Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.4.3 (phospholipase C)
 18,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Phosphoinositide phospholipase C (PLC) activity extracted from bovine liver plasma membranes with sodium cholate was stimulated by GTP gamma S-activated G alpha q/G alpha 11, whereas the enzyme from liver cytosol was not. The membrane-associated PLC was subjected to chromatography on heparin-Sepharose, Q Sepharose, and S300HR, enabling the isolation of the G-protein stimulated activity and its resolution from PLC-gamma and PLC-delta. Following gel filtration, two proteins of 150 and 140 kDa were found to correspond to the activatable enzyme. These proteins were identified immunologically as members of the PLC-beta family and were completely resolved by chromatography on TSK Phenyl 5PW. The 150-kDa enzyme was markedly responsive to GTP gamma S-activated alpha-subunits of G alpha q/G alpha 11 or to purified Gq/G11 in the presence of GTP gamma S. The response of this PLC was of much greater magnitude than that of the 140-kDa enzyme. The partially purified 150-kDa enzyme showed specificity for PtdIns(4,5)P2 and PtdIns4P as compared to PtdIns and had an absolute dependence upon Ca2+. These characteristics were similar to those of the brain PLC-beta 1. The immunological and biochemical properties of the 150-kDa membrane-associated enzyme are consistent with its being the PLC-beta isozyme that is involved in receptor-G-protein-mediated generation of inositol 1,4,5-triphosphate in liver.
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PMID:Identification in bovine liver plasma membranes of a Gq-activatable phosphoinositide phospholipase C. 132 Sep 35

Phosphoinositide phospholipase C activity was investigated in human melanoma grown as solid tumor xenografts in nude mice. The enzyme was dependent on calcium for activity and was stimulated by the detergent deoxycholate. The pH optimum was 5.5 in the absence of detergent, and in the presence of deoxycholate two pH maxima were present, 5.5 and 7.2. Phospholipase C activity was inhibited by the sulfhydryl reagent dithionitrobenzoate with an IC50 in the micromolar range. Phospholipase C activity was distributed widely in mouse tissues. The enzyme showed a progressive increase in activity from heart, liver, lung, colon, spleen, to brain tissue. Mouse and human melanomas grown as solid tumors had higher phospholipase C activity than mouse brain. The relatively high activity of this enzyme in melanoma may suggest a biological role for phospholipase C in solid tumor growth.
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PMID:Characterization of phosphatidylinositol phospholipase C activity in human melanoma. 230 36

Phosphoinositide phospholipase C activity has been measured in erythrocyte membranes from age-matched control and CF subjects. Inositol phospholipids were labelled with [3H]myo-inositol and control experiments demonstrated that the [3H]-labelled products released by incubation of membranes with Ca2+ were derived specifically from erythrocytes (a) by purification of erythrocytes on cellulose columns, (b) by demonstration that the phospholipase C activity was inhibited by 10 mmol/l neomycin but not by 1 mmol/l p-methylsulphonylfluoride. The [3H]-labelled products were shown to be inositol phosphates by their elution from anion-exchange columns. Membranes from CF patients showed increased phospholipase C activity compared to controls which did not correlate with the degree of [3H]inositol labelling of the membranes, with pancreatic function as assessed by serum immunoreactive trypsin or with medications taken by the patients.
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PMID:Increased phosphoinositide breakdown by phospholipase C in erythrocyte membranes from patients with cystic fibrosis. 254 51

Phosphoinositide phospholipase C (PLC) was extracted from the synaptic membrane fraction of rat brain by 1% sodium deoxycholate. The molecular weight and sedimentation coefficient of the membrane PLC were about 160,000 and 6.7 as estimated by gel filtration and sucrose density gradient centrifugation, respectively. These values of the membrane PLC were identical with those of the cytosol PLC of the same tissue. Moreover, the membrane PLC showed the substrate specificity for phosphatidylinositol, phosphatidylinositol-4-monophosphate and phosphatidylinositol-4,5-bisphosphate and the sensitivity to Ca2+, sodium deoxycholate and N-ethylmaleimide similar to those of the cytosol PLC. These results indicate that the rat brain synaptic membrane PLC is indistinguishable from the cytosol PLC in physical and kinetic properties.
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PMID:Similar physical and kinetic properties of rat brain synaptic membrane and cytosol phosphoinositide phospholipases C. 303 20