Artigo Revisado por pares

Molecular Mechanisms for the Activation of Voltage-Independent Ca 2+ Channels by Endothelin-1 in Chinese Hamster Ovary Cells Stably Expressing Human Endothelin A Receptors

2002; American Society for Pharmacology and Experimental Therapeutics; Volume: 62; Issue: 1 Linguagem: Inglês

10.1124/mol.62.1.75

ISSN

1521-0111

Autores

Yoshifumi Kawanabe, Yasuo Okamoto, Soichi Miwa, Nobuo Hashimoto, Tomoh Masaki,

Tópico(s)

Receptor Mechanisms and Signaling

Resumo

We demonstrated recently that in Chinese hamster ovary cells stably expressing human recombinant endothelin A receptors (CHO-ET A R), endothelin-1 (ET-1) activates two types of Ca 2+ -permeable nonselective cation channels (designated NSCC-1 and NSCC-2) and a store-operated Ca 2+ channel (SOCC), which can be distinguished by Ca 2+ channel blockers such as 1-{β-[3-(4-methoxyphenyl)propoxy]-4-methoxyphenylethyl}-1 H -imidazole hydrochloride (SK&F 96365) and ( R , S )-(3,4-dihydro-6,7-dimethoxy-isochinolin-1-yl)-2-phenyl- N , N -di[2-(2,3,4-trimethoxyphenyl)ethyl]acetamid mesylate (LOE 908). We also reported that CHO-ET A R couples with G 12 in addition to G q and G s . The purpose of the present study was to identify the G proteins involved in the activation of these Ca 2+ channels by ET-1, using mutated ET A Rs with coupling to either G q or G s /G 12 (designated ET A RΔ385 and SerET A R, respectively) and a dominant-negative mutant of G 12 (G 12 G228A). ET A RΔ385 is truncated immediately downstream of Cys 385 in the C terminus as palmitoylation sites, whereas SerET A R is unpalmitoylated because of substitution of all the cysteine residues to serine (Cys 383 Cys 385–388 → Ser 383 Ser 385–388 ). In CHO-ET A RΔ385, stimulation with ET-1 activated only SOCC. In CHO-SerET A R or CHO-ET A R pretreated withU73122, an inhibitor of phospholipase C (PLC), ET-1 activated only NSCC-1. Dibutyryl cAMP alone did not activate any Ca 2+ channels in the resting and ET-1–stimulated CHO-SerET A R. Microinjection of G 12 G228A abolished the activation of NSCC-1 and NSCC-2 in CHO-ET A R and that of NSCC-1 in CHO-SerET A R. These results indicate that ET A R activates three types of Ca 2+ channels via different G protein-related pathways. NSCC-1 is activated via a G 12 -dependent pathway, NSCC-2 via G q /PLC- and G 12 -dependent pathways, and SOCC via a G q /PLC-dependent pathway.

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