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

Ultrastructural localization of Na+,K+-ATPase in rat ciliary epithelium was investigated quantitatively by the protein A-gold technique, using an affinity-purified antibody against the alpha-subunit of Na+,K+-ATPase. Immunoblot analysis showed that the antibody bound specifically to the alpha-subunit of Na+,K+-ATPase in the ciliary body. Gold particles were found mainly on the basolateral surfaces of both the pigmented epithelial (PE) and nonpigmented epithelial (NPE) cells with an approximately twofold higher labeling density in the PE cells. A few gold particles were also found on the apical and ciliary channel surfaces of the PE cells, whereas no significant binding was found on the apical surfaces of the NPE cells. The basolateral surfaces of PE and NPE cells are markedly infolded and are much greater in area than the apical surfaces. This means that Na+,K+-ATPase is almost exclusively located on the basolateral surfaces of both the NPE and PE cells. We suggest that the Na+,K+-ATPase of both the NPE and PE cells play an important role in the formation of aqueous humor.
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PMID:Quantitative immunocytochemical localization of Na+,K+-ATPase in rat ciliary epithelial cells. 254 22

The secretion of the aqueous humor has been proposed to occur as the result of active Na+ transport by a ouabain-sensitive Na-K ATPase. We have examined the localization of this enzyme in the epithelium of rabbit ciliary body pars plicata using [3H]ouabain autoradiography. Single ciliary processes were isolated and incubated in Ringer containing [3H]ouabain. Processes were then rapidly frozen, freezedried, sectioned and exposed for autoradiography. In the light microscope, silver grains were found predominantly over the nonpigmented epithelial cells. In the electron microscope, grains could be localized for the most part to the interdigitations of the nonpigmented cell basolateral membrane. Label could also be observed at a much lower density above other membranes and above the pigmented and nonpigmented cell cytoplasm. No label was found in sections of control tissue which had been incubated in [3H]ouabain with an excess of cold ouabain. To show that the [3H]ouabain had free access to all of the membrane surfaces within the epithelium, in parallel experiments we incubated isolated processes in horseradish peroxidase. Our experiments suggest that most of the active Na+ transport in ciliary body epithelium occurs across the basolateral membrane of nonpigmented cells into the posterior chamber. Furthermore, the placement of the Na-K ATPase within the narrow membrane infoldings of the interdigitations is consistent with a role for this enzyme in water transport and the production of the aqueous.
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PMID:[3H]ouabain localization of Na-K ATPase in the epithelium of rabbit ciliary body pars plicata. 283 60

In many tissues, the level of cytoplasmic calcium mediates cell function. Since cytoplasmic calcium is often maintained at a low level by active calcium extrusion, we examined whether calcium-stimulated ATPase is present in the rabbit ciliary epithelium. A technique was developed to measure calcium-stimulated ATPase in a partially enriched plasma membrane preparation. The enhancement of Na,K-ATPase activity was used to indicate the enrichment of plasma membrane. Marked stimulation of ATPase activity by calcium was observed over a range of calcium concentrations (10(-8) to 10(-3) M). The calcium concentration necessary to elicit half-maximal ATPase activity was 10(-6) M, which is similar to that reported for other membrane preparations. Calcium-stimulated ATPase activity was significantly inhibited in the presence of low concentrations of sodium orthovanadate. The inhibitory influence of vanadate was examined over a range of vanadate concentrations (10(-8) to 10(-3) M). The vanadate concentration needed to produce half-maximal inhibition of calcium-stimulated ATPase was 2 X 10(-6) M. These studies show that calcium-stimulated ATPase inhibition can occur, in vitro, at very low levels of vanadate; it is possible that this might contribute to the chain of events which results in the lowering of aqueous humor secretion reported in vanadate-treated rabbits.
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PMID:The effect of vanadate upon calcium-stimulated ATPase of the rabbit iris-ciliary body. 297 47

The distribution of ion-stimulated ATPases of the ciliary epithelium has been examined in tissues from bovine and rabbit eyes. In homogenates of tissues from both species, both Na,K- and anion-stimulated enzyme activities were found, but no K,H-stimulated activity was detected. The anion ATPase had a broad specificity for a number of anions, and was strongly inhibited by thiocyanate. Following separation of pigmented (outer) and non-pigmented (inner) layers of the bovine ciliary epithelium and isolation of the two cell types on density gradients, higher activities of both Na,K- and anion ATPases were found in the non-pigmented cells. Subcellular fractionation of a mixed population of cells showed that the anion ATPase was almost exclusively associated with a mitochondrial fraction, rather than with the plasma-membrane fraction containing the Na,K-ATPase. These results confirm histochemical studies of the distribution of Na,K-ATPase in the ciliary epithelium and support the concept that the inner, non-pigmented cell layer is chiefly responsible for the active transport of ions into the posterior chamber. It is concluded that this transepithelial transport can be driven only by the energy derived via the Na,K-ATPase, and that any subsequent anion or proton transport in the formation of aqueous humor is driven by the sodium gradient through exchange mechanisms.
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PMID:ATPases of ciliary epithelium: cellular and subcellular distribution and probable role in secretion of aqueous humor. 301 67

When corneal microsomes were incubated with arachidonic acid in the presence of an NADPH-generating system, two biologically active metabolites of arachidonic acid were formed. The structure of one of the metabolites, compound C, was previously reported to be 12(R)-hydroxy-5,8,10,14-eicosatetraenoic acid and was found to be a potent inhibitor of the Na+/K+-ATPase in the cornea. The second metabolite, compound D, was found to be a potent vasodilator as well as having the property of stimulating protein influx into the aqueous humor of the eye. Following purification of compound D by thin layer chromatography and high pressure liquid chromatography, it was found to lack a UV chromophore in contrast to the previously reported cytochrome P-450-dependent metabolite. Mass spectrometric analysis using positive and negative ionization modes was carried out on derivatized compound D that had been synthesized from a mixture of labeled [( 5,6,8,9,11,12,14,15-2H8]) and unlabeled arachidonic acid incubated with corneal microsomes. The novel arachidonate metabolite had abundant fragment ions consistent with compound D being a monooxygenated derivative of arachidonic acid with a hydroxyl substituent at carbon 12 of the eicosanoid backbone; only seven deuterium atoms from [2H8]arachidonate were retained in the structure. Oxidative ozonolysis yielded a product indicating that the double bonds in metabolite D resided between carbons at positions 8 and 9 and positions 14 and 15 of the 20-carbon chain. Compound D was therefore characterized as 12-hydroxy-5,8,14-eicosatrienoic acid. Model compounds were synthesized from dimethyl malate with the hydroxy at the 12 position with both the R and S absolute configuration and with all double bonds of the cis configuration. Only the 12(R) isomer was found to be a potent vasodilator and to increase aqueous humor protein concentration, suggesting that the biologically active compound D was 12(R)-hydroxy-5,8,14-(Z,Z,Z)-eicosatrienoic acid. As this compound possesses proinflammatory properties, it may play a role in the wound-healing processes of corneal injury.
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PMID:12(R)-hydroxyeicosatrienoic acid: a vasodilator cytochrome P-450-dependent arachidonate metabolite from the bovine corneal epithelium. 314 17

Some biochemical factors of the iris-ciliary body of the rabbit have been examined for effects induced by water-soluble marihuana-derived material (MDM). Adenylate cyclase activity and sensitivity to beta-adrenergic agonists were unchanged, as measured 4 hours after MDM administration in vivo. Magnesium-dependent and anion-sensitive, but not sodium-potassium, ATPase activities were inhibited 6 hours after MDM administration in vivo, although they were unaffected by in vitro incubation. Topical administration of a potent substance P antagonist had no effect on the time course or magnitude of intravenous MDM-induced ocular effects in rabbit. Intravenously administered sugars antagonized the effects of MDM on intraocular pressure. A variety of drugs which display a range of biochemical effects varying from beta-adrenergic receptor agonism, to alteration of glycoprotein residues were employed. None of the agents employed, ranging from cAMP modifiers to protein synthesis blockers, had any effect on the MDM-induced response. It is apparent that the mechanism underlying the ocular hypotensive effect of MDM does not reside in mediation through adenylate cyclase, ATPase or substance P, but rather through a mechanism mediated by terminal sugar moieties on the molecule. The data suggest that modification of the surface membrane glycoprotein residues on the ciliary epithelium can induce marked alterations in aqueous humor flow rate.
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PMID:Marihuana-derived material: biochemical studies of the ocular responses. 316 May 44

Open-angle glaucoma is treated primarily with drugs, some of which have been used clinically for years. These drugs include: 1) cholinergic agonists that increase aqueous humor outflow, 2) adrenergic agonists and antagonist that affect both aqueous humor formation and outflow, and 3) carbonic anhydrase inhibitors that decrease aqueous humor formation. Several new classes of drugs are being tested for efficacy and mechanism of action. They include: 1) the D-isomer of timolol that reduces aqueous humor formation without producing adrenergic blockade, 2) dopaminergic agonists and antagonists, including bromocriptine and butyrophenones that reduce intraocular pressure, and 3) cannabinoids that reduce aqueous humor formation and increase outflow. In addition, several other types of drugs, such as prostaglandins, diuretics, Na+,K+-ATPase inhibitors, and adenyl cyclase stimulators are just now beginning to be studied.
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PMID:A synopsis of recent developments in antiglaucoma drugs. 391 48

Topical administration of 0.5% vanadate lowers intraocular pressure in monkey and rabbit eyes. This appears to be a consequence of a reduction in the rate of aqueous humor secretion, probably resulting from the inhibition of ciliary epithelium membrane. NaK ATPase. The ubiquitous vanadate and its interactions with catecholamines and ascorbate may play a role in regulating the sodium pump of the ciliary epithelium. Adrenergic blocking agents may also lower intraocular pressure by inhibiting the NaK ATPase of the ciliary epithelium.
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PMID:Vanadate and aqueous humor dynamics. Proctor Lecture. 610 42

The effects of serotonin and five other indoles were tested on the electrical parameters and ionic transport in the isolated toad lens. Serotonin, tryptophan and 5-hydroxy-L-tryptophan did not affect the electrical parameters of the lens at concentrations as high as 1 mM. Tryptamine, 5-methyltryptamine and 5-methoxytryptamine had dual effects: 1 mM in the posterior bathing solution depressed the potential difference of the posterior face of the lens, which resulted in an increase in the translenticular potential difference and short-circuit current; 1 mM in the anterior solution (in contact with the lens epithelium) produced a quick and pronounced reduction of the potential difference of the anterior face. This resulted in a 90-100% decline of the translenticular short-circuit current. Serotonin and tryptamine were then tested for their effect on the ATPases of lens epithelium. Both amines inhibited the enzymes with tryptamine at 5 mM completely inhibiting all ATPase activity. Since tryptophan is transported from the aqueous humor into the lens and may be converted by lens enzymes to serotonin and tryptamine, these findings may have physiological implications in cataractogenesis.
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PMID:Inhibition of ionic transport and ATPase activities by serotonin analogues in the isolated toad lens. 625 64

The effect of timolol on the active transport system in the iris root-ciliary body of rabbits was studied to elucidate the action mechanism of timolol. Neither Na+-K+-adenosine triphosphatase (ATPase) nor Mg++-ATPase was inhibited by timolol at 1 X 10(-4) M concentration. None of the energy production parameters (oxygen consumption, glucose metabolism, and lactic acid formation) was inhibited by timolol either. Further, the biosynthesis of prostaglandins E2 and F2 alpha was not affected by timolol at 1 X 10(-3) M. The blood flow to the eye was measured with a 85Sr-microsphere method. It was found that the blood flow in the iris root-ciliary body and choroid was significantly reduced by a topical application of 0.25% timolol. The dopamine concentration in the iris root-ciliary body was reduced by timolol at 1 X 10(-5) M concentration. Neither epinephrine nor norepinephrine concentration was altered by timolol. The results indicate that timolol reduces the rate of aqueous humor formation through reduction of blood flow to the ciliary process rather than via the inhibition of the active transport system or that of prostaglandin biosynthesis.
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PMID:Action mechanism of timolol to lower the intraocular pressure in rabbits. 631 18


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