Establishment and Characterization of 7 New Monoclonal Antibodies to Tissue Inhibitor of Metalloproteinases-1

Tumor Biology ◽  
2005 ◽  
Vol 26 (2) ◽  
pp. 71-80 ◽  
Author(s):  
Nanna Møller Sørensen ◽  
Barry L. Dowell ◽  
Kent D. Stewart ◽  
Vibeke Jensen ◽  
Lise Larsen ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor

Cloning and Characterization of Human Tissue Inhibitor of Metalloproteinases-3

1994 ◽  
Vol 13 (7) ◽  
pp. 711-718 ◽  
Author(s):  
CRAIG G. WILDE ◽  
PHIL R. HAWKINS ◽  
ROGER T. COLEMAN ◽  
WENDY B. LEVINE ◽  
ANGELO M. DELEGEANE ◽  
...  
Keyword(s):  
Human Tissue ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Tissue Inhibitor

scholarly journals The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinases-2 and tissue inhibitor of metalloproteinases-1

1991 ◽  
Vol 278 (1) ◽  
pp. 179-187 ◽  
Author(s):  
R V Ward ◽  
R M Hembry ◽  
J J Reynolds ◽  
G Murphy
Keyword(s):  
Molecular Mass ◽  
Polyclonal Antiserum ◽  
High Molecular Mass ◽  
U937 Cells ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Gingival Fibroblasts ◽  
Tissue Inhibitor ◽  
Lower Molecular Mass ◽  
Inhibitory Activities

Human gingival fibroblasts in culture were shown to secrete a 72 kDa progelatinase, of which a proportion in the medium was found to be complexed with tissue inhibitor of metalloproteinases-2 (TIMP-2). A purification procedure was devised to purify free enzyme and inhibitor. We also describe the purification of both 95 kDa progelatinase bound to TIMP-1 and free 95 kDa progelatinase from the medium of U937 cells. A polyclonal antiserum to TIMP-2 was prepared and it was shown that TIMP-1 and TIMP-2 are antigenically distinct. The ability to form stable complexes and the relative inhibitory activities of TIMP-1 and TIMP-2 towards 95 kDa and 72 kDa gelatinases, collagenase, stromelysins 1 and 2 and punctuated metalloproteinase were determined; only minor differences were found. Complex-formation between TIMP-2 and 72 kDa progelatinase was demonstrated not to reduce the metalloproteinase-inhibitory activity of TIMP-2, a finding that led to the characterization of high-molecular-mass TIMP activity. Competition experiments between progelatinases and active gelatinases for TIMPs indicated that the affinity of TIMPs for progelatinases is weaker than that for active gelatinases. In a study of the effects of TIMP-1 and TIMP-2 on progelatinase self-cleavage we found that both TIMP-1 and TIMP-2 inhibit the conversion of 95 kDa and 72 kDa progelatinases and prostromelysin into lower-molecular-mass forms. TIMP capable of complexing with progelatinase was shown to be no more efficient an inhibitor of gelatinase self-cleavage than TIMP not able to complex with progelatinase.

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