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The insider's guide to leukocyte integrin signalling and function
This Review focuses on the integrin lymphocyte function-associated antigen 1 (LFA1), which is expressed by T cells, and explores how disparate signalling pathways synergize to regulate LFA1 activity. Expand
A novel coumarin‐labelled peptide for sensitive continuous assays of the matrix metalloproteinases
In assays of the human matrix metalloproteinases, Mca‐Pro‐ Leu‐Gly‐Leu‐Dpa‐Ala‐Arg‐NH2 is about 50 to 100 times more sensitive than dinitrophenyl‐Pro •Leu •Gly •LeU‐Trp •Ala •d‐Arg •NH2 and continuous assays can be made at enzyme concentrations comparable to those used with macromolecular substrates. Expand
Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of gelatinase B.
It can be concluded that the COOH-terminal domain of progelatinase B is not involved in autolytic or cellular activation and does not affect the catalytic activity of the enzyme, however, COO horticultural domain interactions between active gelatinase B and TIMP-1 significantly enhance the rate of complex formation. Expand
Regulation of Matrix Metalloproteinase Activity a
A program of study of the MMPs and TIMPs was initiated to ascertain the relation between their structure and their function, with particular emphasis on the mechanisms of biological regulation. Expand
Assessment of the role of the fibronectin-like domain of gelatinase A by analysis of a deletion mutant.
Comparison of the rates of association of the tissue inhibitors of metalloproteinase (TIMP)-1 and TIMP-2 and their N-terminal domains to both forms of gelatinase indicated that the fibronectin-like domain plays little role in TIMP binding. Expand
The Specificity of TIMP-2 for Matrix Metalloproteinases Can Be Modified by Single Amino Acid Mutations*
This work demonstrates that it is possible to engineer TIMPs with altered specificity and suggests that this form of protein engineering may be useful in the treatment of diseases such as arthritis and cancer where the selective inhibition of key MMPs is desirable. Expand
The role of the C-terminal domain in collagenase and stromelysin specificity.
Analysis of the ability of the different forms of recombinant enzyme to bind to collagen by ELISA showed that both pro and active stromelysin and N-terminal collagenase bound to collagen equally well, as compared with their pro forms. Expand
The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases.
It is concluded that the C-terminal domain plays an important role in the regulation of gelatinase A by a potential physiological activator and inhibitors. Expand
Tissue inhibitors of matrix metalloendopeptidases.
Human Tissue Inhibitor of Metalloproteinases 3 Interacts with Both the N- and C-terminal Domains of Gelatinases A and B
The isolation of complexes between TIMP-3 and progelatinases A and B on gelatin-agarose demonstrated that TIMp-3 binds to both proenzymes, and the effect of various polyanions on the inhibitory activity of TIMP -3 was analyzed. Expand