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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2010-2-1
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pubmed:abstractText |
Angiocidin, a matrix bound and tumor associated protein, has been shown to inhibit tumor progression and angiogenesis. We previously demonstrated that angiocidin binds to thrombospondin-1 and alpha2beta1 integrin. We now show that angiocidin binds and is a preferred substrate for tissue transglutaminase-2 (tTgase). Angiocidin bound tTgase saturably with a Kd of 26 nM, while an angiocidin deletion mutant missing the matrix binding domain of angiocidin failed to bind tTgase. tTgase colocalized with angiocidin on endothelial cells. tTgase bound anti-angiocidin immunoprecipitates of endothelial cell lysates. Breast cancer cells expressing high levels of tTgase attached to angiocidin immobilized on tissue culture plates. Angiocidin was a preferred substrate for tTgase forming high molecular weight cross-linked multimers when treated with tTgase. Cross-linked angiocidin contained iso-peptide bonds as demonstrated by Western blotting and immunohistochemical colocalization studies using endothelial cells treated with angiocidin. Cross-linked angiocidin inhibited cell migration in contrast to monomeric angiocidin and inhibited localization of fibronectin (FN), a pro-tumorigenic matrix protein, into the extracellular matrix (ECM) of tumor and HUVE cells. Our studies provide an additional explanation for the anti-tumor activity of angiocidin suggesting that cross-linked angiocidin disrupts the tumor ECM making it less permissive for tumor growth.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1096-0945
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2009 Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15-25
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:19931242-Animals,
pubmed-meshheading:19931242-Breast Neoplasms,
pubmed-meshheading:19931242-Carrier Proteins,
pubmed-meshheading:19931242-Cell Adhesion,
pubmed-meshheading:19931242-Cell Line,
pubmed-meshheading:19931242-Cell Movement,
pubmed-meshheading:19931242-Child,
pubmed-meshheading:19931242-Endothelial Cells,
pubmed-meshheading:19931242-Extracellular Matrix,
pubmed-meshheading:19931242-Fibronectins,
pubmed-meshheading:19931242-GTP-Binding Proteins,
pubmed-meshheading:19931242-Gene Deletion,
pubmed-meshheading:19931242-Guinea Pigs,
pubmed-meshheading:19931242-Humans,
pubmed-meshheading:19931242-Neovascularization, Pathologic,
pubmed-meshheading:19931242-Proteasome Endopeptidase Complex,
pubmed-meshheading:19931242-Protein Binding,
pubmed-meshheading:19931242-Recombinant Proteins,
pubmed-meshheading:19931242-Transglutaminases
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pubmed:year |
2010
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pubmed:articleTitle |
The interaction of angiocidin with tissue transglutaminase.
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pubmed:affiliation |
Temple University, Department of Neuroscience, Center for Neurovirology, MERB-7th Floor, 3500 N. Broad Street, Philadelphia, PA 19140, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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