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

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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)

Nonspecific lipid transfer protein accelerated cholesterol exchange from brush border vesicles according to a biphasic time course, but sonicated vesicles made from brush border phospholipids and glycosphingolipids showed a single phase exchange. Removal of surface protein with papain or opening brush border vesicles with deoxycholate did not abolish the biphasic exchange pattern. In brush border vesicles treated with cholesterol oxidase, 21 +/- 10% of the free cholesterol was oxidized rapidly, and the remaining cholesterol was oxidized at a slower rate. Opening vesicles with sodium deoxycholate or treatment with phospholipase C, which degraded 55% of the phospholipids, did not increase the size of the rapidly oxidizable cholesterol pool. The rapidly exchangeable and the rapidly oxidizable cholesterol pools appear to represent the same fraction. In double-labeled brush border vesicles 27 +/- 9% of the cholesterol is present in a readily accessible pool, which slowly equilibrates with the remaining membrane cholesterol. The fractional turnover rate of cholesterol in the readily accessible pool equals 0.07 +/- 0.04 h-1 and is increased to 3.35 h-2 by 12 micrograms/ml of nonspecific lipid transfer protein. The heterogeneous distribution of cholesterol in the intact brush border vesicles may not reflect an inside-outside distribution or interaction of cholesterol with membrane lipids but rather an association of more than two-thirds of the membrane cholesterol with a membrane protein fraction.
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PMID:Heterogeneity of rabbit intestine brush border plasma membrane cholesterol. 708 41

The apparent association velocity constant (k'c) was determined before and after disruption of the red blood cell membrane in one of several ways: 1) radiation of the cells using a 137Cs source did not significantly alter k'c (95 +/- 39.3 and 118 +/- 35.5 mM-1.s-1), 2) incubation of the cells with sialidase produced no change in k'c (112 +/- 42.6 and 123 +/- 46.8 mM-1.s-1), 3) using papain for the incubation similarly produced no significant alteration in k'c (94 +/- 21.2 and 113 +/- 51.8 mM-1.s-1), 4) a radiomimetic agent p-chloromercuribenzene sulfonate likewise produced no significant alteration in k'c (128 +/- 16.3 and 122 +/- 3.5 mM-1.s-1), and 5) employing phospholipase C to disrupt the membrane k'c did not significantly change (115 +/- 15.3 and 112 +/- 8.7 mM-1.s-1). We conclude that either O2 traverses the membrane in a manner uninfluenced by the manipulations here employed, or that the membrane offers no significant resistance to the speed of O2 uptake.
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PMID:Resistance of red blood cell membrane to oxygen uptake. 740 13

The biochemical and functional properties of T. cruzi GP50/55, a novel glycosylphosphatidylinositol (GPI)-anchored membrane antigen have been investigated. A 50-52-kDa thiol proteinase activity could be immunoprecipitated with monoclonal antibodies (mAb) directed against GP50/55 (mAb C10), different from the one reactive with mAbs against lysosomal cysteine proteinase GP57/51. Furthermore, the mAb C10-reactive proteinase corresponded to the GPI-anchored surface antigen since the proteolytic and antigenic activity partitioned to the aqueous phase after Triton X114 phase separation of phosphatidylinositol specific phospholipase C (PI-PLC)-treated parasites. Of several proteins immunoprecipitated by a polyclonal anti-lysosomal cysteine proteinase, an mAb to GP57/51 recognized a 60-kDa protein, whereas mAb C10 recognized antigens ranging between 52 and 50 kDa. The GP50/55 antigen detected by mAb C10 is expressed on the parasite surface whereas the GP57/51 antigen is mainly intracellular. The internal peptide sequence obtained from purified GP50/55 showed that it is more homologous to the prototype of the cysteine proteinases superfamily, papain, than to the two T. cruzi lysosomal cysteine proteinases so far described. Our data indicate that the T. cruzi GP50/55 is a novel GPI-anchored cysteine proteinase and may represent another isoform of this heterogeneous group of proteinases.
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PMID:Trypanosoma cruzi: identification of a membrane cysteine proteinase linked through a GPI anchor. 808 Dec 61

High-molecular-mass alkaline phosphatase (H-Mr AP) was detected in sera from children with solid tumors without liver metastases. H-Mr AP activities were determined by a liquid chromatographic and an electrophoretic method. In 5 out of 10 cases with solid tumors--Ewing sarcoma (n = 2), neuroblastoma (n = 2), and rhabdoid tumor (n = 1)--H-Mr AP activities ranged from 3.1-40.4 U/L and 3.1-16% of total serum AP activity. In sera of patients with leukemia (n = 18) H-Mr AP was not detectable. After the treatment of the sera with papain and phosphatidylinositol-specific phospholipase C, which release membrane-associated AP from membrane particles, H-Mr AP was no longer detectable. These results indicate that H-Mr AP in the sera of patients with solid tumors may derive from increasing cell shedding of the tumor cells with elevated levels of membrane fragments in serum, which is a well known phenomenon in liver tumors. H-Mr AP was not more detectable in the serum after successful tumor treatment. These data suggest that H-Mr AP was produced by the tumors and that this parameter may be a serological marker for some solid tumors even in the presence of normal total AP serum activity.
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PMID:High-molecular-mass or macromolecular alkaline phosphatase in sera of children with solid tumors. 815 5

Transformation of cercariae of Schistosoma mansoni into schistosomula is accompanied by release of a soluble 28-kDa serine protease (s28) from the acetabular glands. The postulated activities of s28 include cleavage of skin connective tissue proteins (elastin, etc.), release of the cercarial glycocalyx, and cleavage of complement proteins. Our previous results demonstrated the presence of an antigenically cross-reactive protein on the surface of mechanically transformed schistosomula. As shown here, schistosomula express on their surface a 28-kDa serine protease (m28) which can be immunoprecipitated with anti-s28 antibodies. m28 eluted from the schistosomular tegumental membrane with NP-40 was purified to homogeneity in one step by adsorption on a chymotrypsin inhibitor column: 6-aminocaproyl-D-tryptophan methyl ester-Sepharose. Proteolytic activity of m28 was completely inhibited by the chymotrypsin inhibitor N-succinyl-Ala-Ala-Pro-Phe-chloromethyl ketone. Efficient removal of m28 from schistosomula was achieved with NP-40, deoxycholate, cholate, Tween 20, and phospholipases A2 and C, but not with papain, trypsin, pronase, or proteinase K. Furthermore, treatment with phosphatidyl inositol-specific phospholipase C (PI-PLC) followed by hydroxylamine also released m28. Anti-cross-reactive determinant antibodies which recognize a neo epitope exposed in glycosyl phosphatidyl inositol-containing molecules cleaved by PI-PLC bind to purified m28. The latter results suggest that m28 is anchored to the tegumental membrane of schistosomula by a lipid anchor and that perhaps some of the m28 molecules are bound via glycosylphosphatidyl inositol. Based on inhibitor sensitivity and antigenic cross-reactivity, it is conceivable that s28 and m28 are related, if not identical, proteins. Finally, m28 was detected antigenically also on lung-stage and adult worms of S. mansoni.
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PMID:Schistosoma mansoni: evidence for a 28-kDa membrane-anchored protease on schistosomula. 865 54

Porcine reproductive and respiratory syndrome virus hemagglutinin (HAin) was readily adsorbed on mouse erythrocytes at 4, 22, or 37 degrees C, but not on goose erythrocytes. The adsorbed HAin could not be eluted from the cells by resuspending in phosphate buffered saline, by incubating at 37 or 50 degrees C, or by incubating in the presence of neuraminidase. The hemagglutinating activity was not dependent on the pH and NaCl molarity tested. The receptor of mouse erythrocytes for the HAin was relatively stable to trypsin, neuraminidase, sodium deoxycholate (DOC), potassium periodate (KIO4), dithiothreitol (DTT), 2-mercaptoethanol (2-ME) and formalin treatments. The HAin was inactivated by 2-ME and was gradually inactivated by pepsin, formalin and DTT, but not by beta-glucosidase, trypsin, alpha-amylase, papain, phospholipase C, neuraminidase, KIO4, and ethylendiamine tetraacetic acid (EDTA) treatments. The HAin was stable at 37 degrees C or lower temperatures, but not at 56 degrees C or higher. The HAin was relatively resistant to ultraviolet irradiation and sonication. In the equilibrium centrifugation of the HAin preparation on a CsCl density gradient, the HAin activity showed a sharp peak at 1.17 g/cm2. In the SDS-PAGE analysis, the structural polypeptide of HAin in the peak fraction seems to be the nucleocapsid (N) polypeptide with molecular weight of 15 kDa.
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PMID:Characterization of porcine reproductive and respiratory syndrome virus hemagglutinin. 915 37

Some biochemical and functional characteristics of the swine swC1 antigen, determined by the use of the authors' swC1-specific monoclonal antibody (mAb) 335-2, are reported. The molecular weight of the antigen was determined by immunoprecipitation. The swC1 antigen has 41 and approx. 15 kD components under reducing conditions. It is sensitive to proteolytic enzymes such as bromelain or trypsin, but not to papain. Phosphatidylinositol-specific phospholipase C treatment diminished the expression of swC1 on the surface of leukocytes. Cross-linking of swC1 on the cell surface did not influence the proliferation of mitogen-activated mononuclear cells and had no mitogenic activity by itself. During 48 h of mitogen activation its surface expression did not change significantly. Possible relationships of swC1 to human CD antigens are discussed in the light of the results obtained.
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PMID:Characterisation of the swine swC1 antigen. 927 Jan 26

Spodoptera frugiperda larvae have a microvillar aminopeptidase and both soluble and membrane-bound forms of amylase and trypsin. Membrane-bound aminopeptidase is solubilized by glycosyl phosphatidylinositol-specific phospholipase C (GPI-PLC) and detergents, suggesting it has a GPI anchor. Membrane-bound trypsin is not affected by GPI-PLC, although it is solubilized by papain and by different detergents. Membrane-bound amylase is similar to trypsin, although once solubilized in detergent it behaves as a hydrophilic protein. Musca domestica trypsin antiserum cross-reacts with only one polypeptide from S. frugiperda midgut. With this antiserum, trypsin was immunolocalized in the anterior midgut cells at the microvillar surface and on the membranes of secretory vesicles found in the apical cytoplasm and inside the microvilli. The data suggest that in this region trypsin is bound to the secretory vesicle membrane by a hydrophobic anchor. Vesicles migrate through the microvilli and are discharged into the lumen by a pinching-off process. Trypsin is then partly processed to a soluble form and partly, still bound to vesicle membranes, incorporated into the peritrophic membrane. In posterior midgut cells, trypsin immunolabelling is randomly distributed inside the secretory vesicles and at the microvilli surface, suggesting exocytosis. Amylase probably follows a route similar to that described for trypsin in anterior midgut, although membrane-bound forms (peptide anchor) solubilize apparently as a consequence of a pH increase inside the vesicles.
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PMID:Nature of the anchors of membrane-bound aminopeptidase, amylase, and trypsin and secretory mechanisms in Spodoptera frugiperda (Lepidoptera) midgut cells. 1277 Mar 93

Pharmacological and biochemical characteristics of the binding activity of radiolabeled l-glutamic acid (Glu), a putative central excitatory neurotransmitter, were studied by using supernatant preparations solubilized from the rat adrenal by Nonidet P-40. Binding activity in the solubilized preparations was stereospecific and structure selective. This adrenal binding activity was markedly abolished by quisqualate (QA), l-glutamate diethylester and dl-2-amino-3-phosphonopropionate. None of the other agonists and antagonists for the central acidic amino acid receptors affected the binding activity. Scatchard analysis revealed that Na(+) ions significantly diminished the binding activity through decreasing the number of binding sites. A potent inhibition of the binding activity invariably resulted from the treatment of solubilized preparations with various proteases such as trypsin, chymotrypsin, papain and pronase E. Similarly significant inhibition was induced by the treatment with ?-glucosidase and phospholipase C. Heating at 70 or 100 degrees C completely abolished the binding activity, while heating at 55 degrees C induced no significant change in the activity. Cation exchange column chromatography revealed the formation of radioactive product from [(3)H]Glu during the incubation in a temperature-dependent manner. These results suggest the possible involvement of a heat-stable glycoprotein enzyme system capable of converting the central neurotransmitter to other products in the QA-sensitive [(3)H]Glu binding activity solubilized from the adrenal gland.
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PMID:Characterization of quisqualate-sensitive [(3)H]glutamate binding activity solubilized from rat adrenal. 2050 75


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