Cleavage of the matricellular protein SPARC by matrix metalloproteinase 3 produces polypeptides that influence angiogenesis (Q24309124)

Matrix metallopeptidase 3

GOA release 2020-03-11

1 reference

negative regulation of angiogenesis

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

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E Helene Sage

1

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May Reed

2

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Sarah E Funk

3

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Thao Truong

4

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Melissa Steadele

5

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Pauli Puolakkainen

6

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Donald H Maurice

7

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James A Bassuk

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

26 September 2003

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published in

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volume

278

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issue

39

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page(s)

37849-57

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cites work

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SPARC, a secreted protein associated with morphogenesis and tissue remodeling, induces expression of metalloproteinases in fibroblasts through a novel extracellular matrix-dependent pathway

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SPARC is a source of copper-binding peptides that stimulate angiogenesis

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Expression of SPARC during development of the chicken chorioallantoic membrane: evidence for regulated proteolysis in vivo

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Expression of biologically active human SPARC in Escherichia coli

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Renaturation of SPARC expressed in Escherichia coli requires isomerization of disulfide bonds for recovery of biological activity

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In vivo stimulation of connective tissue accumulation by the tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ in rat experimental wounds

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Inhibition of endothelial cell proliferation by SPARC is mediated through a Ca(2+)-binding EF-hand sequence

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Immunochemical and tissue analysis of protease generated neoepitopes of BM-40 (osteonectin, SPARC) which are correlated to a higher affinity binding to collagens

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inferred from DOI database lookup

7 January 2021

based on heuristic

The biology of SPARC, a protein that modulates cell-matrix interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M302946200