Source:http://linkedlifedata.com/resource/pubmed/id/18443816
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2008-8-20
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pubmed:abstractText |
In this study, we explored the pharmacological and biophysical properties of voltage-activated Ca2+ channels in human chromaffin cells using the perforated-patch configuration of the patch-clamp technique. According to their pharmacological sensitivity to Ca2+ channel blockers, cells could be sorted into two groups of similar size showing the predominance of either N- or P/Q-type Ca2+ channels. R-type Ca2+ channels, blocked by 77% with 20 muM Cd2+ and not affected by 50 muM Ni2+, were detected for the first time in human chromaffin cells. Immunocytochemical experiments revealed an even distribution of alpha (1E) Ca2+ channels in these cells. With regard to their biophysical properties, L- and R-type channels were activated at membrane potentials that were 15-20 mV more negative than P/Q- and N-type channels. Activation time constants showed no variation with voltage for the L-type channels, decreased with increasing potentials for the R- and P/Q-type channels, and displayed a bell shape with a maximum at 0 mV for the N-type channels. R-type channels were also the most inactivated channels. We thus show here that human chromaffin cells possess all the Ca2+ channel types described in neurons, L, N, P/Q, and R channels, but the relative contributions of N and P/Q channels differ among cells. Given that N- and P/Q-type Ca2+ channel types can be differentially modulated, these findings suggest the possibility of cell-specific regulation in human chromaffin cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CACNA1E protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channel Blockers,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels, R-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dopamine beta-Hydroxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylethanolamine...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0031-6768
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
456
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1149-62
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pubmed:meshHeading |
pubmed-meshheading:18443816-Calcium Channel Blockers,
pubmed-meshheading:18443816-Calcium Channels,
pubmed-meshheading:18443816-Calcium Channels, R-Type,
pubmed-meshheading:18443816-Cation Transport Proteins,
pubmed-meshheading:18443816-Cells, Cultured,
pubmed-meshheading:18443816-Chromaffin Cells,
pubmed-meshheading:18443816-Dopamine beta-Hydroxylase,
pubmed-meshheading:18443816-Electrophysiology,
pubmed-meshheading:18443816-Humans,
pubmed-meshheading:18443816-Immunohistochemistry,
pubmed-meshheading:18443816-Patch-Clamp Techniques,
pubmed-meshheading:18443816-Phenylethanolamine N-Methyltransferase
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pubmed:year |
2008
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pubmed:articleTitle |
Pharmacological and biophysical properties of Ca2+ channels and subtype distributions in human adrenal chromaffin cells.
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pubmed:affiliation |
Departamento de Farmacología y Terapéutica, Facultad de Medicina, Universidad Autónoma de Madrid, c/ Arzobispo Morcillo 4, 28029, Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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