Trp1, a candidate protein for the store-operated Ca2+ influx mechanism in salivary gland cells

Citation
Xb. Liu et al., Trp1, a candidate protein for the store-operated Ca2+ influx mechanism in salivary gland cells, J BIOL CHEM, 275(5), 2000, pp. 3403-3411
Citations number
36
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
275
Issue
5
Year of publication
2000
Pages
3403 - 3411
Database
ISI
SICI code
0021-9258(20000204)275:5<3403:TACPFT>2.0.ZU;2-A
Abstract
The trp gene family has been proposed to encode the store operated Ca2+ inf lux (SOC) channel(s). This study examines the role of Trp1 in the SOC mecha nism of salivary gland cells. htrp1, htrp3, and Trp1 were detected in the h uman submandibular gland cell line (HSG), HSG cells stably transfected with htrp1 alpha cDNA displayed (i) a higher level of Trp1, (ii) a 3-5-fold inc rease in SOC (thapsigargin-stimulated Ca2+ influx), determined by [Ca2+](i) and Ca2+-activated K+ channel current measurements, and (iii) similar basa l Ca2+ permeability, and inhibition of SOC by Gd3+ but not by Zn2+, as comp ared with control cells. importantly, (i) transfection of HSG cells with an tisense trp1 alpha cDNA decreased endogenous Trp1 level and significantly a ttenuated SOC, and (ii) transfection of HSG cells with htrp3 cDNA did not i ncrease SOC, These data demonstrate an association between Trp1 and SOC and strongly suggest that Trp1 is involved in this mechanism in HSG cells, Con sistent with this suggestion, Trp1 was detected in the plasma membrane regi on, the proposed site of SOC, of acinar and ductal cells in intact rat subm andibular glands. Based on these aggregate data, we propose Trp1 as a candi date protein for the SOC mechanism in salivary gland cells.