreted by hevin-null dermal fibroblasts were increased by exogenous hevin in vitro, data indicating that hevin might regulate both decorin and collagen fibrillogenesis. We also report a decorin-independent function for hevin in collagen fibrillogenesis. In vitro fibrillogenesis assays indicated that hevin enhanced fibril formation kinetics. Furthermore, cell adhesion assays indicated that cells adhered differently to collagen fibrils formed in the presence of hevin. Our observations support the capacity of hevin to modulate the structure of dermal extracellular matrix, specifically by its regulation of decorin levels and collagen fibril assembly.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M510507200