NDLI: Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.

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Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.

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Specific photoaffinity labeling of two plasma membrane polypeptides with an azido auxin.

Phytochrome induces changes in the immunodetectable level of a wall peroxidase that precede growth changes in maize seedlings.

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Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Goldberg, G. I. Marmer, B. L. Wilhelm, S. Grant, G. A. Eisen, A. Z. He, C. S.
Description	Author Affiliation: Goldberg GI ( Division of Dermatology, Washington University School of Medicine, Saint Louis, MO 63110.);
Abstract	Simian virus 40 (SV40)-transformed human lung fibroblasts secrete both 72-kDa type IV collagenase and a closely related 92-kDa type IV collagenase that was not detected in the parental cell line. The 92-kDa type IV procollagenase purified from these cells exists in a noncovalent complex with the tissue inhibitor of metalloproteases, TIMP. Here we report that the 72-kDa type IV procollagenase purified from HRAS-transformed human bronchial epithelial cells, SV40-transformed lung fibroblasts, and normal skin fibroblasts exists in a stable but noncovalent stoichiometric complex with a 24-kDa inhibitor referred to here as 'TIMP-2.' TIMP-2 is closely related to TIMP, as demonstrated by comparison of the partial amino acid sequence of this protein to that of TIMP, although it does not cross-react with TIMP-specific antibody. The TIMP-2 inhibitor interacts with the 72-kDa type IV collagenase in preference to the 92-kDa type IV collagenase that forms a complex exclusively with TIMP. The 72-kDa type IV collagenase-TIMP-2 complex can be activated with organomercurials to yield a catalytically competent enzyme. Activation occurs concomitantly with autoproteolytic cleavage of the amino terminus of the protein and does not require dissociation of the complex. Both activity and activation of the complex can be completely inhibited by further addition of stoichiometric quantities of purified TIMP-2 or recombinant TIMP.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	86
Language	English
Publisher	National Academy of Sciences
Publisher Date	1989-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Collagenases Glycoproteins Metabolism Metalloendopeptidases Antagonists & Inhibitors Microbial Collagenase Amino Acid Sequence Cell Line Cell Transformation, Viral Chromatography, High Pressure Liquid Enzyme Precursors Isolation & Purification Molecular Sequence Data Molecular Weight Peptide Fragments Simian Virus 40 Genetics Tissue Inhibitor Of Metalloproteinases Trypsin Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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