Present address: Department of Cardiology, Children’s Hospital, Boston, MA 02115, USA.
Mobilization of intracellular calcium stores participates in the rise of [Ca2+]i and the toxic actions of the HIV coat protein GP120
Article first published online: 27 AUG 2008
European Journal of Neuroscience
Volume 11, Issue 4, pages 1167–1178, April 1999
How to Cite
Medina, I., Ghose, S. and Ben-Ari, Y. (1999), Mobilization of intracellular calcium stores participates in the rise of [Ca2+]i and the toxic actions of the HIV coat protein GP120. European Journal of Neuroscience, 11: 1167–1178. doi: 10.1046/j.1460-9568.1999.00550.x
- Issue published online: 27 AUG 2008
- Article first published online: 27 AUG 2008
- Received 14 April 1998, revised 30 September 1998, accepted 2 November 1998
- confocal scanning;
- intracellular stores;
The HIV envelope glycoprotein, GP120, increases intracellular Ca2+ concentration and induces degeneration of human and animal neurons in culture. Using patch-clamp recordings and Ca2+ imaging techniques, we have now examined the contribution of intracellular stores of calcium in the effects of GP120. We report that in rat hippocampal neuronal cultures, GP120 induces a dramatic and persistent increase in [Ca2+]i which is prevented by drugs that either deplete (caffeine, carbachol, thapsigargin) or block (dantrolene) Ca2+ release from intracellular stores. In contrast, N-methyl-d-aspartate (NMDA) receptors or voltage-dependent calcium channels do not participate in these effects, as: (i) the increase in [Ca2+]i was not affected by NMDA receptor antagonists or calcium channel blockers; and (ii) and GP120 did not generate any current in whole-cell recording. Dantrolene, a ryanodine stores inhibitor, also prevented neuronal death induced by GP120. Our results show that the GP120-induced rise in [Ca2+]i originates from intracellular calcium stores, and suggest that intracellular stores of calcium may play a determinant role in the pathological actions of GP120.