Potential mechanism for bradykinin-activated and inositol tetrakisphosphate-dependent Ca2+ influx by Ras and GAP1 in fibroblast cells.
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.
Higashida
H
H
Department of Biophysical Genetics, Kanazawa University Graduate School of Medicine, Japan. haruhiro@med.kanazawa-u.ac.jp
Taketo
M
M
Takahashi
H
H
Yokoyama
S
S
Hashii
M
M
D016475:3T3 Cells; D026905:Amino Acid Transport Systems; D000818:Animals; D001920:Bradykinin / Q000378:metabolism*; D020013:Calcium Signaling / Q000502:physiology*; D005347:Fibroblasts / Q000378:metabolism* / Q000502:physiology; D006801:Humans; D007295:Inositol Phosphates / Q000502:physiology*; D026901:Membrane Transport Proteins / Q000502:physiology*; D051379:Mice; D016283:Proto-Oncogene Proteins p21(ras) / Q000502:physiology*
D026905:Amino Acid Transport Systems; D007295:Inositol Phosphates; D026901:Membrane Transport Proteins; C081655:inositol-1,3,4,5-tetrakisphosphate; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras); D001920:Bradykinin