Matrix metalloproteinase peptides: role in diagnosis and therapy

Details Matrix metalloproteinase peptides: role in diagnosis and therapy Matrix metalloproteinase peptides: role in diagnosis and therapy

1990-02-26

1994-01-18

Wax, Robert A.

Chemistry: natural resins or derivatives; peptides or proteins;

Peptides of 3 to 100 amino acid residues

4 to 5 amino acid residues in defined sequence

530300, 530327, 530329, 530324, 435219, 435226, 930250, C07K 1300, C12N 950, A61K 3900

Patent

active

052801063

ABSTRACT:
A family of metalloproteinases exist which cleave extracellular matrix molecules. These metalloproteinases are secreted in a latent inactive form and require activation in order to specifically cleave the preferred substrate. A series of peptides have been prepared based on the complete sequence analysis of type IV procollagenase. Peptide inhibitors were synthesized which correspond to cysteine repeat regions and histidine containing regions; the mechanism of action of these peptides involves inhibition of binding of the enzyme to the substrate. Peptide inhibitors were synthesized which correspond to the peptide cleaved off during activation, and constitute a novel class of metalloproteinase inhibitors. These inhibitors are members of a series of peptides which contain the core amino acid sequence RKPRC or analogs thereof. The cysteine residue is required for activity. Affinity purified antibodies directed against specific peptides can be used to a) detect any general metalloproteinase enzyme with the sequence in part VAAHE or PRCGNPD, and distinguish it from other known members of the metalloproteinase family, b) block functional domains resulting in the inhibition of enzyme activity, and c) distinguish latent from activated forms of the enzyme.

REFERENCES:
patent: 4923818 (1990-05-01), Goldberg et al.
Hoyhtya et al. (Jun., 1988) FEBS Lett. 233(1):109-113.
Knauper et al. (Apr., 1990) Eur. J. Biochem. 189:295-300.
Stetler-Stevenson et al. (Jan., 1989) J. Biol. Chem. 264(3):1353-1356.
Collier et al. (May, 1988) J. Biol. Chem. 263(14):6579-6587.

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