Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Collagenase has been purified from the culture medium of a human myometrial smooth muscle cell line, and the properties of the pure enzyme compared to those of collagenase from another human mesenchymal cell, the fibroblast. The smooth muscle collagenase was purified using a new, rapid, and convenient three-step purification procedure consisting of chromatography on iminodiacetate-agarose chelated with zinc and on Cibacron Blue-agarose followed by gel filtration on Ultrogel AcA-44. The resultant pure collagenase is secreted as a zymogen indistinguishable from that of the fibroblast enzyme in molecular weight, amino acid composition, and in the nature of its conversion to active enzyme by trypsin. The amino acid sequence of the two enzymes at the trypsin cleavage site is the same. The two collagenases are also indistinguishable immunologically and display essentially identical kinetic behavior on a variety of collagen substrates. Although the two collagenases appear to be identical proteins, the mechanisms which regulate their production appear to be very different. Glucocorticosteroids, which inhibit collagenase production in human skin fibroblasts are without effect in the uterine smooth muscle cell. In contrast, the smooth muscle cell appears to require a component present in fetal bovine serum in order to produce the enzyme.
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PMID:Purification and characterization of human myometrial smooth muscle collagenase. 283 76

Latent human leukocyte collagenase was isolated to apparent homogeneity by a simple and rapid method. Isolation was accomplished by gel filtration on Sepharose 6B and ion exchange chromatography on QAE Sephadex A-50 followed by affinity chromatography on Cibacron Blue Sepharose. The purified latent enzyme exhibits an apparent molecular weight of 70 kD as estimated by SDS-polyacrylamide gel electrophoresis. Reduction with dithiothreitol does not change the mobility of the latent human leukocyte collagenase on SDS-polyacrylamide gel electrophoresis, indicating that the enzyme consists of a single polypeptide chain. The enzyme could be activated by trypsin and thiol reagents such as phenylmercuric chloride and N-ethylmaleimide. Upon activation by trypsin a 54 kD polypeptide was formed from the 70 kD latent enzyme. Concomitant with the activation by thiol reagents, no loss of molecular weight was detected. Inactivated trypsin, i.e. phenylmethyl sulfonyl-trypsin or soybean trypsin inhibitor treated trypsin, was not able to activate latent human leukocyte collagenase. The results support the concept that latent human leukocyte collagenase exists as a proenzyme and thiol-dependent activation occurs through conformational perturbation in the proenzyme molecule.
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PMID:Activation of latent collagenase purified from human leukocytes. 303 86