Human skin fibroblast stromelysin: structure, glycosylation, substrate specificity, and differential expression in normal and tumorigenic cells
Journal Article
·
· Proc. Natl. Acad. Sci. U.S.A.; (United States)
The authors have purified and determined the complete primary structure of human stromelysin, a secreted metalloprotease with a wide range of substrate specificities. Human stromelysin is synthesized in a preproenzyme form with a calculated size of 53,977 Da and a 17-amino acid long signal peptide. Prostromelysin is secreted in two forms, with apparent molecular masses on NaDodSO/sub 4//PAGE of 60 and 57 kDa. Human stromelysin is capable of degrading proteoglycan, fibronectin, laminin, and type IV collagen but not interstitial type I collagen. The enzyme is not capable of activating purified human fibroblast procollagenase. Analysis of its primary structure shows that stromelysin is in all likelihood the human analog of rat transin, which is an oncogene transformation-induced protease. The pattern of enzyme expression in normal and tumorigenic cells revealed that human skin fibroblasts in vitro secrete stromelysin constitutively. Human fetal lung fibroblasts transformed with simian virus 40, human bronchial epithelial cells transformed with the ras oncogene, fibrosarcoma cells (HT-1080), and a melanoma cell strain (A 2058), do not express this protease nor can the enzyme be induced in these cells by treatment with phorbol 12-myristate 13-acetate. The data indicate that the expression and the possible involvement of secreted metalloproteases in tumorigenesis result from a specific interaction between the transforming factor and the target cell, which may vary in different species.
- Research Organization:
- Washington Univ. School of Medicine, St. Louis, MO (USA)
- OSTI ID:
- 7242245
- Journal Information:
- Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 84:19; ISSN PNASA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ALDEHYDES
AMINO ACID SEQUENCE
AMINO ACIDS
ANIMAL CELLS
ANIMALS
AUTORADIOGRAPHY
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
CARBOHYDRATES
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
CLONING
CONNECTIVE TISSUE CELLS
DAYS LIVING RADIOISOTOPES
DNA
DNA-CLONING
DRUGS
ELECTROPHORESIS
ENZYMES
EVEN-ODD NUCLEI
FIBROBLASTS
HEXOSES
HYDROLASES
ISOTOPES
LABELLED COMPOUNDS
LEUCINE
LIGHT NUCLEI
LIPOTROPIC FACTORS
MAMMALS
MAN
MANNOSE
METHIONINE
MOLECULAR STRUCTURE
MONOSACCHARIDES
NUCLEI
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
ORGANS
PEPTIDE HYDROLASES
PRIMATES
PURIFICATION
RADIOISOTOPES
RECOMBINANT DNA
SACCHARIDES
SKIN
SOMATIC CELLS
SULFUR 35
SULFUR ISOTOPES
TRITIUM COMPOUNDS
TUMOR CELLS
VERTEBRATES
59 BASIC BIOLOGICAL SCIENCES
ALDEHYDES
AMINO ACID SEQUENCE
AMINO ACIDS
ANIMAL CELLS
ANIMALS
AUTORADIOGRAPHY
BETA DECAY RADIOISOTOPES
BETA-MINUS DECAY RADIOISOTOPES
BODY
CARBOHYDRATES
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
CLONING
CONNECTIVE TISSUE CELLS
DAYS LIVING RADIOISOTOPES
DNA
DNA-CLONING
DRUGS
ELECTROPHORESIS
ENZYMES
EVEN-ODD NUCLEI
FIBROBLASTS
HEXOSES
HYDROLASES
ISOTOPES
LABELLED COMPOUNDS
LEUCINE
LIGHT NUCLEI
LIPOTROPIC FACTORS
MAMMALS
MAN
MANNOSE
METHIONINE
MOLECULAR STRUCTURE
MONOSACCHARIDES
NUCLEI
NUCLEIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC SULFUR COMPOUNDS
ORGANS
PEPTIDE HYDROLASES
PRIMATES
PURIFICATION
RADIOISOTOPES
RECOMBINANT DNA
SACCHARIDES
SKIN
SOMATIC CELLS
SULFUR 35
SULFUR ISOTOPES
TRITIUM COMPOUNDS
TUMOR CELLS
VERTEBRATES