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)

The subsynaptosomal distribution of the borohydride stabilizable binding of serotonin (5-HT) in the brain was investigated using various enzyme markers, such as NAD glycohydrolase (NADase), Na+, K+-activated ATPase for synaptic membranes, and monoamine oxidase (MAO) for outer mitochondrial membranes. The gross distribution of the activity of NADase and Na+, K+-activated ATPase in various membrane fractions was found to parallel the distribution of 5-HT binding in these fractions. Radioactivity bound to brain fractions was extractable with chloroform-methanol (2:1). The membranous material was solubilized by chloroform-methanol (2:1) and the recovered material, suspended in 0.32 M sucrose was found to retain its 5-HT binding capacity. The protein-phospholipid nature of the binding subcellular macromolecule was demonstrated with proteolytic and lipolytic enzymes.
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PMID:Subsynaptosomal localization and biochemical characterization of serotonin binding sites in the brain. 18 52

We have undertaken the analytical fractionation of epithelial cells from toad urinary bladder, a tissue extensively used to study epithelial transport of ions and water. In an attempt to establish markers for the main subcellular organelles, a number of enzymes were assayed in cell homogenates. The nearly ubiquitous plasma membrane marker 5'-nucleotidase, and the transferases that donate N-acetylglucosaminyl, galactosyl, and sialyl residues to glycoproteins and glycolipids in the Golgi complex were not detectable. Glucose-6-phosphatase activity was low in relation to that of nonspecific phosphatases and, therefore, not suitable for identifying the endoplasmic reticulum. Like the cytosolic enzyme lactate, dehydrogenase, catalase was essentially found in the high-speed supernatant, with a noteworthy part of aminopeptidase (substrate, leucyl-beta-naphthylamide) and NAD glycohydrolase. Other enzymes, including cytochrome c oxidase, acid phosphatase, acid N-acetyl-beta-glucosaminidase, alkaline phosphatase, alkaline phosphodiesterase I, nucleoside diphosphatase (substrate ADP), oligomycin-resistant Mg++-ATPase, and mannosyltransferase (acceptor, dolichylphosphate) were fairly active and largely sedimentable. After differential centrifugation, cytochrome oxidase, acid phosphatase, and acid N-acetyl-beta-glucosaminidase were typically associated with the large granule fraction, whereas the other sedimentable enzymes exhibited a broad distribution profile overlapping the nuclear, large granule, and microsome fractions. Their behavior in density equilibrium centrifugation is examined in a companion paper.
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PMID:Subcellular fractionation of epithelial cells from toad urinary bladder. 1. Assay of marker enzymes and differential centrifugation. 250 71

Purified plasma membranes were obtained from five transplantable human tumors, a grade IV astrocytoma, an oat cell carcinoma, and three melanomas. Plasma membrane fractions were isolated from tumor homogenates by differential and discontinuous sucrose gradient centrifugation. Determination of enzyme activities indicated that the plasma membranes were enriched 10- to 20-fold with respect to 5'-nucleotidase, nicotinamide adenine dinucleotide glycohydrolase, Mg2+-activated nucleoside triphosphatase, and sialic acid. Specific activities of nearly all the enzymes varied with the individual tumors, even among tumors of the same type, i.e., the melanomas. Electron micrographs of the plasma membrane fractions showed smooth single-membrane vesicles with slight contamination by lysosomes. Therefore, these membranes are suitable for comparative biochemical studies and for the preparation of tumor-specific monoclonal antibodies. Plasma membranes from all five tumors contained very high Mg2+-adenosine triphosphatase (ATPase) activities. The Na+-K+-ATPase was a minor component of the total ATPase of these membranes (less than 30%). The major component was an ATPase exhibiting similar activity toward several nucleoside triphosphates. The activity of such a nucleoside triphosphatase has been correlated with tumorigenicity in cultured liver epithelial cells. The nucleoside triphosphatase of the plasma membranes of astrocytoma and oat cell carcinoma was stimulated from 50 to 1005 by concanavalin A, whereas ATPase of the melanoma plasma membranes was not or only slightly stimulated. The different response to concanavalin A could be due to differences in the ATPase molecules of the individual tumors or to the different environment of the ATPase.
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PMID:Isolation and characterization of plasma membranes from transplantable human astrocytoma, oat cell carcinoma, and melanomas. 611 38

The vertebrate corneal endothelium represents a unique model system for investigating many cellular aspects of wound repair within an organized tissue in situ. The tissue exists as a cell monolayer that resides upon its own natural basement membrane that can be prepared as a flat mount to observe the entire cell population. Thus, it readily avails itself to many cytological and immunocytochemical methods at both the light microscopic and ultrastructural levels. In addition, the tissue is easily explanted into organ culture where further investigations can be carried out. These techniques have enabled investigators to use many approaches to explore function and changes in response to injury. In vivo, the endothelium acts as a transport tissue to actively pump Na+ and bicarbonate ions from the corneal stroma into the aqueous humor to control corneal transparency. Physiological findings indicate that fluid diffuses back into the stroma, across the endothelium, and thus hydration is said to be controlled by a pump-leak mechanism. Ultrastructural investigations, some employing horseradish peroxidase and lanthanum, have established the morphological basis for this mechanism as apical focal junctions that are not the classical tight junctions and do not constitute a complete zona occludens. Along with these apical focal junctions are gap junctions that appear identical to their counterparts in other cell types. Cytochemical studies localized both Na+K(+)-ATPase and carbonic anhydrase, the main pump enzymes associated with corneal hydration, to the lateral plasma membranes. Corneal endothelial cells of noninjured tissue do not traverse the cell cycle and are considered to be in the "Go" phase of the cell cycle as determined by microfluorometric analysis with DNA binding dyes such as auramin O and pararosaniline-Feulgen. However, injury can initiate cell cycle transverse and histochemical and cytological methods have been used to understand the tissue's response. Classical histochemical studies revealed that increased staining was observed for metabolic (NADase and NADPase) and lysosomal enzymes in cells bordering the wound area. The use of radiolabelled agents has further lead to an understanding of the endothelial wound response. Autoradiographic analyses of 3H-actinomycin D incorporation indicated that injury initiates changes in chromatin leading to increased binding levels of the drug in cells surrounding the wound. This change suggests that those cells undergo heightened macromolecular synthesis and this was confirmed by examining 3H-uridine and 3H-thymidine incorporation. The major mechanism involved in corneal endothelial repair is cell migration. Cytochemical and immunocytochemical investigations have allowed investigators an opportunity to gain some insight into changes that occur during this cellular process.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Cytological and immunocytochemical approaches to the study of corneal endothelial wound repair. 805 65

Snake envenomation employs three well integrated strategies: prey immobilization via hypotension, prey immobilization via paralysis, and prey digestion. Purines (adenosine, guanosine and inosine) evidently play a central role in the envenomation strategies of most advanced snakes. Purines constitute the perfect multifunctional toxins, participating simultaneously in all three envenomation strategies. Because they are endogenous regulatory compounds in all vertebrates, it is impossible for any prey organism to develop resistance to them. Purine generation from endogenous precursors in the prey explains the presence of many hitherto unexplained enzyme activities in snake venoms: 5'-nucleotidase, endonucleases (including ribonuclease), phosphodiesterase, ATPase, ADPase, phosphomonoesterase, and NADase. Phospholipases A(2), cytotoxins, myotoxins, and heparinase also participate in purine liberation, in addition to their better known functions. Adenosine contributes to prey immobilization by activation of neuronal adenosine A(1) receptors, suppressing acetylcholine release from motor neurons and excitatory neurotransmitters from central sites. It also exacerbates venom-induced hypotension by activating A(2) receptors in the vasculature. Adenosine and inosine both activate mast cell A(3) receptors, liberating vasoactive substances and increasing vascular permeability. Guanosine probably contributes to hypotension, by augmenting vascular endothelial cGMP levels via an unknown mechanism. Novel functions are suggested for toxins that act upon blood coagulation factors, including nitric oxide production, using the prey's carboxypeptidases. Leucine aminopeptidase may link venom hemorrhagic metalloproteases and endogenous chymotrypsin-like proteases with venom L-amino acid oxidase (LAO), accelerating the latter. The primary function of LAO is probably to promote prey hypotension by activating soluble guanylate cyclase in the presence of superoxide dismutase. LAO's apoptotic activity, too slow to be relevant to prey capture, is undoubtedly secondary and probably serves principally a digestive function. It is concluded that the principal function of L-type Ca(2+) channel antagonists and muscarinic toxins, in Dendroaspis venoms, and acetylcholinesterase in other elapid venoms, is to promote hypotension. Venom dipeptidyl peptidase IV-like enzymes probably also contribute to hypotension by destroying vasoconstrictive peptides such as Peptide YY, neuropeptide Y and substance P. Purines apparently bind to other toxins which then serve as molecular chaperones to deposit the bound purines at specific subsets of purine receptors. The assignment of pharmacological activities such as transient neurotransmitter suppression, histamine release and antinociception, to a variety of proteinaceous toxins, is probably erroneous. Such effects are probably due instead to purines bound to these toxins, and/or to free venom purines.
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PMID:Ophidian envenomation strategies and the role of purines. 1173 31

In this study, the consequences of modification of human erythrocyte membrane sulfhydryl groups by N-ethyl maleimide (NEM), 5,5'dithiobis-(2-nitrobenzoic acid) (DTNB) andp-hydroxymercuriphenyl sulfonate (PHMPS) were investigated. These reagents differ in chemical reactivity, membrane penetrability and charge characteristics.Results of sulfhydryl modification were analyzed in terms of inhibitory effects on activities of five membrane enzymes; Mg(++)- and Na(+), K(+)-ATPase, K(+)-dependent and independentp-nitrophenyl phosphatase (NPPase) and DPNase. Structural considerations involved in the sulfhydryl-mediated inhibition were evaluated by studying the changes in susceptibility to sulfhydryl alteration produced by shearing membranes into microvesicles and by the addition of the membrane modifiers, Mg(++) and ATP.Conclusions from the data suggest that the effects of NEM appeared to result from modification of a single class of sulfhydryls; DTNB interacted with two different sulfhydryl classes. Increasing concentrations of PHMPS resulted in the sequential modification of many types of sulfhydryls, presumably as a result of increasing membrane structural disruption. DTNB and PHMPS caused solubilization of about 15% of membrane protein at concentrations giving maximal enzyme inhibition.In contrast to the usually observed parallels between Na(+), K(+)-ATPase and K(+)-dependent NPPase, activities of Mg(++)-ATPase, Na(+), K(+)-ATPase and K(+)-dependent NPPase varied independently as a result of sulfhydryl modification. We suggest complex structural and functional relationships exist among these components of the membrane ATP-hydrolyzing system.Our studies indicate that the effects of sulfhydryl group reagents on these membrane systems should not be ascribed to sulfhydryl modificationper se, but rather to the resulting structural perturbations. These effects depend upon the structural characteristics of the particular membrane preparation studied and on the chemical characteristics of the sulfhydryl group reagent used.
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PMID:Modification of the erythrocyte membrane by sulfhydryl group reagents. 2417 12