Ionic selectivity of the Ca2+/H+ antiport in synaptic vesicles of sheep brain cortex.

Autor: Gonçalves PP; Centro de Biologia Celular, Departamento de Biologia, Universidade de Aveiro, 3810 Aveiro, Portugal. pgoncalves@bio.ua.pt, Meireles SM, Neves P, Vale MG
Jazyk: angličtina
Zdroj: Brain research. Molecular brain research [Brain Res Mol Brain Res] 1999 Apr 20; Vol. 67 (2), pp. 283-91.
DOI: 10.1016/s0169-328x(99)00081-9
Abstrakt: As we previously reported, synaptic vesicles isolated from sheep brain cortex contain a Ca2+/H+ antiport that permits Ca2+ accumulation inside the vesicles ( approximately 5 nmol/mg protein) at expenses of the pH gradient generated by the H+-pumping ATPase. We observed that the system associates Ca2+ influx to H+ release and operates with low affinity for Ca2+. In the present work, we found that Ca2+/H+ antiport mediates exchange of protons with other cations such as Zn2+ and Cd2+, suggesting that these cations and Ca2+ share the same transporter molecules to enter the intravesicular space. Zn2+ and Cd2+ induce H+ release in a concentration-dependent manner (fluorimetrically evaluated) and they inhibit the antiport-mediated Ca2+ uptake by the vesicles (isotopically measured). In contrast, large cations such as Ba2+ and Cs+ do not alter Ca2+ influx and they are unable to induce proton release from the vesicles. With respect to Sr2+, which has an intermediary size relatively to the other groups of cations, we found that it does not induce H+ liberation from the vesicles, but it has a concentration-dependent inhibitory effect on the Ca2+-induced H+ release and Ca2+ uptake by the vesicles. These results indicate that the cation selectivity of the synaptic vesicles Ca2+/H+ antiport is essentially determined by the size of the cation transported into the vesicles.
(Copyright 1999 Elsevier Science B.V.)
Databáze: MEDLINE
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