The influence of monovalent cations on trimeric G protein Gi1alfa activity in HEK293 cells stably expressing DOR-Gi1alfa (Cys351-Ile351) fusion protein

0370263 - FGÚ 2012 RIV CZ eng J - Journal Article
Vošahlíková, Miroslava - Svoboda, Petr
The influence of monovalent cations on trimeric G protein Gi1alfa activity in HEK293 cells stably expressing DOR-Gi1alfa (Cys351-Ile351) fusion protein.
Physiological Research. Roč. 60, č. 3 (2011), s. 541-547. ISSN 0862-8408. E-ISSN 1802-9973
R&D Projects: GA AV ČR(CZ) IAA500110606; GA MŠMT(CZ) LC554; GA ČR(CZ) GD305/08/H037
Institutional research plan: CEZ:AV0Z50110509
Keywords : delta-opioid receptor (DOR) * monovalent ions * G(i)1alfa protein
Subject RIV: CE - Biochemistry
Impact factor: 1.555, year: 2011

The effect of monovalent cations on trimeric G protein Gi1alfa was measured at equimolar concentration of chloride anion in pertussis-toxin (PTX)-treated HEK293 cells stably expressing PTX-insensitive DOR-Gi1alfa (Cys351-Ile351) fusion protein by high-affinity [35S]GTPgamaS binding assay. The high basal level of binding was detected in absence of DOR agonist and monovalent ions and this high level was inhibited with the order of: Naplus je větší než Kplus je větší nez Liplus. The inhibition by monovalent ions was reversed by increasing concentrations of DOR agonist DADLE. The maximum DADLE response was also highest for sodium and decreased in the order of: Naplus je větší než Kplus rovná se Liplus. Our data indicate i) an inherently high activity of trimeric G protein Gi1alfa when expressed within DOR-Gi1alfa fusion protein and determined in the absence of monovalent cations, ii) preferential sensitivity of DOR-Gi1alfa to sodium as far as maximum of agonist response is involved
Permanent Link: http://hdl.handle.net/11104/0204113