Phage Display of Tissue Inhibitor of Metalloproteinases-2 (TIMP-2)
نویسندگان
چکیده
منابع مشابه
Phage display of tissue inhibitor of metalloproteinases-2 (TIMP-2): identification of selective inhibitors of collagenase-1 (metalloproteinase 1 (MMP-1)).
Tissue inhibitor of metalloproteinases-2 (TIMP-2) is a broad spectrum inhibitor of the matrix metalloproteinases (MMPs), which function in extracellular matrix catabolism. Here, phage display was used to identify variants of human TIMP-2 that are selective inhibitors of human MMP-1, a collagenase whose unregulated action is linked to cancer, arthritis, and fibrosis. Using hard randomization of ...
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UNLABELLED Metalloproteinases are the proteolytic enzymes that digest components of the extracellular matrix in many physiological and pathological conditions. Their activity is regulated by their natural inhibitors: non-specific alpha2-macroglobulin and specific tissue inhibitors of metalloproteinases (TIMP). There are four TIMPs. TIMP-2 is the only enzyme that is expressed in constitutive man...
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The extensive remodelling of the human endometrium throughout the menstrual cycle is accompanied by changes in production of matrix metalloproteinases, the activity of which can be inhibited by specific tissue inhibitors or by tissue inhibitors of metalloproteinases (TIMP)s with a 1:1 stoichiometry. This study immunolocalized TIMP-1, TIMP-2 and TIMP-3 in dated normal human endometrium across th...
متن کاملFunctional domains of human TIMP-1 (tissue inhibitor of metalloproteinases).
To define domains of tissue inhibitor of metalloproteinases (TIMP-1) that are important to its ability to inhibit fibroblast-type collagenase (FIB-CL), two different approaches were used: (i) competition with synthetic peptides modeled after the human TIMP-1 sequence and (ii) localization of epitopes of blocking antibodies. TIMP-1 consists of six loops, held in place by six disulfide bonds arra...
متن کاملDisulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP).
Disulphide bonds in human recombinant tissue inhibitor of metalloproteinases (TIMP) were assigned by resolving proteolytic digests of TIMP on reverse-phase h.p.l.c. and sequencing those peaks judged to contain disulphide bonds by virtue of a change in retention time on reduction. This procedure allowed the direct assignment of Cys-145-Cys-166 and the isolation of two other peptides containing t...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2011
ISSN: 0021-9258
DOI: 10.1074/jbc.m111.253328