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J Biol Chem, Vol. 273, Issue 32, 20168-20174, August 7, 1998

Activation of Phospholipase C-1 via G_q/11 during Calcium Mobilization by Calcitonin Gene-related Peptide

Hicham Drissi, Françoise Lasmoles, Véronique Le Mellay^§, Pierre J. Marie, and Michèle Lieberherr^§

From the  Institut National de la Santé et de la Recherche Médicale, U 349, Hôpital Lariboisière, Paris, and the ^§ Centre National de la Recherche Scientifique, UPR 1524, Jouy-en-Josas, France

Interaction of calcitonin gene-related peptide (CGRP) with its receptors leads to stimulation of adenylyl cyclase and/or phospholipase C (PLC). While regulation of adenylyl cyclase is thought to involve the G-protein G_s, it is not known whether activation of PLC results from coupling the receptor to G_q family proteins or whether subunits released from receptor-activated G_s activate PLC. We used human bone cells OHS-4 bearing CGRP receptors in which CGRP activates only the PLC signaling pathway to determine how CGRP acts. CGRP increased the concentration of intracellular calcium ([Ca²⁺]_i) within 5 s via a Ca²⁺ influx through voltage-gated calcium channels and by mobilizing calcium from the endoplasmic reticulum. The activation of effectors, like PLC coupled to G-proteins, is the early event in the pathway leading to inositol 1,4,5-trisphosphate formation, which is responsible for Ca²⁺ mobilization. Western blotting demonstrated a range of PLC- isoforms (1, 3, 4, but not 2) and G-proteins (G_q/11 and G_s). Only phospholipase C-1 is involved in the mobilization of Ca²⁺ from the endoplasmic reticulum of Fura-2-loaded confluent OHS-4 cells and the formation of inositol 1,4,5-trisphosphate by CGRP; PLC- have no effect. Activation of PLC-1 by CGRP involves the G_q/11 subunit, which is insensitive to pertussis toxin, but not G subunits. We therefore believe that CGRP causes the activation of two separate G-proteins.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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