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The interaction causes a conformational change in the structure of the protein that leads to the opening of the channel pore and subsequent ion flux across the plasma membrane. Most ROCs are permeable to Ca and represent an important mechanism for the generation of second messengers.

L-type Ca channels is observed with neuronal aging (Thibault and Landfield, 1996) and their expression is increased in hippocampi of patients with Alzheimer’s disease (AD) compared to healthy subjects (Coon et al., 1999). Pubmed Abstract | Pubmed Full Text | Cross Ref Full Text Contractor, A., Swanson, G., and Heinemann, S.

The interaction occurs at a specific site, synprint, in the large intracellular loop connecting domains II and III of the α1 subunit of Ca then binds to synaptotagmin and the SNARE complex, resulting in the fusion of the vesicular membrane with the plasma membrane, and release of the neurotransmitter (Catterall and Few, 2008).

Inhibition of presynaptic P/Q-types and N-type currents with reduction of neurotransmitter release is typically produced by a positive shift in the voltage dependence and a slowing of channel activation (Bean, 1989). A hippocampal Glu R5 kainate receptor regulating inhibitory synaptic transmission. Pubmed Abstract | Pubmed Full Text | Cross Ref Full Text Collingridge, G.

In young neurons, sustained depolarization or activation of NMDA receptors reduces L-type Ca1.2 channels trough a dynamin-dependent endocytosis mechanism, protecting the neurons from excitotoxic cell death (Green et al., 2007).

It is thus possible that some of the impairments observed in neurons in aging and degenerative disorders are due to an altered regulation of Ca2 channels directly interact with the SNARE complex, formed by the vesicle-associated-v-SNARE protein synaptobrevin (VAMP/synaptobrevin) and two plasma-membrane-associated t-SNARE proteins, SNAP-25 and syntaxin-1 (Bajjalieh and Scheller, 1995; Sudhof, 2004).

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