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Identification of a sequence in the matricellular protein SPARC that interacts with the scavenger receptor stabilin‐1
Author(s) -
Workman Gail,
Sage E. Helene
Publication year - 2011
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.23015
Subject(s) - matricellular protein , scavenger receptor , identification (biology) , microbiology and biotechnology , receptor , sequence (biology) , biology , genetics , biochemistry , extracellular matrix , botany , cholesterol , lipoprotein
SPARC (osteonectin/BM‐40), a secreted matricellular protein that promotes cellular deadhesion and motility in wound healing, carcinogenesis, and inflammation, binds to the scavenger receptor stabilin‐1 in alternatively activated macrophages and undergoes endocytosis and clearance from the extracellular space. Both SPARC and stabilin‐1 are expressed by endothelial cells during inflammation, but their interaction in this context is unknown. We have identified a binding site on SPARC for stabilin‐1 by a solid‐state peptide array coupled with a modified enzyme‐linked immunosorbent assay. A monoclonal antibody that recognizes the identified binding site was also characterized that could be an inhibitor for the SPARC‐stabilin‐1 interaction in macrophages or endothelial cells. J. Cell. Biochem. 112: 1003–1008, 2011. © 2011 Wiley‐Liss, Inc.