Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1990-3-20
|
pubmed:abstractText |
The incubation of isolated rat hepatocytes with extracellular adenosine 5'-triphosphate (ATP) resulted in an inhibition of Ca2+ efflux. The ATP-induced Ca2+ accumulation as determined by the increase in phosphorylase a activity and the Ca2+-sensitive fluorescent indicator (2-[(2-bis-[carboxymethyl]-amino-5-methylphenoxy)-methyl]-6-methoxy-8- bis-[carboxymethyl]aminoquinoline-tetrakis-[acetoxymethyl]ester) (Quin 2-AM) was associated with both the hydrolysis of ATP and the phosphorylation of a 110 kDa protein. No significant alteration in the intracellular ATP level was observed. The appearance of surface blebs and cytotoxicity followed the rise in cytosolic Ca2+, suggesting that the increased free Ca2+ may be responsible for the loss of viability. When a calmodulin inhibitor, 1-[bis(4-chlorophenyl)methyl]-3-[ 2-(2,4-dichlorophenyl)-2-[(2,4-dichlorophenyl)methoxy] ethyl]-1H- imidazolium chloride (calmidazolium), was included in the medium prior to ATP addition, bleb formation was reduced and the loss of viability was completely prevented, indicating that a Ca2+-calmodulin process may be involved in the initiation of cytotoxicity.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Aminoquinolines,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Imidazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphorylase a,
http://linkedlifedata.com/resource/pubmed/chemical/Quin2-acetoxymethyl ester,
http://linkedlifedata.com/resource/pubmed/chemical/calmidazolium
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0887-2082
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
1
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
29-39
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:3271869-Adenosine Triphosphate,
pubmed-meshheading:3271869-Aminoquinolines,
pubmed-meshheading:3271869-Animals,
pubmed-meshheading:3271869-Calcium,
pubmed-meshheading:3271869-Calmodulin,
pubmed-meshheading:3271869-Cytosol,
pubmed-meshheading:3271869-Homeostasis,
pubmed-meshheading:3271869-Imidazoles,
pubmed-meshheading:3271869-Liver,
pubmed-meshheading:3271869-Male,
pubmed-meshheading:3271869-Phosphorylase a,
pubmed-meshheading:3271869-Phosphorylation,
pubmed-meshheading:3271869-Rats,
pubmed-meshheading:3271869-Rats, Inbred Strains
|
pubmed:year |
1986
|
pubmed:articleTitle |
Ca2+ homeostasis and cytotoxicity in isolated hepatocytes: studies with extracellular adenosine 5'-triphosphate.
|
pubmed:affiliation |
Department of Toxicology, Karolinska Institutet, Stockholm, Sweden.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|