From worm to man: three subfamilies of TRP channels
A steadily increasing number of cDNAs for proteins that are structurally related to the TRP ion channels have been cloned in recent years. All these proteins display a topology of six transmembrane segments that is shared with some voltage-gated channels and the cyclic-nucleotide-gated channels. The...
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Published in: | Trends in Neurosciences Vol. 23; no. 4; pp. 159 - 166 |
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Main Authors: | , , |
Format: | Book Review Journal Article |
Language: | English |
Published: |
Oxford
Elsevier Ltd
01-04-2000
Elsevier Science Elsevier Sequoia S.A |
Subjects: | |
Online Access: | Get full text |
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Summary: | A steadily increasing number of cDNAs for proteins that are structurally related to the TRP ion channels have been cloned in recent years. All these proteins display a topology of six transmembrane segments that is shared with some voltage-gated channels and the cyclic-nucleotide-gated channels. The TRP channels can be divided, on the basis of their homology, into three TRP channel (TRPC) subfamilies: short (S), long (L) and osm (O). From the evidence available to date, this subdivision can also be made according to channel function. Thus, the STRPC family, which includes
Drosophila TRP and TRPL and the mammalian homologues, TRPC1-7, is a family of Ca
2+-permeable cation channels that are activated subsequent to receptor-mediated stimulation of different isoforms of phospholipase C. Members of the OTRPC family are Ca
2+-permeable channels involved in pain transduction (vanilloid and vanilloid-like receptors), epithelial Ca
2+ transport and, at least in
Caenorhabditis elegans, in chemo-, mechano- and osmoregulation. The LTRPC family is less well characterized. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 ObjectType-Feature-3 ObjectType-Review-1 |
ISSN: | 0166-2236 1878-108X |
DOI: | 10.1016/S0166-2236(99)01532-5 |