Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.1.3 (ATPase)
 65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A histochemical study of the metabolism of rat renal arteries and arterioles. Rat renal arteries and arterioles were examined histochemically to determine their metabolic profiles. Succinate, malate and NAD-isocitrate dehydrogenase, cytochrome oxidase and ubiquinone were assessed to determine aerobic metabolism. Glucose-6-phosphate dehydrogenase and DPN diaphorase were evaluated to determine hexose-monophosphate-shunt activity. Anaerobic metabolism was evaluated via lactate dehydrogenase, and the substrate, glycogen. Gomori's lipase, beta-hydroxybutyrate dehydrogenase and amounts of neutral fat and free fatty acids were assessed as indicators of lipid utilization. Myosin ATPase activity was evaluated as an index of ATP utilization for contraction. Deoxyribonucleic and ribonucleic acids were appraised as indicators of protein synthesis. In general, the oxidative enzymes and myosin ATPase demonstrate considerable activity in renal arteries and arterioles which suggests aerobic metabolism and ATP usage. Renal arteries and arterioles also appear capable of anaerobic metabolism as indicated by strong lactate dehydrogenase reactivity and by the presence of slight to moderate quantities of glycogen, while high levels of glucose-6-phosphate dehydrogenase and moderate amounts of deoxyribonucleic acid suggest a potential for beta-hydroxybutyrate dehydrogenase, minimal lipase activity, and the absence of fatty acids with substantial amounts of neutral fat, indicate limited lipid catabolism.
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PMID:A histochemical study of the metabolism of rat renal arteries and arterioles. 620 11

Lysosomal hydrolases (e.g., acid phosphatase, AcPase; adenosine triphosphatase, ATPase, and lipase) and the mitochondrial 'marker' enzyme succinic dehydrogenase (SDH) were evaluated histochemically in the prostate gland of sexually 'quiescent' and 'active' bats. During the former state, AcPase activity was significantly less than in sexually active animals, suggesting that prostate AcPase activity is androgen dependent. Levels of lipase activity also were highest in the prostate of sexually active bats, suggesting the importance of endogenous lipids which may be mobilized and used as a source of energy. SDH and ATPase sites and patterns of distribution in the prostate gland of bats were closely similar during the two reproductive states. Differential enzymological patterns do not seem to have any significant correlation with the morphological changes which occur in the glandular epithelium, musculature, urethra and the luminal fluid, as the animals pass from a 'quiescent' phase to one of activity and vice versa as observed in the present study.
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PMID:Histoenzymological comparison of the prostate gland of sexually 'quiescent' and 'active' Taphozous melanopogon melanopogon Temmnick (Microchiroptera: Mammalia). 621 18

An enzyme histochemical and cytochemical study of normal dermal microvasculature showed that respiratory enzymes, lipase and non-specific esterase occurred in all vascular segments. Lysosomal enzymes were also widely distributed and acid phosphatase activity was localized in lysosomes, Golgi apparatus and small portions of endoplasmic reticulum of both endothelial cells and pericytes. Alkaline phosphatase activity, however, was confined to the arterial side and tip of the capillary loop where it occurred in vesicles along the luminal surface of the endothelium and in junctions between endothelial cells. The localization of nucleoside phosphatase activity within the endothelium varied according to substrate; with adenosine triphosphate as substrate, the reaction product occurred in vesicles distributed throughout the endothelial cells; with adenosine diphosphate it was limited to vesicles along the luminal surface; and with adenosine monophosphate, activity was mostly localized to the lateral surfaces of endothelial cells. These findings suggest functional variation between different vascular segments and between various components of the endothelium. Attempts to demonstrate a specific Na+K+ adenosine triphosphatase (transport ATPase) within the endothelium were not successful.
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PMID:Human dermal microvasculature: II. Enzyme histochemical and cytochemical study. 723 11

Twenty eight enzymatic activities and four macromolecular substances have been histochemically compared in rat and rabbit aortas, embedded in a common block. The study was carried out at different stages of development: 3 days, 3 months, 7-9 months and 17-19 months. In addition, lipase and cholinesterase were biochemically assayed in adult rat and rabbit aortas. The rat aortas (atheroresistant) had a better supply of aerobic oxidoreductases [linked to the pentose pathway (G6PD, 6PGD) as well as to the Krebs cycle (SD, ICD)], lipolytic enzymes (acid esterases, cholinesterase, lipase), lysosomal enzymes (acid PH/ase, Aryl-sulf/ase - Betaglu/ase), ADPase - ATPase - AlK Ph/ase Alpha GPD and acid lipids. Rabbit aortas (atherosensitive) were richer in metachromatic GAG, UDPGD (GAG Anabolism), glycogen, and related enzymes (phosphorylase, glycogen synthetase) as well as 5'-nucleotidase, Beta HBD, Lactate D and Aldolase. These differences support the hypothesis that arterial atherosensitivity is related to the activity and efficiency of smooth muscle cell energetic and catabolic processes, which govern the behaviour of lipids, proteins and carbohydrates as they penetrate the arterial wall. The factors that determine the proliferative and sclerogenic responses of arterial tissues to aggressions and, in particular, the response to lipids, remain, however, to be determined.
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PMID:A comparative study of the arterial tissue metabolism in atherosensitive and atheroresistant species. I. Comparison between rabbit and rat aortas. 734 89

African swine fever virus polypeptides with molecular weight of 120, 78, 69, 59, 56, 45, 39, 28, 26, 24, 16, and 14 kD are the major proteins in the purified virions, as shown by electrophoresis and immunoblotting. A mixture of proteases and pancreatic lipase hydrolyzed the polypeptides of 120 and 78 kD in viral preparations at low concentrations of enzymes, polypeptides of 69, 56, 45, 39, 28, and 14 kD disappeared after treatment with this mixture at medium concentrations, and 26 kD polypeptide was eliminated at a high concentration of the enzymes. The 21 kD polypeptide which did not react with the specific antiviral serum in immunoblotting was not hydrolyzed by proteases contaminating lipase. Treatment with triton X-100 and ether boosted the activity of DNA-dependent RNA-polymerase, whereas treatment with ether followed by resedimentation markedly decreased polymerase activity in the resultant sediment. Treatment with diethyl ether did not influence the activity of virus-associated ATPase, which was partially resistant to denaturating organic solvents acetone and chloroform-methanol mixture. Our findings and published data permitted us to propose a schematic arrangement of viral polypeptides and enzymes in the virion structure.
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PMID:[Localizing the major peptides of African swine fever virus and virus-associated enzymes in the virion structure]. 747 38

Chronic renal failure (CRF) is associated with increased Ca2+ content of liver and reduced hepatic lipase activity. This has been attributed to a rise in cytosolic Ca2+ ([Ca2+]i) of the hepatocytes, but data on this issue are lacking. We examined the [Ca2+]i and ATP content of hepatocytes as well as the activity of Na(+)-K(+)-adenosinetriphosphatase (Na(+)-K(+)-ATPase), Ca(2+)-ATPase, and Na+/Ca2+ exchanger of hepatic membrane vesicles from normal rats, animals with 6 wk of CRF, CRF normocalcemic parathyroidectomized (CRF-PTX) rats, and CRF and normal animals treated with verapamil (CRF-V, normal-V). [Ca2+]i in hepatocytes of CRF rats was higher (281 +/- 7.4 nM) and ATP lower (6.4 +/- 1.8 nmol/mg protein) than in normal (209 +/- 5.3 nM; 12.5 +/- 0.89 nmol/mg protein), CRF-PTX (212 +/- 1.0 nM; 13.7 +/- 0.79 nmol/mg protein), normal-V (215 +/- 2.3 nM; 14.2 +/- 0.77 nmol/mg protein), and CRF-V rats (209 +/- 7.4 nM; 14.8 +/- 0.72 nmol/10(6) cells). The Na(+)-K(+)-ATPase, the maximal velocity of Ca(2+)-ATPase, and the activity of the Na+/Ca2+ exchanger were reduced, whereas the Michaelis constant of Ca(2+)-ATPase was increase in CRF rats compared with the other four groups of rats. The values in the latter groups were not different.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Chronic renal failure increases cytosolic Ca2+ of hepatocytes. 763 86

Chronic renal failure (CRF) is associated with increased calcium content of, and impaired lipase release from lipid cells. This has been attributed to a rise in the cytosolic calcium ([Ca2+]i) of these cells. However, data on [Ca2+]i of lipid cells in CRF and on the mechanisms responsible for such an abnormality are lacking. To study this issue we examined the [Ca2+]i and ATP content of lipid cells and Vmax of Na(+)-K(+)-ATPase and Ca2+ ATPase of membrane preparation and Na(+)-Ca2+ exchange of membrane vesicles of adipocytes from normal rats, 6 week CRF, CRF normocalcemic parathyroidectomized (CRF-PTX) and CRF, and normal rats treated with verpamil (CRF-V, normal-V). [Ca2+]i in adipocytes of CRF rats was higher (199 +/- 8.5 nM) and ATP lower (2.9 +/- 0.31 nmol/10(6) cells) than in normal (120 +/- 4.3 nM; 5.7 +/- 0.27 nmol/10(6) cells), CRF-PTX (128 +/- 4.7 nM; 5.8 +/- 0.39 nmol/10(6) cells), normal-V (121 +/- 3.2 nM; 5.3 +/- 0.36 nmol/10(6) cells), CRF-V (123 +/- 7.4 nM; 5.5 +/- 0.30 mmol/10(6) cells). Vmax Ca2+ ATPase and the activity of Na(+)-K(+)-ATPase and of Na(+)-Ca2+ exchanger were reduced in CRF rats as compared to the other four groups of rats. The values in normal, CRF-PTX, CRF-V and normal-V rats were not different.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Elevated cytosolic calcium of adipocytes in chronic renal failure. 764 31

One of the strategies used by Gram-negative bacteria to secrete proteins across the two membranes which delimit the cells is sec-independent and dedicated to proteins lacking an N-terminal signal peptide. Most of these proteins display a C-terminal secretion signal located in the last 60 amino acids (aa). Using one Erwinia chrysanthemi protease, PrtG, secreted by such a pathway it was shown that the smallest C-terminal sequence allowing efficient secretion contains the last 29 aa of PrtG and that low but significant secretion can be promoted by the last 15 aa of PrtG. Moreover, the extreme C-terminal motif, consisting of a negatively charged aa followed by several hydrophobic aa must be exposed and is conserved amongst many proteins following this pathway. This secretion system depends on ABC protein-mediated exporters, which consist of three cell envelope proteins: two inner membrane proteins, an ATPase (the ABC protein), a membrane fusion protein (MFP) and an outer membrane polypeptide. These Gram-negative bacterial protein exporters are dedicated to the secretion of one or several closely related proteins belonging to the toxin, protease and lipase families. The genes encoding the three secretion proteins and the exoproteins are usually all linked, consistent with the specificity of the systems. Er. chrysanthemi metalloproteases B and C and Serratia marcescens hemoprotein HasA are secreted by such homologous pathways and interact with the ABC protein. Interaction between the ABC protein and its substrate has also been evidenced by studies on protease and HasA hybrid transporters obtained by combining components from each system. Association between hemoprotein HasA and the three exporter secretion proteins was demonstrated by affinity chromatography on hemin agarose on which the substrate remained bound with the three secretion proteins. The three components' association was ordered and substrate binding was required for the formation of this multiprotein complex.
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PMID:Protein secretion by Gram-negative bacterial ABC exporters--a review. 922 68

The mechanism of contractile effect of vanadate was investigated in rat aortae. Sodium metavanadate (NaVO3; 10(-5)-3 x 10(-3) M) induced contractile responses in a concentration-dependent manner. Removal of endothelium did not affect the response to NaVO3. The response to NaVO3 was inhibited by nifedipine, a voltage-operated Ca2+ channel (VOC) inhibitor; NCDC, a phospholipase C inhibitor; and H-7, a protein kinase C inhibitor, but not by prazosin, an alpha1-adrenoceptor antagonist; methysergide, a serotonin-receptor antagonist; tripelennamine, a histamine-receptor antagonist; glibenclamide, an adenosine triphosphate (ATP)-dependent K+-channel inhibitor; or iberiotoxin, a large-conductance Ca2+-activated K+-channel inhibitor. In addition, genistein or tyrphostin A48, tyrosine kinase inhibitors, did not affect the contraction induced by NaVO3. Mg2+ removal or antimycin A, a Ca2+-ATPase inhibitor, did not cause any contraction. Ouabain, a Na+, K+-ATPase inhibitor, or K+-free medium caused the contraction of the aortae. The maximal contraction induced by NaVO3 plus ouabain was similar to that induced by NaVO3 alone. In addition, the response to NaVO3 was inhibited by AA861, a 5-lipoxygenase inhibitor, and RHC-80267, a diacylglycerol (DAG) lipase inhibitor. In the presence of AA861, either H-7 or nifedipine further inhibited the residual response to NaVO3. In the presence of NCDC, however, AA861 failed further to affect the residual response to NaVO3. In rat aortae, NaVO3 increased the levels of inositol monophosphate (IP) and prostaglandin F2alpha (PGF2alpha). AA861 and NCDC inhibited the IP increase. In addition, NCDC inhibited the PGF2alpha increase. These results suggest that the response to NaVO3 in rat aortae may be mainly the result of the increased phosphoinositide metabolism.
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PMID:The contractile mechanism of sodium metavanadate in isolated rat aortae. 926 25

The isolated, perfused rat mesenteric bed releases a cytochrome P450-linked metabolite of arachidonic acid (AA) as endothelium-derived hyperpolarizing factor (EDHF) in response to acetylcholine and histamine. This study assessed the relative contribution of two AA-generating pathways, phospholipase A2 (PLA2) and diacylglycerol (DAG) lipase, to EDHF-mediated dilation of the rat mesenteric bed. We tested the hypothesis that PLA2-mediated release of AA is essential for the production of EDHF. Mesenteric beds were perfused with physiological salt solution (PSS) containing indomethacin and nitro-L-arginine methyl ester to block cyclooxygenase and nitric oxide synthase, respectively, and constricted with cirazoline (an alpha1-adrenoceptor agonist). Bolus applications of acetylcholine and histamine caused dose-dependent dilation of the constricted beds. The 85-kDa PLA2 inhibitor, arachidonyl trifluoromethyl ketone (AACOCF3), at 3 microM, profoundly blunted decreases in perfusion pressure initiated by 1 nmol acetylcholine (94.3+/-1.7%) and by 100 nmol histamine (88.5+/-3.3%) to 9.6+/-7.5 and 8.6+/-6.0%, respectively. AACOCF3 also blocked cirazoline-stimulated release of 6-keto-PG1alpha, but did not alter the vasodilation initiated by sodium nitroprusside (a nitric oxide donor), cromakalim (a K+ channel activator), or by Na+/K+-ATPase activation, as measured by KCl vasodilation in preconstricted beds perfused with K+-free PSS. The 14-kDa PLA2 inhibitor, oleyloxyethyl phosphorylcholine, also blocked EDHF vasodilation and also significantly inhibited K+ channel activity. Neither the Ca2+-independent PLA2 inhibitor, HELSS [E-6-(bromomethylene)-tetrahydro-3-(1-naphthalenyl)-2H-pyran-2-one], nor DAG lipase inhibitor, RHC-80267 [1,6-bis-(cyclohexyloximino-carbonylamino)-hexane] altered EDHF-mediated vasodilation. However, RHC-80267 blocked cirazoline-stimulated release of 6-keto-PGF1alpha. We conclude that Ca2+-dependent PLA2, rather than DAG lipase, generates the AA for the production of EDHF in the perfused rat mesenteric bed.
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PMID:Calcium-dependent phospholipase A2 mediates the production of endothelium-derived hyperpolarizing factor in perfused rat mesenteric prearteriolar bed. 948 93


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