Captopril inhibits the 72 kDa and 92 kDa matrix metalloproteinases
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چکیده
منابع مشابه
Preferential inhibition of 72- and 92-kDa gelatinases by tissue inhibitor of metalloproteinases-2.
Transformed human fibroblasts secrete two structurally and functionally related inhibitors of matrix metalloproteinases, tissue inhibitor of metalloproteinases (TIMP) 1 and 2. In assays measuring the relative inhibitory capability of TIMP-1 and TIMP-2 against autoactivated 72-kDa gelatinase, which consists of two major active peptides and several inactive fragments, TIMP-2 was more effective th...
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 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 کاملpurification and identification of 72 kda and 15 kda allergens from broussonetia papyrifera pollen.
“broussonetia papyrifera” (chinese mulberry) pollen is an important source of allergens in regions surrounding shanghai, china. to identify and purify major allergens from “b. papyrifera” pollen that reacted with serum antibodies from sensitized patients, “b. papyrifera” pollen was defatted, dried, and extracted proteins were separated using sp cationic exchange or q anionic exchange columns. s...
متن کاملThe structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases. Role of the fibronectin type II-like repeats.
Several matrix metalloproteinases, including the 92-kDa and 72-kDa gelatinases, macrophage metalloelastase (MME), and matrilysin degrade insoluble elastin. Because elastolytically active MME and matrilysin consist only of a catalytic domain (CD), we speculated that the homologous CDs of the 92-kDa and 72-kDa gelatinases would confer their elastolytic activities. In contrast to the MME CD, the 9...
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ژورنال
عنوان ژورنال: Kidney International
سال: 1993
ISSN: 0085-2538
DOI: 10.1038/ki.1993.378