Expression Cloning Identifies Transgelin (SM22) as a Novel Repressor of 92-kDa Type IV Collagenase (MMP-9) Expression
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منابع مشابه
Expression cloning identifies transgelin (SM22) as a novel repressor of 92-kDa type IV collagenase (MMP-9) expression.
The 92-kDa gelatinase (MMP-9) expression is prerequisite for tissue remodeling in physiology and cancer. However, there are few known regulators of MMP-9 expression. Using an expression cloning strategy, we identified transgelin (SM22), a 22-25-kDa actin-binding protein localized to the cell membrane and cytoplasm, as a novel regulator of MMP-9 expression. Overexpression of a SM22 cDNA in HT108...
متن کاملExpression cloning of novel regulators of 92 kDa type IV collagenase expression.
Overexpression of the 92 kDa type IV collagenase (MMP-9) contributes to cancer progression. However, to date, there are few known regulators of expression of this metalloproteinase. We employed an expression library comprising 500,000 cDNA clones to screen for novel regulators of MMP-9 expression. HT1080 cells were transiently co-transfected with an MMP-9 promoter-luciferase reporter and pools ...
متن کاملMMP 9 ( matrix metallopeptidase 9 ( gelatinase B , 92 kDa gelatinase , 92 kDa type IV collagenase ) )
MMP-9 is a Zn+2 dependent endopeptidase, synthesized and secreted in monomeric form as zymogen. The structure is almost similar to MMP2, another member of matrixmetalloproteinase family. The nascent form of the protein shows an N-terminal signal sequence ('pre' domain) that directs the protein to the endoplasmic reticulum. The pre domain is followed by a propeptide-'pro' domain that maintains e...
متن کاملMMP 2 ( matrix metallopeptidase 2 ( gelatinase A , 72 kDa gelatinase , 72 kDa type IV collagenase ) .
Description MMP2 is a Zn dependent endopeptidase, synthesized and secreted in zymogen form. The nascent form of the protein shows an N-terminal signal sequence ('pre' domain) that directs the protein to the endoplasmic reticulum. The pre domain is followed by a propeptide'pro' domain that maintains enzyme-latency until cleaved or disrupted, and a catalytic domain that contains the conserved zin...
متن کاملInduction of fibroblast 92 kDa gelatinase/type IV collagenase expression by direct contact with metastatic tumor cells.
Previous studies have correlated release of the 92 kDa type IV collagenase/gelatinase by tumor cells in culture with metastatic potential. We have now demonstrated that the ability of tumor cells that do not express the 92 kDa gelatinase to induce release of this metalloproteinase from normal fibroblasts may also be associated with the metastatic phenotype. A transformed rat embryo cell line, 2...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2006
ISSN: 0021-9258
DOI: 10.1074/jbc.m602703200