Proteins and glycosaminoglycans in the intercellular matrix of the human cumulus-oophorus and their effect on conversion of proacrosin to acrosin
| Autor: | D. Cechova, J. Tesarik, V. Vilim, J. Drahorad |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Embryology
Biology Matrix (biology) Glycosaminoglycan Extracellular matrix Endocrinology Ovarian Follicle Humans Polyacrylamide gel electrophoresis Cells Cultured Chromatography High Pressure Liquid Acrosin Enzyme Precursors Activator (genetics) Chondroitin Sulfates Obstetrics and Gynecology Cell Biology Cumulus oophorus Extracellular Matrix Enzyme Activation Reproductive Medicine Biochemistry Proteoglycan Immunology biology.protein Microscopy Electron Scanning Autoradiography Female Proteoglycans |
| Zdroj: | Journal of reproduction and fertility. 93(2) |
| ISSN: | 0022-4251 |
| Popis: | Human cumuli-oophori were cultured in vitro in the presence of radioactive protein and polysaccharide precursors. The time course of the cumulus cell secretion was traced by histoautoradiography. Matrix solubilization, and sodium dodecyl sulphate polyacrylamide gel electrophoresis and high-performance liquid chromatography showed that proteoglycan (Mr greater than 1,700,000) was the main cumulus cell product that was prevailingly deposited in the cumulus intercellular matrix and partly released into the culture medium. It was capable of accelerating the conversion of proacrosin to acrosin and this activity was abolished by enzymatic removal of chondroitin sulphate, the predominant glycosaminoglycan of this proteoglycan fraction. None of the other fractions, including a proteoglycan of Mr 80,000-90,000, containing heparan sulphate, accelerated the conversion of proacrosin to acrosin under the conditions used. The results suggest that chondroitin sulphate is the active component of the high-Mr proacrosin activator of the human cumulus-oophorus. |
| Databáze: | OpenAIRE |
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