Ca super(2+) Entry Mediated by Store Depletion, S-Nitrosylation, and TRP3 Channels Comparison of coupling and function

The mechanism for coupling between Ca super(2+) stores and store-operated channels (SOCs) is an important but unresolved question. SOC-mediated Ca super(2+) entry is complex and may reflect more than one type of channel and coupling mechanism. To assess such possible divergence the function and coup...

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Published in:The Journal of biological chemistry 2000-09, Vol.275 (37), p.28562-28568
Main Authors: van Rossum, DB, Patterson, R L, Ma, H T, Gill, D L
Format: Article
Language:English
Subjects:
nitrosylation
Trp3 protein
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Summary:The mechanism for coupling between Ca super(2+) stores and store-operated channels (SOCs) is an important but unresolved question. SOC-mediated Ca super(2+) entry is complex and may reflect more than one type of channel and coupling mechanism. To assess such possible divergence the function and coupling of SOCs was compared with two other distinct yet related Ca super(2+) entry mechanisms. SOC coupling in DDT sub(1)MF-2 smooth muscle cells was prevented by the permeant inositol 1,4,5-trisphosphate (InsP sub(3)) receptor blockers, 2-aminoethoxydiphenyl borate (2-APB) and xestospongin C. In contrast, Ca super(2+) entry induced by S-nitrosylation and potentiated by store depletion (Ma, H-T., Favre, C. J., Patterson, R. L., Stone, M. R., and Gill, D. L. (1999) J. Biol. Chem. 274, 35318-35324) was unaffected by 2-APB, suggesting that this entry mechanism is independent of InsP sub(3) receptors. The cycloalkyl lactamimide, MDL-12,330A (MDL), prevented SOC activation (IC sub(50) 10 mu M) and similarly completely blocked S-nitrosylation-mediated Ca super(2+) entry. Ca super(2+) entry mediated by the TRP3 channel stably expressed in HEK293 cells was activated by phospholipase C-coupled receptors but independent of Ca super(2+) store depletion (Ma, H.-T., Patterson, R. L., van Rossum, D. B., Birnbaumer, L., Mikoshiba, K., and Gill, D. L. (2000) Science 287, 1647- 1651). Receptor-induced TRP3 activation was 2-APB-sensitive and fully blocked by MDL. Direct stimulation of TRP3 channels by the permeant diacylglycerol derivative, 1-oleoyl-2-acetyl-sn-glycerol, was not blocked by 2-APB, but was again prevented by MDL. The results indicate that although the activation and coupling processes for each of the three entry mechanisms are distinct, sensitivity to MDL is a feature shared by all three mechanisms, suggesting there may be a common structural feature in the channels themselves or an associated regulatory component
ISSN:0021-9258