4.6 Article

Identification of a Sequence in the Matricellular Protein SPARC That Interacts With the Scavenger Receptor Stabilin-1

Journal

JOURNAL OF CELLULAR BIOCHEMISTRY
Volume 112, Issue 4, Pages 1003-1008

Publisher

WILEY-BLACKWELL
DOI: 10.1002/jcb.23015

Keywords

VASCULAR PERMEABILITY; ALTERNATIVELY ACTIVATED MACROPHAGES; PEPTIDE ARRAY; EPITOPE; OSTEONECTIN; EXTRACELLULAR MATRIX

Funding

  1. NIH/National Institute of General Medical Sciences [R01 GM40711]
  2. National Institutes of Health [GM40711]

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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. (C) 2011 Wiley-Liss, Inc.

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