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:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

K+-dependent phosphatase and Mg2+, Na+, K+-ATPase were studied under the activating effect of surfactant homologs of the alkyl sulphate series with the hydrocarbon radical long chain C4-C15. The homologs are shown to activate the enzymes when they are in the molecular-disperse but not in micellar state. A clear regularity is observed in the effect of these surfactants on K+-phosphatase depending on the length of the hydrocarbon radical chain: the degree of the activating effect rises with the chain lengthening, reaching the maximum value when the number of carbon atoms is 12. The lower and upper bounds of the alkyl sulphate hydrocarbon radical chain length necessary for manifestation of the activating effect shift somewhat for K+-dependent phosphatase as compared with Mg2+, Na+, K+-ATPase. The data obtained evidence for a stronger stability of the phosphatase to a destructive effect of the surfactants as compared with transport ATPase.
...
PMID:[Activation of brain K+-phosphatase and Mg2+, Na+, K+-AtPase by sodium alkyl sulfates]. 626 11

Adenine nucleotide translocase (EC 3.6.1.3.), pyruvate dehydrogenase (active and total forms, EC 1.2.4.1) and the long chain acyl CoA content were measured in liver and kidney from normal and alloxan-diabetic rats. The long chain acyl CoA content was significantly increased in liver, but not in kidney, in the diabetic group. Adenine nucleotide translocase activity was decreased in liver and raised in the kidney of alloxan-diabetic rats relative to the control group. Pyruvate dehydrogenase (active) was inhibited to a similar degree in both tissues in diabetes. The results are discussed in the light of the possible regulatory role of long chain acyl CoA and the diverse metabolic demands of the two tissues in diabetes.
...
PMID:Differential response of liver and kidney adenine nucleotide translocase and pyruvate dehydrogenase activity to alloxan diabetes. The possible regulatory role of long chain acyl CoA. 630 7

The accumulation of long chain of acyl carnitine, which is thought to exaggerate myocardial ischemic damage, has been demonstrated in ischemic myocardium. The purpose of this study was to determine the effect of palmitoyl carnitine on the Na+, K+-ATPase and adenylate cyclase activity of myocardial sarcolemma in vitro. Controversial views exist at present regarding the effect of palmitoyl carnitine on Na+, K+-ATPase. Wood et al. [23] observed that palmitoyl carnitine inhibited the activity of Na+, K+-ATPase but this inhibition was not observed by Owens et al. [17]. We did observe an inhibition of Na+, K+-ATPase by palmitoyl carnitine. The 50% inhibition of the maximum activity was observed at a palmitoyl carnitine concentration of 110 microM and complete inhibition at 160 microM. Adenylate cyclase activity was inhibited by palmitoyl carnitine irrespective of the assay conditions. The (isoproterenol + GTP)-stimulated activity, fluoride-stimulated activity and basal activity with Mg-ATP or Mn-ATP as a substrate were all inhibited though to varying degrees. The 50% inhibition of adenylate cyclase activity was observed at 84 microM, 94 microM, 200 microM and 105 microM of palmitoyl carnitine in the above mentioned order. The inhibition curve showed a shoulder or even a peak at about 75 microM of palmitoyl carnitine. It is suggested that elevated levels of palmitoyl carnitine in ischemic myocardium may play a role in inhibiting sarcolemmal function.
...
PMID:Effect of palmitoyl carnitine on Na+, K+-ATPase and adenylate cyclase activity of canine myocardial sarcolemma. 632 16

Cat intrafusal muscle fibers were examined histochemically in serial transverse sections of tenuissimus muscle spindles. The "myofibrillar" adenosine triphosphatase staining reaction was used to recognize the nuclear bag and the nuclear chain fibers in 309 spindle poles. Poles of 40 nuclear chain fibers extended for 1,000 micrometer or more beyond the termination of the spindle capsule. These long chain fibers stained less intensely for nicotinamide adenine dinucleotide tetrazolium reductase (NADH-TR) than the typical chain fibers of shorter polar length. In sections stained for cholinesterases (ChE), the extracapsular regions of most long chain fibers displayed one or two short, dense "plate"-type ChE deposits, which may represent the terminals of skeleto-fusimotor axons. In addition, about one-third of the long chain fibers displayed one or more thinner and smaller areas of ChE activity, possibly corresponding to the endings of fusimotor axons. The overall ChE staining pattern of the typical chain fibers was unlike that of the long chains. However, some of the shorter nuclear chain fibers resembled long chain fibers with the NADH-TR reaction, even though their ChE "plates" were located intracapsularly. It is concluded that nuclear chain fibers in the cat spindle form a class of intrafusal fibers with heterogeneous histochemical properties, and that the long chain fibers represent one fiber subtype.
...
PMID:Histochemical study of long nuclear chain fibers in the cat muscle spindle. 645 71

Isolated working hearts from diabetic rats have a decreased ability to respond to increasing preload or afterload. The ability of cardiac sarcoplasmic reticulum to transport Ca2+ was examined in diabetic rats. Hearts were obtained from female Wistar rats 120 days or 7 days after the induction of diabetes by a single I.V. injection of either alloxan (65 mg/kg) or streptozotocin (60 mg/kg). At all Ca2+ concentrations tested (0.2-5.0 microM free Ca2+) cardiac sarcoplasmic reticulum from 120-day diabetic rats showed a significant decrease in the rate of ATP-dependent tris-oxalate facilitated Ca2+ transport (62-73% of control). This was accompanied by a decrease in Ca2+ ATPase activity. The levels of long chain acylcarnitines associated with the microsomal sarcoplasmic reticulum preparation from 120-day diabetic rats were significantly higher than those present in sarcoplasmic reticulum from control rats. Palmitylcarnitine, the most abundant of the long chain acylcarnitines, in concentrations less than 7 microM was found to be a potent time-dependent inhibitor of Ca2+ transport in both control and diabetic rat sarcoplasmic reticulum preparations; inhibition of Ca2+ transport was found to be more marked in the control preparations. This would indicate that a degree of inhibition produced by the high endogenous levels of palmitylcarnitine may already be present in the diabetic rat preparations. Cardiac sarcoplasmic reticulum prepared from acutely diabetic rats (7 days) did not show any decrease in Ca2+ transport ability. Levels of long chain acylcarnitines associated with the microsomal preparation enriched in sarcoplasmic reticulum were also unchanged. These findings suggest that the alteration in heart function in 120-day diabetic rats may be due to the buildup of cellular long chain acylcarnitines which inhibit sarcoplasmic reticulum Ca2+ transport. The absence of any change in Ca2+-transport activity or levels of long chain acylcarnitines at 7 days suggests that the alterations seen in 120-day diabetic rats must be of gradual onset.
...
PMID:The effect of alloxan- and streptozotocin-induced diabetes on calcium transport in rat cardiac sarcoplasmic reticulum. The possible involvement of long chain acylcarnitines. 688 99

Muscle spindles were traced in serial transverse sections of cat tenuissimus muscles. "Myofibrillar" adenosine triphosphatase staining reaction was used to identify nuclear bag1, nuclear bag2 and nuclear chain intrafusal muscle fibers. Typical chain fibers and long chain fibers were distinguished, the latter extending for more than 1,000 micron beyong the termination of the spindle capsule. Simple "rim" and more elaborate "plate" deposits were demonstrated histochemically along the poles of the typical chain fibers in staining for cholinesterases. They were considered to correspond, respectively, to the trail and plate motor nerve terminals. Most long chain fibers and the majority of nuclear bag fibers had their motor innervation limitd to "plate"-type endings. In addition, faint diffuse cholinesterase staining occurred along the spindle capsule and the surface of some intrafusal fibers. These histochemical observations are discussed with regard to the current concepts concerning the morphological and functional organization of the motor innervation of the cat muscle spindle.
...
PMID:Motor innervation of the cat muscle spindle studied by the cholinesterase technique. 739 81

Chicken gastrin has a C-terminal sequence resembling mammalian cholecystokinin, but its biological properties resemble mammalian gastrin. The mechanisms controlling chicken gastrin release are poorly understood. We have investigated the factors which influence chicken gastrin secretion in vivo. Plasma gastrin concentration was decreased within 12 h of fasting, but tissue gastrin concentrations were not significantly changed even after 24 h of food deprivation. In birds fasted for 24 h and treated with the H+/K(+)-ATPase inhibitor, omeprazole, plasma gastrin concentration was greatly enhanced indicating the importance of acid inhibition of the gastrin cell. It is well established that amino acids (particularly aromatics like Phe and Trp) and peptides stimulate gastrin release in mammals. In chicken, however, Met, His and Arg were the strongest stimulant amongst the essential amino acids investigated. Of these three amino acids, Met rapidly stimulated gastrin release. The GRP antagonist M216140 did not suppress the Met-induced gastrin release, suggesting that Met did not stimulate GRP release. Aromatic amino acids did not strongly influence gastrin release. Medium chain triacylglycerol, which is rapidly hydrolyzed to fatty acids in the lumen, strongly stimulated gastrin secretion but long chain triacylglycerol had no effect. The data suggest that amino acids (Met, Arg and His) and fatty acids, but not triacylglycerol, are gastrin releasing factors in birds while acid inhibits secretion: there are therefore both similarities and differences between birds and mammals in the control of gastrin release.
...
PMID:The regulation of gastrin secretion in the chicken. 776 24

The Na+,K(+)-ATPase is an important enzyme in determining the ionic milieu of the cerebromicrovasculature and neurons. The effect of hypertension or aging on this enzyme, as well as its susceptibility to regulation by fatty acids or aluminum, is the focus of this study. A significant increase (34%) in the apparent affinity constant (KD) but no change in the maximum binding capacity (Bmax) for [3H]ouabain binding to the cerebromicrovascular Na+,K(+)-ATPase occurs after induction of acute hypertension. In addition, long chain unsaturated fatty acids stimulate the binding of [3H]ouabain to the enzyme in microvessels from normotensive and hypertensive rats. The synaptosomal Na+,K(+)-ATPase is sensitive to aluminum. AlCl3 (1-100 microM) inhibits the K(+)-dependent-p-nitrophenylphosphatase (K(+)-NPPase) activity of the Na+,K(+)-ATPase in a dose-dependent manner. AlCl3 (100 microM) decreases the Vmax by 14% but does not alter the KM, suggestive of non-competitive inhibition. The enzyme from aged brain displays a greater Vmax, but shows the same susceptibility to AlCl3 as the enzyme from younger brain. In summary, disruption of the Na+,K(+)-ATPase may underlie, at least in part, abnormalities of nerve and vascular cell function in disorders where elevated concentrations of fatty acids or metal ions are involved.
...
PMID:Control of the Na+,K(+)-ATPase under normal and pathological conditions. 810 35

The influence of dietary (n-3) fatty acids (such as eicosapentaenoic and docosahexaenoic acids) as found in fish oil on Na+ sensitivity and ouabain affinity of Na+,K(+)-ATPase isoenzymes (alpha 1, alpha 2, alpha 3) was studied in whole brain membranes from weaned and adult rats fed diets for two generations. The long chain (n-3) fatty acids supplied by fish oil decreased the fatty acids of the (n-6) series compared with the standard diet, resulting in a decrease in the (n-6)/(n-3) molar ratio in both 21- and 60-day-old rats. On the basis of ouabain titration, three inhibitory processes with markedly different affinities were associated with isoenzymes, i.e., low affinity (alpha 1), high affinity (alpha 2), and very high affinity (alpha 3). It appears that the fish oil diet, in part via the modification of membrane fatty acid composition, altered the proportion and ouabain affinity of isoenzymes. Na+ sensitivity is the best criterion of physiologic change induced by fish oil diet. We calculated the Na+ activation for each isoenzyme and found one Na+ sensitivity and two Na+ sensitivities per isoenzyme in weanling and adult rats fed different diets, respectively. In contrast to alpha 2 and alpha 3, alpha 1 appears insensitive to membrane change induced by fish oil diet. Fish oil diet, which is known to confer cardioprotection, induced significant modulation of Na+,K(+)-ATPase isoenzymes at the brain level.
...
PMID:Effect of fish oil diet on fatty acid composition of phospholipids of brain membranes and on kinetic properties of Na+,K(+)-ATPase isoenzymes of weaned and adult rats. 813 84

We have characterized the effects of hypoxia on carnitine metabolism in proximal tubules. Hypoxia for 10 minutes resulted in a significant increase in the mass of long chain acylcarnitines (LCAC) (control 53 +/- 20 vs. hypoxia 118 +/- 38 pmol. mg-1 protein). Since LCAC are proximal metabolites in the beta-oxidation of fatty acids, these data suggest that inhibition of fatty acid oxidation occurs during hypoxia in the proximal tubule. In addition to LCAC accumulation, hypoxia resulted in a significant increase in the mass of lysoplasmenylcholine LPLasCho (control 62 +/- 15 pmol/mg vs. 20 min hypoxia 146 +/- 21 pmol/mg protein, N = 4) and also in increases in the mass of monoacyl LPC (control 122 +/- 24 pmol/mg protein vs. 283 +/- 35 pmol/mg protein after 40 min of hypoxia). We tested the possibility that these compounds that accumulate during hypoxia could inhibit proximal tubule Na+, K(+)-ATPase. LPC, LPlasC, and LCAC inhibited proximal tubule nystatin-stimulated oxygen consumption (QO2) and proximal tubule Na+, K(+)-ATPase activity in a dose-dependent manner. In addition, LPC, LPlasC, and LCAC directly inhibited' (65%, 80%, and 60%, respectively) Na+, K(+)-ATPase activity purified from kidney cortex at similar concentrations at which they accumulate during hypoxia (above 25 microM). The present data suggest that amphiphile accumulation may have a potential pathophysiologic role in the proximal tubule during renal ischemia.
...
PMID:Hypoxia-induced amphiphiles inhibit renal Na+, K(+)-ATPase. 873 Oct 93


<< Previous 1 2 3 4 5 Next >>

---