Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5533
pubmed:dateCreated
2001-8-17
pubmed:abstractText
We characterized an activation mechanism of the human LTRPC2 protein, a member of the transient receptor potential family of ion channels, and demonstrated that LTRPC2 mediates Ca2+ influx into immunocytes. Intracellular pyrimidine nucleotides, adenosine 5'-diphosphoribose (ADPR), and nicotinamide adenine dinucleotide (NAD), directly activated LTRPC2, which functioned as a Ca2+-permeable nonselective cation channel and enabled Ca2+ influx into cells. This activation was suppressed by intracellular adenosine triphosphate. These results reveal that ADPR and NAD act as intracellular messengers and may have an important role in Ca2+ influx by activating LTRPC2 in immunocytes.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosyl Cyclase, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate Ribose, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD38, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation, http://linkedlifedata.com/resource/pubmed/chemical/CD38 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Calcium, http://linkedlifedata.com/resource/pubmed/chemical/Calcium Channels, http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/NAD, http://linkedlifedata.com/resource/pubmed/chemical/NAD Nucleosidase, http://linkedlifedata.com/resource/pubmed/chemical/TRPM Cation Channels, http://linkedlifedata.com/resource/pubmed/chemical/TRPM2 protein, human
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
293
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1327-30
pubmed:dateRevised
2007-3-19
pubmed:meshHeading
pubmed-meshheading:11509734-ADP-ribosyl Cyclase, pubmed-meshheading:11509734-Adenosine Diphosphate Ribose, pubmed-meshheading:11509734-Adenosine Triphosphate, pubmed-meshheading:11509734-Antigens, CD, pubmed-meshheading:11509734-Antigens, CD38, pubmed-meshheading:11509734-Antigens, Differentiation, pubmed-meshheading:11509734-Apoptosis, pubmed-meshheading:11509734-Calcium, pubmed-meshheading:11509734-Calcium Channels, pubmed-meshheading:11509734-Cell Line, pubmed-meshheading:11509734-Eosinophils, pubmed-meshheading:11509734-Humans, pubmed-meshheading:11509734-Ion Channels, pubmed-meshheading:11509734-Jurkat Cells, pubmed-meshheading:11509734-Membrane Glycoproteins, pubmed-meshheading:11509734-Membrane Potentials, pubmed-meshheading:11509734-Membrane Proteins, pubmed-meshheading:11509734-Monocytes, pubmed-meshheading:11509734-NAD, pubmed-meshheading:11509734-NAD+ Nucleosidase, pubmed-meshheading:11509734-Patch-Clamp Techniques, pubmed-meshheading:11509734-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11509734-T-Lymphocytes, pubmed-meshheading:11509734-TRPM Cation Channels
pubmed:year
2001
pubmed:articleTitle
Immunocyte Ca2+ influx system mediated by LTRPC2.
pubmed:affiliation
Molecular Medicine Laboratories, Institute for Drug Discovery Research, Yamanouchi Pharmaceutical Co., Ltd., 21 Miyukigaoka, Tsukuba, Ibaraki 305-8585, Japan. sano.yorikata@yamanouchi.co.jp
pubmed:publicationType
Journal Article