Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Electron spin resonance, enzymatic, and SDS-polyacrylamide gel electrophoretic investigations of erythrocyte membranes from patients with Alzheimer's disease were performed. Alterations in the physical state of membrane proteins in Alzheimer's disease erythrocytes were found by spin labeling studies. However, no alterations in membrane lipid fluidity or in the activities of membrane-bound sodium plus potassium-stimulated, magnesium-dependent adenosine triphosphatase or acetylcholinesterase could be demonstrated. Also, no changes in staining profiles of AD erythrocyte membrane proteins subjected to electrophoresis were observed. The altered conformation and/or organization of extraneural membrane proteins in Alzheimer's disease suggests the possibility that this disorder may have more widespread membrane involvement than was originally thought.
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PMID:Spin label and biochemical studies of erythrocyte membranes in Alzheimer's disease. 624 87

The distribution pattern of cholinesterase, alkaline and acid phosphatases, adenosine triphosphatase and succinic dehydrogenase in the various cellular constituents of the gustatory epithelium, taste buds and lingual glands of the rat was subjected to a detailed histochemical study. An attempt was made to explain the structural and functional relationship on the basis of the distribution of the enzymes in these regions of the rat tongue.
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PMID:Histochemical distribution and functional role of phosphatases, cholinesterase and succinic dehydrogenase in the gustatory epithelium and lingual glands of the rat. 644 28

Muscle spindles were examined histochemically in serial transverse sections of cat tenuissimus muscles. The myofibrillar adenosine triphosphatase (ATPase) staining reaction was used to identify nuclear bag1, bag2 and nuclear chain intrafusal muscle fibers. Regional differences in ATPase staining occurred along the bag1 and bag2 fibers but not along the chain fibers. All intrafusal fiber types displayed regional variability in staining for nicotinamide adenine dinucleotide tetrazolium reductase (NADH-TR). Motor nerve terminals were demonstrated along the poles of bag1, bag2 and chain fibers by staining for cholinesterase (ChE). There was no consistent spatial correlation between the intensity of regional ATPase staining along the bag fibers and location, number or type of motor endings. However, most ChE deposits occurred in intrafusal fiber regions that displayed the greatest NADH-TR variability. Some fiber poles or whole intrafusal fibers were devoid of any ChE deposits but their ATPase and NADH-TR content was comparable to that of fibers bearing ChE deposits. The observations suggested that motor nerve fibers per se may not play a major role in determining the histoenzymatic content of intrafusal fibers.
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PMID:Histochemical profiles of cat intrafusal muscle fibers and their motor innervation. 646 12

Muscle spindles were studied histochemically in serial transverse sections of 42 cat tenuissimus muscle specimens. Staining for myofibrillar adenosine triphosphatase was employed to identify nuclear bag 1, nuclear bag 2, and nuclear chain intrafusal muscle fibers. The nuclear chain fibers were further subdivided into three categories according to their polar length and the intensity of their staining for nicotinamide adenine dinucleotide tetrazolium reductase. A total of 430 spindle poles were surveyed. The mean spindle content of bag 1, bag 2, and chain fibers was established. The mean polar length of intrafusal fibers as well as that of the intracapsular and extracapsular spindle regions was determined. A cholinesterase (ChE) staining technique was used to demonstrate the termination sites of motor axons along intrafusal fibers. Two types of circumscribed ChE deposits. The "rim" and the "plate," occurred on the fibers. The nuclear chain fibers usually carried both the ChE rims and plates, while most nuclear fibers displayed only the plates. The ChE plates were assessed in term of their appearance, staining intensity, length, and location along the fibers. The mean number of ChE plates found along the fibers was established for each of the various intrafusal fiber types. These histochemical observations are discussed with regard to the current concepts of cat spindle morphology and motor innervation. The results suggest a degree of predictability in the spindle fiber content and in the distribution of motor nerve terminals along intrafusal muscle fibers, at least in the tenuissimus muscle.
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PMID:Morphometric studies on tenuissimus muscle spindles in the cat. 646 Aug 72

Cat tenuissmus muscles were deprived of motor nerve supply for three months by sectioning of the appropriate ventral spinal roots. Muscle spindles were located in the chronically de-efferented muscles and examined histochemically in serial transverse sections. Staining for nicotinamide adenine dinucleotide tetrazolium reductase showed that the spindle sensory innervation was preserved. The de-efferented intrafusal muscle fibers retained their differential staining with the reaction for myosin adenosine triphosphatase. However, all cholinesterase-active areas that are normally found along nuclear bag and nuclear chain intrafusal fibers demonstrated loss of the enzyme activity in the chronically de-efferented spindles. It is concluded that all histochemically demonstrable cholinesterase activity within the cat muscle spindle is dependent upon the continuous presence of motor innervation.
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PMID:Examination of chronically de-efferented cat muscle spindles for cholinesterase activity. 706 45

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.
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PMID:Motor innervation of the cat muscle spindle studied by the cholinesterase technique. 739 81

Lipid composition, fluidity, and Na+,K(+)-adenosine triphosphatase (ATPase), Mg(2+)-ATPase, and acetylcholinesterase (AChE) activities of erythrocyte membranes were examined in comparison to plasma lipid composition and lecithin:cholesterol acyltransferase (LCAT) activities in 39 patients with hepatic cirrhosis due to viral hepatitis (Child-Pugh class A, n = 12; class B, n = 13; and class C, n = 14). Plasma LCAT activities decreased and the plasma free-cholesterol to phospholipid molar ratio (C/PL) increased with progressive severity of hepatic cirrhosis. C/PL and fluorescence polarization (inverse of fluidity) of erythrocyte membranes also increased with disease progression (C/PL: Child-Pugh A, 0.911 +/- 0.010; B, 0.941 +/- 0.011; C, 0.979 +/- 0.028; and normal, 0.798 +/- 0.010; fluorescence polarization: Child-Pugh A, 0.348 +/- 0.002; B, 0.351 +/- 0.002; C, 0.355 +/- 0.002; and normal, 0.340 +/- 0.002). There was a correlation between C/PL and fluorescence polarization of erythrocyte membranes (r = .629, P < .001). Na+,K(+)-ATPase activity of erythrocyte membranes did not differ between cirrhotic patients and normal subjects. On the other hand, Mg(2+)-ATPase activity decreased in Child-Pugh C cirrhosis. AChE activity was decreased in Child-Pugh A cirrhosis, and decreased further in Child-Pugh B and C cirrhosis. AChE and Mg(2+)-ATPase activities correlated inversely with fluorescence polarization (r = -.652, P < .001 and r = -.381, P < .01, respectively).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Altered lipid composition and differential changes in activities of membrane-bound enzymes of erythrocytes in hepatic cirrhosis. 761 39

Isatin (10 microM) strongly inhibited the activity of rat brain monoamine oxidase-B (MAO-B) in vitro. At millimolar concentrations (1-10 mM) it inhibited brain acetylcholinesterase (AChE) and sodium, potassium-adenosine triphosphatase (Na+, K(+)-ATPase) activity also. However, isatin did not affect these enzymes after both acute and chronic treatments in vivo. Administration of isatin to rats at 300 mg/kg body weight for 2 and 6 h significantly raised brain serotonin levels. Chronic treatment for 20 days resulted in enhanced brain glycolipids and plasmalogen levels. There was no change in the levels of 5-hydroxy indole acetic acid (5 HIAA), phospholipids, cholesterol and gangliosides under these conditions.
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PMID:In vivo effects of isatin on certain enzymes, lipids & serotonergic system of rat brain. 782 61

Thiobencarb (S-(4-chlorobenzyl)-N,N-diethyl thiol carbamate), a dithiocarbamate herbicide, was found to cause neuronal dysfunction in adult and neonate albino rats. In general, organocarbamates exert their action by inhibiting acetylcholinesterase (AChE) activity. Thiobencarb inhibited both acetylcholinesterase and adenosine triphosphatase (ATPase) activities in rat brain. Withdrawal of thiobencarb treatment resulted in the recovery of AChE activity to a normal level, whereas there was no recovery of Na(+)-K(+)-ATPase activity in either neonate or adult rat brains. The results suggest that neuronal dysfunction caused by thiobencarb is mainly due to the inhibition of ATPase activity rather than to the inhibition of AChE activity.
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PMID:Comparative study on the changes in AChE and ATPase activities in neonate and adult rat brains under thiobencarb stress. 844 Aug 73

Little information is available on the structure-central nervous system membrane toxicity relationship of alcohols. The purpose of the present study was to study in vitro influence of alcohols (n = 20) on the activity of the toxic indicator Na+/K(+)-adenosine triphosphatase (Na+/K(+)-ATPase) and acetylcholinesterase (AchE), and membrane fluidity in mouse brain synaptosomes, in terms of the structure-activity relationship. The potency of inhibition for the enzymes (IC50) and the potency of increasing membrane fluidity (IC12.5) were determined experimentally, and n-octanol/water partition coefficient (P) and the steric constant Taft Es are cited from the literature. Regression analysis revealed that log 1/IC50 for Na+/K(+)-ATPase is a function of log P and Taft Es. The situation was true for AchE activity. The results indicate that the hydrophobicity expressed as log P and the steric effect of the alcohols play an important role in inhibiting both enzyme activities. A linear relationship between log 1/IC12.5 for membrane fluidity and log P is shown, indicating a significant effect of the alcohols on membrane fluidity. Based on these results, it is suggested that the alcohols inhibit the Na+/K(+)-ATPase and AchE activity through a direct action on the enzymes and/or through changing the membrane fluidity.
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PMID:In vitro influences of alcohols on mouse synaptosomes, and structure-activity relationships. 866 Jan 39


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