Large inhibitor of metalloproteinases (LIMP) contains tissue inhibitor of metalloproteinases (TIMP)-2 bound to 72,000-Mr progelatinase
| Autor: | H F Bigg, Ian M. Clark, Tim E. Cawston, V. A. Curry |
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| Rok vydání: | 1992 |
| Předmět: |
Blotting
Western Connective tissue Matrix metalloproteinase Biochemistry Extracellular matrix medicine Humans Secretion Fibroblast Molecular Biology Cells Cultured Enzyme Precursors Tissue Inhibitor of Metalloproteinase-2 Metalloproteinase biology Metalloendopeptidases Cell Biology Pepsin A Neoplasm Proteins Cell biology medicine.anatomical_structure Gelatinases Cell culture Enzyme inhibitor Chromatography Gel biology.protein Autoradiography Electrophoresis Polyacrylamide Gel Carrier Proteins Research Article |
| Zdroj: | Biochemical Journal. 285:143-147 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2850143 |
| Popis: | Connective-tissue cells in culture produce a family of metalloproteinases which, once activated, can degrade all the components of the extracellular matrix. These potent enzymes are all inhibited by the tissue inhibitor of metalloproteinases (TIMP), and it was thought that this inhibitor was solely responsible for the inhibition of these enzymes within connective tissue. However, other inhibitors have recently been described, including large inhibitor of metalloproteinases (LIMP) present in the culture medium of human foetal lung fibroblasts. Here we show that a large proportion of the inhibitory activity of LIMP consists of 72,000-M(r)-progelatinase bound to TIMP-2, a recently discovered low-M(r) metalloproteinase inhibitor closely related to TIMP. The physiological implications of the secretion of a complex of 72,000-M(r) progelatinase and TIMP-2 are discussed, and the separation of the complex in 6 M-urea is described. |
| Databáze: | OpenAIRE |
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