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)

From various rat organs, alkaline phosphodiesterase I was liberated by the action of phosphatidylinositol-specific phospholipase C obtained from Bacillus thuringiensis. Especially, a large amount of alkaline phosphodiesterase I was released from slices of small intestine, testis, lung, and kidney, but not from pancreas and liver. The release of the enzyme induced by phospholipase C was dependent on, or proportional to, the reaction time and the concentrations of the phospholipase C and the weight of the slices of small intestine or testis. Furthermore, little enzyme was released from the homogenate of pancreas. These results suggest an important role of phosphatidylinositol in the binding of alkaline phosphodiesterase I to the plasma membranes of rat small intestine and pancreas. The alkaline phosphodiesterase I released from slices of rat small intestine and testis had a molecular weight of about 240,000, and was activated by Mg2+ and Ca2+ but inhibited by EDTA. The enzyme hydrolyzed the phosphodiester linkage of p-nitrophenyl-thymidine 5'-monophosphate at pH 8.9, having the Km values of 0.36 mM (small intestine) and 0.25 mM (testis). The intestinal enzyme differed from the testis enzyme in pI values, thermostability, and Arrhenius plot having a single breakpoint.
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PMID:Alkaline phosphodiesterase I release from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C. I. The release from rat organs. 301 61

Ectoenzyme release from porcine intestinal brush border membranes by phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis was studied. Alkaline phosphodiesterase I, alkaline phosphatase and 5'-nucleotidase were released from both slices and brush border membranes. The pattern of alkaline phosphodiesterase I release was the same as that of alkaline phosphatase. The release of alkaline phosphodiesterase I induced by phospholipase C was dependent on, or proportional to, the reaction time and the concentration of phospholipase C. The Arrhenius plot for phosphodiesterase I release showed a single break at 30 degrees C for brush border membranes. Only 40% of alkaline phosphodiesterase I present in the brush border membranes were solubilized by phosphatidylinositol-specific phospholipase C treatment. The data indicate the presence of two forms of phosphodiesterase I, which are different in their sensitivity to phospholipase C. The released alkaline phosphodiesterase I had a molecular weight of 240,000 and was activated by Mg2+ and Ca2+, but strongly inhibited by EDTA.
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PMID:Alkaline phosphodiesterase I release from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C. II. The release from brush border membranes of porcine intestine. 302

The release of plasma-membrane-bound enzymes by phosphatidylinositol-specific phospholipase C obtained from Bacillus thuringiensis was investigated. Among the ectoenzymes of plasma membrane tested, alkaline phosphodiesterase I was released markedly from rat kidney cortex slices, in addition to alkaline phosphatase and 5'-nucleotidase. Other membrane-bound enzymes; alanine aminopeptidase, leucine aminopeptidase, dipeptidyl peptidase, leucine aminopeptidase, dipeptidyl peptidase IV, esterase and gamma-glutamyl transpeptidase could not be liberated from the treated slices. Alkaline phosphodiesterase I was released linearly from rat kidney slices with the concentration of phosphatidylinositol-specific phospholipase C, but little enzyme was released from rat liver slices. Alkaline phosphodiesterase I separated from kidney tissue with n-butanol still retained phosphatidylinositol and was transformed into a lower molecular weight form by phosphatidylinositol-specific phospholipase C. This suggests an important function for phosphatidylinositol in the binding of alkaline phosphodiesterase I to the plasma membrane of rat kidney cells. The alkaline phosphodiesterase I released from rat kidney had a molecular weight of about 240,000 and an isoelectric point (pI) of 5.4. The enzyme hydrolyzed the phosphodiester linkage of p-nitrophenyl-thymidine 5'-monophosphate at pH 8.9 and had a Km value of 0.3 mM. The enzyme was activated by Mg2+ and Ca2+, but was inhibited by EDTA. Strong inhibition took place on the addition of adenosine 5'-phosphosulfate or the nucleotide pyrophosphates, i.e., UDP-galactose and alpha, beta-methylene ATP.
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PMID:Release of alkaline phosphodiesterase I from rat kidney plasma membrane produced by the phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis. 609 28

The role of phosphatidylinositol-specific phospholipase C (PIase C) in a) the enigmatic phosphatidylinositol (PI) turnover and b) in our understanding of membrane enzyme-PI interactions is the subject matter of this article. PIase C is present in both procaryotes and eukaryotes. This enzyme is considered to be involved in the cells PI breakdown which occurs in response to several external stimuli. Recent information on the physical properties, Ca2+ requirement, cellular localization and modulation of the activity of PIase C of mammalian systems can help to evaluate the PI turnover from a new angle. Existing evidence suggests that Ca2+-dependent PI breakdown is probably mediated through the cytosolic and particulate PIase C while a Ca2+ independent pathway is catalyzed by a lysosomal enzyme. Apparently PI turnover may be operating through more than one mechanism. The association of this phenomenon with a membrane receptor event linked with "Ca2+ gating" may have to be reconsidered. Modulation of the PIase C activity by unsaturated amphiphiles or the presence of this enzyme in different physico-chemical forms could be a potential regulatory feature. Hydrolysis of membrane PI of a number of cells and tissues by the bacterial PIase C has been shown to cause substantial release of acetylcholinesterase, alkaline phosphatase and 5'-nucleotidase in free, soluble form. Other membrane enzymes, e.g., alkaline phosphodiesterase I, L-leucyl-beta naphthyl amidase and Ca2+ or Mg2+ ATPase are not affected. These results indicate a specific interaction between PI and certain enzymes in membranes. The chemical nature of this linkage, whether it is covalent or non-covalent, has also been explored and has provided intriguing insight into this phenomenon. New findings also indicate that hydrolysis of PI by PIase C also can cause modifications in membrane-enzyme activities, e.g., adenylate cyclase.
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PMID:Minireview. Phosphatidylinositol specific phospholipases C. 708 67

Prostasomes are human prostate derived organelles that were isolated from both prostatic fluid and seminal plasma for the present study. Specific activities were determined for prostasome membrane-associated enzymes, alkaline phosphatase (ALP), 5'-nucleotidase (5'NT), and alkaline phosphodiesterase I (APD). The mode of their membranous anchoring was studied by treatment of prostasomes with phosphoinositol-specific phospholipase C (PIPLC) and different detergents. A substantial amount of ALP (50%) and 5'NT (31%) was released by incubation of prostasomes with 2 U/ml of PIPLC contrary to the small amount of APD (12%) released by the same treatment. After PIPLC treatment, the enzymes were recovered in the aqueous phase after phase repartition in Triton X-114 indicating that PIPLC removed the hydrophobic domain converting the enzymes from membrane-linked to aqueous soluble forms. Octyl glycoside was the most efficient one among different detergents to solubilize the enzymes from the prostasome membrane. Both ALP and 5'NT were resistant to the treatment with Triton X-100 and Triton X-114. These results suggest that ALP, 5'NT, and APD are more or less extensively linked to the prostasome membrane via a glycophosphoinositide anchor.
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PMID:Association of some hydrolytic enzymes with the prostasome membrane and their differential responses to detergent and PIPLC treatment. 763 87

1. Alkaline phosphodiesterase I release from two tumor cell lines, KB III or AH-130 cells, by the action of phosphatidylinositol-specific phospholipase C (PIPLC) of Bacillus thuringiensis was studied. 2. A significant amount of alkaline phosphodiesterase I was released from both the cell suspension and homogenate of KB III cells, but not from AH-130 cells. 3. The release of the enzyme from KB III cells was dependent on, or proportional to, the reaction time and the PIPLC or cell concentrations. 4. Alkaline phosphatase and 5'-nucleotidase were also released from KB III cells, while gamma-glutamyl transpeptidase and dipeptidyl peptidase IV were not solubilized. The enzyme release by the action of PIPLC was suppressed when purified anti-PIPLC antibody was added to the reaction mixture. This suggests that the enzyme release must be due to the direct action of PIPLC on KB III cells. 5. The alkaline phosphodiesterase I released from KB III cells had a mol. wt of 240,000 and was activated by Mg2+, but strongly inhibited by EDTA and thiol reagents and by 5'-nucleotide-containing compounds. Although KB III cells were derived from Homo sapiens tumor, the released alkaline phosphodiesterase I appeared to be very similar to enzymes obtained from normal tissues of Rattus norvegicus.
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PMID:Alkaline phosphodiesterase I release from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C. III. The release from tumor cells. 790 75

1. Alkaline phosphodiesterase I release from organs of Cacia porcellus by the action of phosphatidylinositol-specific phospholipase C (PIPLC) of Bacillus thuringiensis was studied. 2. A significant amount of alkaline phosphodiesterase I was released from both slices and homogenate of the kidney and small intestine but not from the liver or pancreas. 3. The release of the enzyme from kidney brush border membranes was dependent on, or proportional to, the reaction time and the PIPLC concentration. The enzyme release by PIPLC was suppressed when the PIPLC was heat-inactivated before addition to the reaction mixture. This suggests that the enzyme release must be due to direct action of PIPLC on kidney brush border membranes. 4. The released alkaline phosphodiesterase I had a molecular weight of 240,000 and was activated by Mg2+, but strongly inhibited by EDTA, thiol reagents and 5'-nucleotide-containing compounds.
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PMID:Alkaline phosphodiesterase I release from eucaryotic plasma membranes by phosphatidylinositol-specific phospholipase C--IV. The release from Cacia porcellus organs. 817 51

1. Ectoenzyme release from kidney brush border membranes of Rattus norvegicus and Sus scrofa domesticus by phosphatidylinositol-specific phospholipase C (PIPLC) of Bacillus thuringiensis was studied. 2. The levels of specific activities of ectoenzymes in R. norvegicus kidney brush border membranes were higher than those in S. scrofa domesticus. About 10-fold higher values were found for specific activities of alkaline phosphatase and gamma-glutamyl transpeptidase in R. norvegicus. 3. Alkaline phosphodiesterase I, alkaline phosphatase and 5'-nucleotidase were released from both R. norvegicus and S. scrofa domesticus brush border membranes, while gamma-glutamyl transpeptidase and dipeptidyl peptidase IV were not solubilized. The enzyme release by the action of PIPLC was suppressed when purified anti-PIPLC antibody was added to the reaction mixture. This suggests that enzyme release must be due to the direct action of PIPLC on kidney brush border membranes. 4. The released alkaline phosphodiesterase I from kidney of S. scrofa domesticus had a molecular weight of 240,000 and was activated by Mg2+ and Ca2+, but strongly inhibited by EDTA.
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PMID:Proof of alkaline phosphodiesterase I as a phosphatidylinositol-anchor enzyme. 839 52

This study investigated ectoenzyme release from small intestine brush border membranes (duodenum and jejunum, Preparation A; ileum, Preparation B) of mice by the action of phosphatidylinositol-specific phospholipase C or glycosyl-phosphatidylinositol-specific phospholipase D. Most of the alkaline phosphatase was solubilized from Preparation A, but about 60% was released from Preparation B. As for alkaline phosphodiesterase I activity, 15 and 10% were released from Preparations A and B, respectively. With Preparation B, octylglucoside treatment followed by phosphatidylinositol-specific phospholipase C or glycosyl-phosphatidylinositol-specific phospholipase D completely solubilized the alkaline phosphatase activity. However, this treatment did not change the ratio of release of alkaline phosphodiesterase I from Preparation A or B. These results indicate that the resistance to alkaline phosphatase found in Preparation B is due to hindered accessibility of the bonding splitting by phosphatidylinositol-specific phospholipase C and not to a modified glycosyl-phosphatidylinositolanchor.
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PMID:Release of ectoenzymes from small intestine brush border membranes of mice by phospholipases. 905 73

Phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus thuringiensis added to a culture of LLC-PK1 cells inhibited cell growth by 40%. In contrast with normal cells, the cells cultured in the presence of PI-PLC showed needle-like appendages which seemed to have been formed due to portions of the cell remaining adhered to the culture dish as the cell shrank. When LLC-PK1 cells were treated with PI-PLC, significant amounts of alkaline phosphatase and alkaline phosphodiesterase I were released specifically from the apical surface of the LLC-PK1 cells. Furthermore, PI-PLC treatment caused a delay of enzyme production and dome formation. These data indicate that glycosyl-phosphatidylinositol (GPI)-anchored proteins on the surface of LLC-PK1 cells are important in cell growth and differentiation. Also, the combined use of LLC-PK1 cells and PI-PLC of B. thuringiensis is effective for investigating the function of GPI-anchor proteins.
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PMID:Growth inhibition, morphological change, and ectoenzyme release of LLC-PK1 cells by phosphatidylinositol-specific phospholipase C of Bacillus thuringiensis. 917 52


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