Effect of temperature and divalent cations on the substratum attachment of rat hepatocytes in vitro
| Autor: | R. Gjessing, P.O. Seglen |
|---|---|
| Rok vydání: | 1978 |
| Předmět: |
Male
Cycloheximide Biology Divalent chemistry.chemical_compound medicine Cell Adhesion Animals Magnesium Cytochalasin B Cells Cultured chemistry.chemical_classification Dose-Response Relationship Drug Temperature Cell Biology Blood Proteins Trypsin Arrhenius plot Rats Enzyme chemistry Biochemistry Liver Collagenase Biophysics biology.protein Microscopy Electron Scanning Calcium Neuraminidase medicine.drug |
| Zdroj: | Journal of cell science. 34 |
| ISSN: | 0021-9533 |
| Popis: | The attachment of rat hepatocytes to polystyrene-adsorbed serum protein is relatively insensitive to inhibitors such as dextran sulphate, cycloheximide, colchicine and cytochalasin B, and enzymes like trypsin and neuraminidase, but it is strongly dependent on divalent cations. Mg2+ supports attachment better than Ca2+, but a combination of both is required for maximal attachment. The attachment is very temperature-sensitive, with a biphasic Arrhenius plot indicating an activation energy of 123 kJ/mol above 34 °C and 374 kJ/mol below 34 °C. The adsorbed attachment-promoting serum factor is inactivated by trypsin, or by Ca2+-dependent proteases which contaminate commercial preparations of collagenase. The adsorbed factor is resistant to treatment with glutaraldehyde, neuraminidase and heating to 90 °C, whereas the same factor in the unadsorbed state (in serum) is destroyed by heating to 70 °C. The factor in serum is unable to compete with the adsorbed factor for cell binding, hence it would appear that adsorption to polystyrene induces the active, heat-resistant conformation of the factor. |
| Databáze: | OpenAIRE |
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