NDLI: Human Trp3 forms both inositol trisphosphate receptor-dependent and receptor-independent store-operated cation channels in DT40 avian B lymphocytes.

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Human Trp3 forms both inositol trisphosphate receptor-dependent and receptor-independent store-operated cation channels in DT40 avian B lymphocytes.

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Human Trp3 forms both inositol trisphosphate receptor-dependent and receptor-independent store-operated cation channels in DT40 avian B lymphocytes.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Putney, J. W. St Bird, G. J. Vazquez, G. Lievremont, J. P.
Description	Author Affiliation: Vazquez G ( Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA. vasquez@niehs.nih.gov);
Abstract	Mammalian Trp proteins are candidates for plasma membrane calcium channels regulated by receptor activation or by intracellular calcium store depletion [capacitative calcium entry (CCE)]. One extensively investigated member of the Trp family, the human Trp3 (hTrp3), behaves as a receptor-activated, calcium-permeable, nonselective cation channel when expressed in cell lines and does not appear to be activated by store depletion. Nonetheless, there is good evidence that Trp3 can be regulated by interacting with inositol trisphosphate receptors (IP(3)Rs), reminiscent of the conformational coupling mode of CCE. To investigate the role of Trp3 in CCE, and its regulation by IP(3)R, we transiently expressed hTrp3 in the wild-type DT40 chicken B lymphocyte cell line and its variant lacking IP(3)R. Expression of hTrp3 in either wild-type or IP(3)R-knockout cells did not increase basal membrane permeability, but resulted in a substantially greater divalent cation entry after thapsigargin-induced store depletion. This hTrp3-dependent divalent cation entry was significantly greater in the wild type than in IP(3)R-knockout cells. Thus, it appears that in this cell line, hTrp3 forms channels that are store-operated by both IP(3)R-dependent and IP(3)R-independent mechanisms. Trp3, or one of its structural relatives, is a candidate for the store-operated, nonselective cation channels observed in smooth muscle cells and other cell types.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	98
Language	English
Publisher	National Academy of Sciences
Publisher Date	2001-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	B-Lymphocytes Physiology Calcium Channels Ion Channels Receptors, Cytoplasmic And Nuclear Animals Drug Effects Barium Metabolism Calcium Genetics Cell Line Cloning, Molecular DNA Primers Fura-2 Genetic Vectors Inositol 1,4,5-Trisphosphate Receptors Reverse Transcriptase Polymerase Chain Reaction TRPC Cation Channels Thapsigargin Pharmacology Transcription, Genetic Transfection Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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