Prostaglandin E1 binding and adenylate cyclase activation in normal and transformed fibroblasts
Autor: | Ira Pastan, Ruth Chabay, Mones Berman, Loren Zech, Peter J.A. Davies |
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Rok vydání: | 1980 |
Předmět: |
Prostaglandins E
Synthetic medicine.medical_specialty Prostaglandin E2 receptor medicine.medical_treatment Biophysics Drug Resistance Adenylate kinase Kidney Biochemistry Cyclase Avian sarcoma virus Cell Line Sarcoma Viruses Murine chemistry.chemical_compound Internal medicine medicine Animals Binding site Receptor Prostaglandin E1 Molecular Biology urogenital system Cell Membrane Fibroblasts equipment and supplies Molecular biology Rats Enzyme Activation Endocrinology Cell Transformation Neoplastic chemistry Avian Sarcoma Viruses lipids (amino acids peptides and proteins) hormones hormone substitutes and hormone antagonists Prostaglandin E Adenylyl Cyclases |
Zdroj: | Biochimica et biophysica acta. 629(2) |
ISSN: | 0006-3002 |
Popis: | The binding of [3H]prostaglandin E1 to membranes of clones of normal rat kidney fibroblasts (NRK cells) has been measured. Cell lines that responded to prostaglandin E1, such as NRK and NRK transformed with Schmitt-Ruppin strain of Rous sarcoma virus (SR-NRK cells), have a high affinity prostaglandin E1 binding site. Murine-sarcoma-virus-transformed lines of NRK cells are unresponsive to prostaglandin E1 and have reduced prostaglandin E1 binding Exposure of cells to prostaglandin E1 results both in decreased prostaglandin E1 responsiveness and reduced prostaglandin E1 binding. Activation of adenylate cyclase is correlated to binding of prostaglandin E1 to receptors in both NRK and SR-NRK cell membranes. Mathematical models suggest that GTP decreases the affinity of hormone for its receptor while increasing the catalytic efficiency of adenylate cyclase, and that aggregates of occupied receptors may play an important role in the activation of adenylate cyclase. |
Databáze: | OpenAIRE |
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