Isolation and characterization of a high molecular weight type IV collagenase isolated from human carcinoma tissue

A proform of high molecular weight type IV collagenase was isolated and purified 1230-fold from human metastatic carcinoma tissue. Like matrix metalloproteinases (MMPs), the enzyme was activated by trypsin and degraded type IV collagen and gelatin at a neutral pH, the activity was inhibited by EDTA...

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Bibliographic Details
Published in:FEBS letters 1993-03, Vol.319 (1), p.35-39
Main Authors: Tsuda, Tomi T., Kodama, Akira, Yamamura, Masaichi, Matsuzaki, Shohei, Tsuda, Michio
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
APMA, 4-aminophenylmercuric acetate
Biological and medical sciences
Collagen - metabolism
Collagenases - chemistry
Collagenases - isolation & purification
Collagenases - metabolism
DTT, dithiothreitol
ECM, extracellular matrix
Edetic Acid - pharmacology
EDTA, ethylenediaminetetraacetic acid
Enzyme Activation - drug effects
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Gelatin - metabolism
Gelatinases
Glycoproteins - pharmacology
High molecular weight type IV collagenase
HPLC, high performance liquid chromatography
Humans
Hydrogen-Ion Concentration
Hydrolases
Liver Neoplasms - enzymology
Liver Neoplasms - secondary
Matrix Metalloproteinase 9
Metalloendopeptidases - chemistry
Metalloendopeptidases - metabolism
Metastatic carcinoma tissue
MMPs, matrix metalloproteinases
Molecular Weight
PAGE, polyacrylamide gel electrophoresis
Pepsin A - isolation & purification
Phenanthrolines - pharmacology
PMSF, phenylmethylsulfonyl fluoride
SDS, sodium dodecyl sulfate
Substrate Specificity
TIMP, tissue inhibitor of metalloproteinases
Tissue Inhibitor of Metalloproteinases
Trypsin - pharmacology
Type IV collagenase
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Summary:A proform of high molecular weight type IV collagenase was isolated and purified 1230-fold from human metastatic carcinoma tissue. Like matrix metalloproteinases (MMPs), the enzyme was activated by trypsin and degraded type IV collagen and gelatin at a neutral pH, the activity was inhibited by EDTA and o-phenanthroline. However, the molecular weight was much higher than MMPs which degraded type IV collagen, gelatinase A (MMP-2; 72 kDa gelatinase/type IV collagenase) (EC 3.4.24.24), gelatinase B (MMP-9; 92 kDa gelatinase/type IV collagenase) (EC 3.4.24.35), stromelysin-1 (MMP-3; 57 kDa) (EC 3.4.24.17) and stromelysin-2 (MMP-10; 57 kDa) (EC 3.4.24.22). The other significant difference from MMPs was that the enzyme was not activated by 4-aminophenylmercuric acetate nor inhibited by TIMP. Taking together these results, this high molecular weight type IV collagenase might be a newly found enzyme different from MMPs or might have the same configuration as MMPs already reported.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(93)80032-P