Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
|
pubmed:dateCreated |
1991-5-21
|
pubmed:abstractText |
Extracellular adenosine triphosphate (ATP), at micromolar/nanomolar concentrations, has been shown to induce significant functional changes in a wide variety of normal and transformed cell types. While ATP can be nonspecifically released from the cytosol of damaged cells, it is also co-packaged in certain exocytotic vesicles/granules containing conventional neurotransmitters and hormones. The diverse biologic responses to ATP appear to be mediated by a variety of so-called P2-purinergic, cell surface receptors that are activated upon binding ATP and other nucleotides. Recent physiologic, biochemical, and pharmacologic studies suggest that there are multiple ATP receptor subtypes. These include: (1) G-protein-coupled ATP receptors, which stimulate inositol phospholipid hydrolysis, Ca2+ mobilization, and activation of protein kinase C; (2) ATP receptors that directly activate nonselective cation channels in the plasma membranes of a variety of excitable cell types; and (3) ATP receptors that, via the rapid induction of surface membranes pores permeable to both ions and endogenous metabolites, can produce cytotoxic or activation responses in T lymphocytes and other immune effector cells. In addition to these functional criteria, these putative ATP receptor subtypes can be distinguished by characteristic selectivities for a variety of structurally modified ATP analogs. Current research is directed towards the identification, isolation, and structural characterization of these receptors by both biochemical and molecular biologic approaches.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ATP carrier receptor,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ion Channels,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial ADP, ATP Translocases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol...,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Diester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Purinergic
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
1044-1549
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
4
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
295-300
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:1707633-Animals,
pubmed-meshheading:1707633-GTP-Binding Proteins,
pubmed-meshheading:1707633-Ion Channels,
pubmed-meshheading:1707633-Mitochondrial ADP, ATP Translocases,
pubmed-meshheading:1707633-Phosphatidylinositol Diacylglycerol-Lyase,
pubmed-meshheading:1707633-Phosphoric Diester Hydrolases,
pubmed-meshheading:1707633-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:1707633-Receptors, Purinergic,
pubmed-meshheading:1707633-Signal Transduction,
pubmed-meshheading:1707633-Synaptic Transmission
|
pubmed:year |
1991
|
pubmed:articleTitle |
Signal transduction by P2-purinergic receptors for extracellular ATP.
|
pubmed:affiliation |
Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio, 44106.
|
pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|