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)

Ductin is a highly conserved and polytopic transmembrane protein which is the subunit c component of the vacuolar H(+)-ATPase (V-ATPase) and a component of a connexon channel of gap junctions. Previous studies have suggested that ductin in the V-ATPase has the opposite orientation of ductin in a connexon. Using an in vitro translation system coupled to microsomes derived from the endoplasmic reticulum, we show that ductin is co-translationally inserted into the membrane bilayer, suggesting a dependency on the signal recognition particle for synthesis. By attaching a C-terminal polypeptide derived from beta-lactamase and by using cysteine replacement coupled to chemical labelling, we show that ductin is inserted into the microsomal membrane in both orientations in similar proportions. In contrast, squid rhodopsin appears to be inserted in a single orientation. Changing conserved charged residues at the N-terminus of ductin does not affect the ratio of the two orientations. Once in the microsomal membrane, ductin assembles into an oligomeric complex which contains a pore accessible to a water-soluble probe, reminiscent of the ductin complex found in the V-ATPase and a connexon.
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PMID:Membrane insertion and assembly of ductin: a polytopic channel with dual orientations. 764 80

An infrared spectroscopic method has been developed to quantify the residual amount of detergent present in membranes, e.g., after reconstitution of a membrane protein in phospholipids. A detergent-specific band is selected in the ir spectrum and the intensity is ratioed against a phospholipid-specific band (around 1235 cm-1, vas (P = O)). This ratio shows a linear relation with the molar ratio of detergent of phospholipid, down to as low as 1 to 10. The new method is illustrated in two case studies, viz., tris(hydroxyethyl)ammonium cholate in Na+/K(+)-ATPase proteoliposomes and n-dodecyl-beta-D-maltoside in rhodopsin proteoliposomes.
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PMID:Quantitative analysis of residual detergent in proteoliposomes by Fourier transform infrared spectroscopy. 798 2

Melanophores in the isolated tail from the amphibian larvae Xenopus laevis, Hyla japonicus, Rana pirica, and Hynobius retardatus aggregated melanin granules in response to light and dispersed them when placed in darkness. The spectral characteristics for the melanin-aggregation response were examined by irradiating the Xenopus tail-fin locally (diameter, 2.1 mm) with monochromatic light (380-1,020 nm). The spectral region of wave length which induced melanosome aggregation depended on the light intensity but was limited to the visible spectrum. At low light intensity (1.59 microW/cm2, delta lambda = 5 nm), the aggregation response occurred in the spectral region between 400 and 600 nm and the maximum response was observed at 500 nm. This range is very close to the absorption spectrum of rhodopsin in the visual rod cell. Hypodermic injection of cGMP into isolated tail-fin induced a marked melanin-dispersion in spite of light-stimuli. When the tail-fin was treated with isobutylmethylxanthine (IBMX; phosophodiesterase inhibitor) in darkness and then was re-exposed to light, the aggregation response was inhibited. The photo-sensitive melanin aggregation was independent of a requirement for Ca2+ ions but melanosome dispersion in darkness was Ca(2+)-dependent. K(+)-rich Hanks' solution, ouabain (inhibitor of Na(+)-K(+)-ATPase) or nonactin (cation ionophore), which induced a change of the membrane potential of melanophores, inhibited the aggregation response when the melanophores were re-exposed to light after a period in darkness. These results suggest that the molecular mechanism of photoreception in melanophores of amphibian tadpoles is similar to that in visual cells.
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PMID:Light-sensitive response in melanophores of Xenopus laevis: I. Spectral characteristics of melanophore response in isolated tail fin of Xenopus tadpole. 882 82

Light stimulation of insect photoreceptors causes opening of cation channels and an inward current that is partially carried by Na+ ions. There is also an efflux of K+ ions upon photostimulation. Na+ and K+ gradients across the photoreceptor membrane are reestablished by the activity of the enzyme Na+,K(+)-ATPase. About two-thirds of the total amount of ATP consumed in response to a light stimulus is attributed to the activity of this ion pump, demonstrating the importance of this enzyme for photoreceptor function. Insect photoreceptor cells are polarized epithelial cells; their plasma membrane is organized into two domains having a distinct morphology, molecular composition, and function. The visual pigment rhodopsin and the molecular components of the transduction machinery are localized in the rhabdomere, an array of densely packed microvilli, whereas Na+,K(+)-ATPase resides in the nonrhabdomeric membrane. Comparative immunolocalization studies on compound eyes of diverse insect species have demonstrated subtle variations in the distribution patterns of Na+,K(+)-ATPase. These may be accounted for by differences in the mechanisms responsible for Na+,K(+)-ATPase positioning.
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PMID:Distribution of Na+,K(+)-ATPase in photoreceptor cells of insects. 939 22

An understanding of the action of many drugs requires a knowledge of how the drug reaches the site of action in a cell. A detailed knowledge of the structure and function of cell membranes is often required to understand the transport of drugs across the plasma membrane. To obtain this information proteins must be isolated. The isolation and characterisation of cell membrane proteins usually requires the solubilisation of the membrane and a method of separation of the various membrane proteins and glycoproteins. The starting point for such an investigation is the choice of a suitable surfactant (detergent) to solubilise the membrane. This review considers the range of surfactants that are available for membrane solubilisation, how surfactants interact with membranes, the part they play in the separation of integral membrane proteins and in the reconstitution of membrane proteins for functional studies. The solubilisation of specific membrane proteins and glycoproteins including the human erythrocyte anion transporter, mitochondrial porin, sarcoplasmic reticulum Ca(2+)-ATPase, the ATPase-active multidrug transporter P-glycoprotein, bacteriorhodopsin and rhodopsin are also discussed.
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PMID:Surfactants in membrane solubilisation. 1020 10

Drosophila melanogaster photoreceptors are highly polarized cells and their plasma membrane is organized into distinct domains. Zonula adherens junctions separate a smooth peripheral surface, the equivalent of the basolateral surface in other epithelial cells, from the central surface (approximately equal to apical surface). The latter consists of the microvillar rhabdomere and the juxtarhabdomeric domain, a nonmicrovillar area between the rhabdomere and the zonulae adherens. The distribution of Na/K-ATPase over these domains was examined by immunocytochemical, developmental, and genetic approaches. Immunofluorescence and immunogold labeling of adult compound eyes reveal that the distribution of Na/K-ATPase is concentrated at the peripheral surface in the photoreceptors R1-R6, but extends over the juxtarhabdomeric domain to the rhabdomere in the photoreceptors R7/R8. Developmental analysis demonstrates further that Na/K-ATPase is localized over the entire plasma membrane in all photoreceptors in early pupal eyes. Redistribution of Na/K-ATPase in R1-R6 occurs at about 78% of pupal life, coinciding with the onset of Rh1-rhodopsin expression on the central surface of these cells. Despite the essential role of Rh1 in structural development and intracellular trafficking, Rh1 mutations do not affect the distribution of Na/K-ATPase. These results suggest that Na/K-ATPase and rhodopsin are involved in distinct intracellular localization mechanisms, which are maintained independent of each other.
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PMID:Localization of Na/K-ATPase in developing and adult Drosophila melanogaster photoreceptors. 1086 20

Rhodopsin is essential for photoreceptor morphogenesis; photoreceptors lacking rhodopsin degenerate in humans, mice, and Drosophila. Here we report that transgenic expression of a dominant-active Drosophila Rho guanosine triphosphatase, Drac1, rescued photoreceptor morphogenesis in rhodopsin-null mutants; expression of dominant-negative Drac1 resulted in a phenotype similar to that seen in rhodopsin-null mutants. Drac1 was localized in a specialization of the photoreceptor cortical actin cytoskeleton, which was lost in rhodopsin-null mutants. Thus, rhodopsin appears to organize the actin cytoskeleton through Drac1, contributing a structural support essential for photoreceptor morphogenesis.
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PMID:Rescue of photoreceptor degeneration in rhodopsin-null Drosophila mutants by activated Rac1. 1118 46

Phospholipids containing docosahexaenoic acid (22:6n-3) have been proposed to be required as conformational cofactors for the functional assembly of membrane proteins such as rhodopsin, ion pumps and the various complexes of the mitochondrial electron transport chain (Infante, 1987, Mol. Cell. Biochem. 74, 111-116; Infante and Huszagh, 2000, FEBS Lett. 468, 1-5). This hypothesis predicts that high-frequency contraction muscles, which are endowed with a high content of sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) and mitochondrial respiration enzymes, would have higher concentrations of 22:6n-3-containing phospholipids when compared with other muscles in the same species known to have a much lower contraction frequency. We have analyzed the fatty acid composition of ruby-throated hummingbird (Archilochus colubris) pectoral and leg muscles and of rattlesnake (Crotalus atrox) shaker and ventral muscles. We have found that hummingbird pectoral muscles, which are high contraction frequency muscles with the highest known respiratory rate among vertebrates, have a 22:6n-3 concentration of 20.8% vs. 4.9% for the low frequency leg muscles. Similarly, rattler muscles in rattlesnakes, also high contraction frequency muscles, have a higher 22:6n-3 concentration than that of their ventral muscles (15.1% vs. 10.6%, respectively). These results are consistent with a specific molecular role for 22:6n-3-containing phospholipids, as proposed.
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PMID:High levels of docosahexaenoic acid (22:6n-3)-containing phospholipids in high-frequency contraction muscles of hummingbirds and rattlesnakes. 1156 91

The present models of phototransduction for vertebrates and invertebrates have been reviewed and the relative literature updated. The emerging picture for vertebrate phototransduction is a result of a better knowledge of its general outlines, although some important details such as the role of calcium ions are still lacking. The molecular events involved in the rising phase of the electrical response have basically been understood, whilst those involved in response inactivation and recovery remain to be elucidated. In an overall strategy, the phototransduction in invertebrates shares a great deal of similarity with that in vertebrates but differs in the underlying molecular events. However, a complete picture of phototransduction in invertebrate photoreceptors has not yet emerged. The available data on the structure of the visual pigment rhodopsin reveal further details on the present model of the retinal-binding pocket of the protein and consequently of the "red shift" of the absorbance of retinal. The problem of the energy supplied during photoreception, in particular, the availability of ATP in the rod outer segment and the presence in the disk membranes of a Ca-ATPase are discussed. Finally, recent progress in understanding the molecular mechanisms of inherited retinal diseases and relative gene identification are summarized.
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PMID:Recent advances in our understanding of rhodopsin and phototransduction. 1158 16

Starting with a mutation impacting photoreceptor morphogenesis, we identify here a Drosophila gene, eyes closed (eyc), as a fly homolog of p47, a protein co-factor of the p97 ATPase implicated in membrane fusion. Temporal misexpression of Eyc during rhabdomere extension early in pupal life results in inappropriate retention of normally transient adhesions between developing rhabdomeres. Later Eyc misexpression results in endoplasmic reticulum proliferation and inhibits rhodopsin transport to the developing photosensitive membrane. Loss of Eyc function results in a lethal failure of nuclear envelope assembly in early zygotic divisions. Phenotypes resulting from eyc mutations provide the first in vivo evidence for a role for p47 in membrane biogenesis.
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PMID:Eyes closed, a Drosophila p47 homolog, is essential for photoreceptor morphogenesis. 1178 8


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