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Title: H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen

Abstract

H-ras transformed human bronchial epithelial cells (TBE-1) secrete a single major extracellular matrix metalloprotease which is not found in the normal parental cells. The enzyme is secreted in a latent form which can be activated to catalyze the cleavage of the basement membrane macromolecule type IV collagen. The substrates in their order of preference are: gelatin, type IV collagen, type V collagen, fibronectin, and type VII collagen; but the enzyme does not cleave the interstitial collagens or laminin. This protease is identical to gelatinase isolated from normal human skin explants, normal human skin fibroblasts, and SV40-transformed human lung fibroblasts. Based on this ability to initiate the degradation of type IV collagen in a pepsin-resistant portion of the molecule, it will be referred to as type IV collagenase. This enzyme is most likely the human analog of type IV collagenase detected in several rodent tumors. Type IV collagenase consists of three domains. Type IV collagenase represents the third member of a newly recognized gene family coding for secreted extracellular matrix metalloproteases, which includes interstitial fibroblast collagenase and stromelysin.

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Washington Univ. School of Medicine, St. Louis, MO (USA)
OSTI Identifier:
6838377
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Biol. Chem.; (United States); Journal Volume: 263:14
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; COLLAGEN; BIODEGRADATION; PEPTIDE HYDROLASES; BIOCHEMISTRY; BRONCHI; CARBON 14 COMPOUNDS; EPITHELIUM; FIBROBLASTS; MAN; ONCOGENES; ONCOGENIC TRANSFORMATIONS; SKIN; ANIMAL CELLS; ANIMAL TISSUES; ANIMALS; BODY; CELL TRANSFORMATIONS; CHEMICAL REACTIONS; CHEMISTRY; CONNECTIVE TISSUE CELLS; DECOMPOSITION; ENZYMES; GENES; HYDROLASES; LABELLED COMPOUNDS; MAMMALS; ORGANIC COMPOUNDS; ORGANS; PRIMATES; PROTEINS; RESPIRATORY SYSTEM; SCLEROPROTEINS; SOMATIC CELLS; TISSUES; VERTEBRATES 550201* -- Biochemistry-- Tracer Techniques

Citation Formats

Collier, I.E., Wilhelm, S.M., Eisen, A.Z., Marmer, B.L., Grant, G.A., Seltzer, J.L., Kronberger, A., He, C., Bauer, E.A., and Goldberg, G.I. H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. United States: N. p., 1988. Web.
Collier, I.E., Wilhelm, S.M., Eisen, A.Z., Marmer, B.L., Grant, G.A., Seltzer, J.L., Kronberger, A., He, C., Bauer, E.A., & Goldberg, G.I. H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen. United States.
Collier, I.E., Wilhelm, S.M., Eisen, A.Z., Marmer, B.L., Grant, G.A., Seltzer, J.L., Kronberger, A., He, C., Bauer, E.A., and Goldberg, G.I. 1988. "H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen". United States. doi:.
@article{osti_6838377,
title = {H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen},
author = {Collier, I.E. and Wilhelm, S.M. and Eisen, A.Z. and Marmer, B.L. and Grant, G.A. and Seltzer, J.L. and Kronberger, A. and He, C. and Bauer, E.A. and Goldberg, G.I.},
abstractNote = {H-ras transformed human bronchial epithelial cells (TBE-1) secrete a single major extracellular matrix metalloprotease which is not found in the normal parental cells. The enzyme is secreted in a latent form which can be activated to catalyze the cleavage of the basement membrane macromolecule type IV collagen. The substrates in their order of preference are: gelatin, type IV collagen, type V collagen, fibronectin, and type VII collagen; but the enzyme does not cleave the interstitial collagens or laminin. This protease is identical to gelatinase isolated from normal human skin explants, normal human skin fibroblasts, and SV40-transformed human lung fibroblasts. Based on this ability to initiate the degradation of type IV collagen in a pepsin-resistant portion of the molecule, it will be referred to as type IV collagenase. This enzyme is most likely the human analog of type IV collagenase detected in several rodent tumors. Type IV collagenase consists of three domains. Type IV collagenase represents the third member of a newly recognized gene family coding for secreted extracellular matrix metalloproteases, which includes interstitial fibroblast collagenase and stromelysin.},
doi = {},
journal = {J. Biol. Chem.; (United States)},
number = ,
volume = 263:14,
place = {United States},
year = 1988,
month = 5
}
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