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J. Biol. Chem., Vol. 263, Issue 14, 6579-6587, 05, 1988
IE Collier, SM Wilhelm, AZ Eisen, BL Marmer, GA Grant, JL Seltzer, A Kronberger, CS He, EA Bauer and GI Goldberg
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 of 72 kDa, 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 its 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, which has
the same molecular mass and has been linked to their metastatic potential.
Type IV collagenase consists of three domains. Two of them, the amino-
terminal domain and the carboxyl-terminal domain, are homologous to
interstitial collagenase and human and rat stromelysin. The middle domain,
of 175 residues, is organized into three 58-residue head-to- tail repeats
which are homologous to the type II motif of the collagen- binding domain
of fibronectin. 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.
H-ras oncogene-transformed human bronchial epithelial cells (TBE-1) secrete a single metalloprotease capable of degrading basement membrane collagen
Division of Dermatology, Washington University School of Medicine, St. Louis, Missouri 63110.
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