Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

---

Query: EC:3.1.4.3 (phospholipase C)
18,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The role of protein kinase C in the mechanism of stimulation of glucose transport in rat adipocytes was investigated. Glucose transport was stimulated by dioleoylglycerol (DOG), tetradecanoyl phorbol acetate (TPA) and phospholipase C (PLC). Agents that inhibit protein kinase C (polymyxin B, gossypol and quercitin) also inhibited glucose transport that had been stimulated by DOG, TPA, PLC and insulin.
...
PMID:Evidence that protein kinase C is involved in regulating glucose transport in the adipocyte. 329 42

A glycophospholipid has been purified from rat liver membranes, which copurified with an insulin-sensitive glycophospholipid isolated from H35 hepatoma cells. The polar head group of this glycophospholipid, which is a phosphooligosaccharide, was generated by treatment with a phosphatidylinositol-specific phospholipase C from Staphylococcus aureus. There was an "insulin-like" inhibitory effect of this phosphooligosaccharide on isoproterenol-stimulated lipolysis in adipocytes, whereas there was no effect on glucose oxidation under conditions that measure glucose transport. The antilipolytic effect of this phosphooligosaccharide was demonstrated in intact adipocytes. There was a linear correlation between the concentration of phosphooligosaccharide and its antilipolytic effect, the magnitude and time course of which were similar to that obtained with physiological concentrations of insulin. Submaximal concentrations of insulin and phosphooligosaccharide produced an additive antilipolytic effect. The antilipolytic effect of the phosphooligosaccharide was demonstrated only after release of this compound from the precursor glycophospholipid with phosphatidylinositol-specific phospholipase C, and the activity of the phosphooligosaccharide was sensitive to alkali. It is proposed that this phosphooligosaccharide plays a role in mediating certain insulin actions.
...
PMID:Glucose transport and antilipolysis are differentially regulated by the polar head group of an insulin-sensitive glycophospholipid. 330 76

The major cell surface glycoconjugate of Leishmania major, a putative parasite receptor for macrophages, is a lipophosphoglycan containing 81.6% (wt/wt) carbohydrate, 17.0% (wt/wt) phosphate, and 1.4% (wt/wt) lipid. It has been purified to homogeneity by hydrophobic chromatography and consists of a polydisperse family of molecules with Mr 5000-40,000. It contains galactose, mannose, glucose, arabinose, glucosamine, and inositol in the molar ratio of 51:21:5:6:1:1. The lipophosphoglycan has a complex structure, consisting mainly of tri- and tetrasaccharide units linked by phosphodiester bonds, which are cleaved by HF hydrolysis. The phosphate groups are located on the 6-hydroxyl of both galactose and mannose residues. The lipophosphoglycan is anchored to the parasite surface by a 1-O-alkyl-sn-glycero-3-phosphoinositol moiety. This conclusion is supported by analysis of the products of nitrous acid deamination, HF hydrolysis, and Staphylococcus aureus phosphatidylinositol specific-phospholipase C treatment. The 24:0 and 26:0 alkyl chains accounted for 93% of the ether-linked fatty acids in the lipid anchor. The results are also consistent with a glycosidic linkage between the inositol and a non-N-acetylated glucosamine residue. The lipophosphoglycan membrane anchor shares limited structural homology with the glycosylphosphatidylinositol anchors of several eukaryotic proteins, indicating that this type of membrane anchor is not limited to proteins. Vaccination of mice with the purified L. major lipophosphoglycan in liposomes induced resistance against cutaneous leishmaniasis.
...
PMID:Lipophosphoglycan of Leishmania major that vaccinates against cutaneous leishmaniasis contains an alkylglycerophosphoinositol lipid anchor. 348 May 20

The influence of exogenous phospholipase C and melittin on electrical activity in islet B cells was determined to assess the extent to which polyphosphatidylinositol turnover serves to generate components that influence the electrical events in the plasma membrane. Phospholipase C hydrolyzes polyphosphatidylinositol to diacylglycerol and polyphosphoinositol, whereas melittin increases the susceptibility of phospholipids to phospholipases and increases the permeability of the membrane to ions. Application of both 20 mU/ml phospholipase C or 0.5 mg/ml melittin to 11.1 mM glucose elicited a time-dependent enhancement of glucose-induced electrical activity that stabilized after 10 min. Phospholipase C increased both the active phase fraction and the burst frequency, whereas melittin only increased the burst frequency. These results indicate that both compounds, which disrupt the phospholipid environment of the plasma membrane, play a role in modulating the oscillatory pattern of electrical activity in the B cell, although melittin is obviously not influencing the factors controlling the ionic events in the same manner as phospholipase C.
...
PMID:Phospholipase C and melittin enhancement of glucose-induced electrical activity. 351 Jan 16

We have previously suggested that insulin effects on 2-deoxyglucose (2-DOG) uptake in BC3H-1 myocytes are due to increases in de novo phospholipid synthesis, diacylglycerol generation, and protein kinase C activation. To test this hypothesis further, we examined the effects of phenylephrine, an agonist that increases diacylglycerol and protein kinase C activity through phospholipase C activation. As evidence for phospholipase activation in BC3H-1 myocytes, we found that phenylephrine increased acute 32PO4 incorporation into phosphatidic acid and phosphatidylinositol, generation of [3H]inositol phosphates from prelabeled [3H]inositol phospholipids, cytosolic Ca2+, and membrane-bound protein kinase C. Phenylephrine also provoked dose-related increases in [3H]2-DOG uptake that were similar in magnitude and time course to those induced by insulin. As with insulin, phenylephrine effects on 2-DOG uptake were not apparent in myocytes that were maximally stimulated with 12-O-tetradecanoylphorbol-13-acetate, a diacylglycerol analogue that activates protein kinase C. These findings support our hypothesis that diacylglycerol generation and protein kinase C activation may be important in the stimulation of glucose uptake by agents such as phenylephrine and insulin that activate the phosphoinositide cycle.
...
PMID:Further evidence implicating diacylglycerol generation and protein kinase C activation in agonist-induced increases in glucose uptake. Insulin-like effects of phenylephrine in BC3H-1 myocytes. 352 26

Phospholipase A2 induced crenation of human erythrocytes and decreased glucose transport activity (influx rate) by 40% when 51% of phosphatidylcholine (PC) in the membrane was hydrolyzed. On the other hand, phospholipase C induced invagination of the cells and negligibly affected the glucose transport in the case of 21% hydrolysis of the PC. By altering the pH of the medium for suspending cells treated with phospholipase A2 from 7.4 to 6.0, cell shape was changed from clear crenation to slight invagination, but glucose transport activity was not affected. Cells that were treated with phospholipase A2 and then washed with albumin to remove free fatty acids produced in the cell membrane showed an almost normal cell shape and slightly higher glucose transport activity than did untreated cells. The ratios of beta-D-glucose transport rate to alpha-D-glucose transport rate in untreated cells, cells treated with phospholipase A2 and cells treated with phospholipase C were 1.13, 1.04, and 1.20, respectively. These results demonstrate that the drastic morphological change (invagination or crenation) induced by the treatment with phospholipases bears no clear relationship to the activity of glucose transport and suggest that the increase in the volume of the outer half of the lipid bilayer might reduce the rate of glucose transport across the human erythrocyte membrane and change the anomeric preference of glucose transport.
...
PMID:Glucose transport into human erythrocytes treated with phospholipase A2 or C. 373 Apr 28

For the enumeration of vegetative cells and spores of Bacillus cereus in foods, a mannitol-egg yolk-phenol red-agar has been developed which exploits the failure of B. cereus to dissimilate mannitol, and the ability of most strains to produce phospholipase C. When a high degree of selectivity was required, polymyxin B sulfate in a concentration of 10 ppm appeared to be the most effective selective additive. Useful characteristics for the identification of presumptive isolates of B. cereus were found to be: morphology, dissimilation of glucose mostly to acetyl methyl carbinol under anaerobic conditions, hydrolysis of starch and gelatin, reduction of nitrate, and growth on 0.25% chloral hydrate agar.
...
PMID:Enumeration of Bacillus cereus in foods. 429 56

Staphylococcal alpha-toxin induces the release of previously sequestered anions or glucose from artificial phospholipid spherules, an effect abolished by specific antitoxin. Alphatoxin resembles streptolysin S in releasing anions or glucose from spherules prepared without cholesterol, and can be distinguished from the membrane-active polyene amphotericin B, which preferentially disrupts spherules containing cholesterol. It may affect biological structures by a similiar interaction with membrane phospholipids.
...
PMID:Staphylococcal alpha-toxin: effects on artificial lipid spherules. 591 41

Mepacrine and p-bromophenacylbromide were both found to impair 3H-inositol phosphate production in response to both nutrient and hormone-neurotransmitter stimuli in islets prelabelled with 3H-inositol. Both drugs also inhibited net 45Ca uptake in response to glucose or glibenclamide and considerably modified the patterns of 45Ca and 86Rb efflux from perifused islets under both basal and glucose-stimulated conditions. In addition, the oxidation of [U-14C] glucose in islets was impaired by either mepacrine or p-bromophenacylbromide. These inhibitory effects were found to be concentration-related for both mepacrine (0.01-1.0 mM) and p-bromophenacylbromide (0.03-0.3 mM) and were accompanied, in general, by a similar degree of inhibition of insulin secretion. These results suggest that both mepacrine and p-bromophenacylbromide can inhibit phospholipase C activity in intact islets, but also impair 45Ca and 86Rb fluxes and oxidation of nutrients. The diversity of these drugs' inhibitory actions makes them unsuitable tools for examining the role of specific cellular processes in the regulation of islet function.
...
PMID:Inhibition by mepacrine and p-bromophenacylbromide of phosphoinositide hydrolysis, glucose oxidation, calcium uptake and insulin release in rat pancreatic islets. 608 37

Preincubation of rat pancreatic islets with 3H-inositol, and subsequent exposure, in the presence of LiCl, to either glucose or carbamylcholine resulted in a rapid stimulation of 3H-inositol 1,4,5-triphosphate and 3H-myo-inositol 1,4-bisphosphate formation, the level of which reached a plateau after about 5 min of stimulation. Both stimuli also caused an approximately linear accumulation of 3H-myo-inositol 1-phosphate. The amounts of 3H-inositol phosphates formed were dependent on the concentration of LiCl. Studies of 32P-labeling of islet ATP, phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), and phosphatidylinositol 4-phosphate revealed that these approached isotopic equilibrium after about 240-min incubation, whereas 32P-labeling of phosphatidylinositol, phosphatidic acid, phosphatidylcholine, and phosphatidylethanolamine proceeded at a lower rate. Carbamylcholine provoked an immediate fall in 32P-PtdIns(4,5)P2 and, to a lesser extent, 32P-phosphatidylinositol 4-phosphate. Glucose caused a similar response although, in this case, the most marked decline was in a more polar 32P-labeled lipid. Cholecystokinin-pancreozymin was also found to induce 32P-PtdIns(4,5)P2 hydrolysis, although the ionophore A23187 was without effect. Both carbamylcholine and glucose induced an increase in 32P-phosphatidic acid. The results provide two independent pieces of evidence suggesting that phospholipase C-mediated hydrolysis of polyphosphoinositides occurs as an early response in rat islets to either nutrient or neurotransmitter secretagogues.
...
PMID:Nutrient and hormone-neurotransmitter stimuli induce hydrolysis of polyphosphoinositides in rat pancreatic islets. 609 36


<< Previous 1 2 3 4 5 6 7 8 9 10

---