Potential mechanism for bradykinin-activated and inositol tetrakisphosphate-dependent Ca2+ influx by Ras and GAP1 in fibroblast cells
| Autor: | Haruhiro Higashida, Hiroto Takahashi, Shigeru Yokoyama, Minako Hashii, Megumi Taketo |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Pharmacology
chemistry.chemical_classification Amino Acid Transport Systems G protein Inositol Phosphates Membrane Transport Proteins Bradykinin Tyrosine phosphorylation 3T3 Cells Fibroblasts Cell biology Proto-Oncogene Proteins p21(ras) Mice chemistry.chemical_compound chemistry Biochemistry Second messenger system Animals Humans Phosphorylation Inositol Calcium Signaling Inositol phosphate G protein-coupled receptor |
| Zdroj: | Immunopharmacology. 45:7-11 |
| ISSN: | 0162-3109 |
| DOI: | 10.1016/s0162-3109(99)00051-x |
| Popis: | Here we propose a molecular model for bradykinin receptor-operated and second messenger (inositol-1,3,4,5-tetrakisphosphate)-evoked Ca2+ influx and its potentiation by oncogenic Ras, which is not store-depletion-induced, so-called capacitative, Ca2+ influx. The principal idea for this hypothesis stems from observation that two bradykinin B2 receptor-activated signal pathways, protein tyrosine phosphorylation and formation of inositol tetrakisphosphate, merge during the Ca2+ influx process and that GTPase activating-protein 1 (GAP 1) is inositol tetrakisphosphate binding protein. |
| Databáze: | OpenAIRE |
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