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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1993-9-2
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pubmed:abstractText |
Phospholipase A2 activity has been measured in membrane and cytosolic fractions from non-pregnant and pregnant guinea pig myometrium has been studied. Enzyme activity was measured with 1-stearoyl-2- [3H]arachidonoyl-phosphatidylcholine exhibiting Michaelis-Menton kinetics with Km of 83.8 +/- 21.6 and 53.2 +/- 14.1 for membrane and cytosolic enzymes respectively. Fractionation of the myometrium from non-pregnant guinea pigs suggested that 35% of the activity was membrane associated compared with 20% (P < 0.01) in tissue from pregnant animals. In the presence of 1 mM calcium total activity rose from 3.03 +/- 0.41 to 1737 +/- 368 nmol/h per uterus between non-pregnant and late pregnancy. Calcium activated the membrane enzyme, but the effect was greater late in pregnancy with almost a 6-fold increase in activity at 1 mM calcium compared with a doubling in membrane from non-pregnant guinea pigs. The K0.5 for calcium activation was about 150 microM. Immunoblotting with anti-human-110 KDa phospholipase A2 showed in guinea pig uterus a 34 KDa form of the enzyme that, consistent with changes in activity, showed a fifteen-fold increase in quantity between non-pregnant and late pregnancy. The data are consistent with dramatic increases in the capacity for arachidonic acid release and prostaglandin production in the guinea pig myometrium late in pregnancy.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-stearoyl-2-arachidonylphosphatidyl...,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0141-9846
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
271-7
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1307379-Animals,
pubmed-meshheading:1307379-Arachidonic Acid,
pubmed-meshheading:1307379-Calcium,
pubmed-meshheading:1307379-Cell Membrane,
pubmed-meshheading:1307379-Enzyme Activation,
pubmed-meshheading:1307379-Female,
pubmed-meshheading:1307379-Guinea Pigs,
pubmed-meshheading:1307379-Kinetics,
pubmed-meshheading:1307379-Myometrium,
pubmed-meshheading:1307379-Phosphatidylcholines,
pubmed-meshheading:1307379-Phospholipases A,
pubmed-meshheading:1307379-Phospholipases A2,
pubmed-meshheading:1307379-Pregnancy,
pubmed-meshheading:1307379-Pregnancy, Animal
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pubmed:year |
1992
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pubmed:articleTitle |
Changes in phospholipase A2 in myometrium of the guinea pig uterus during pregnancy.
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pubmed:affiliation |
Laboratory of Cellular and Developmental Physiology, University of Oxford, John Radcliffe Hospital, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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