The Experts below are selected from a list of 114 Experts worldwide ranked by ideXlab platform
Andrej A Kochegarov - One of the best experts on this subject based on the ideXlab platform.
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modulators of Ion Transporting ATPases
Expert Opinion on Therapeutic Patents, 2001Co-Authors: Andrej A KochegarovAbstract:This review focuses on Ion-Transporting ATPases which play an essential role in the generatIon and maintenance of Ionic gradients between cell compartments and environment. There are three types of catIon Transporting ATPases: oligomycin sensitive F-ATPases, bafilomycin-sensitive V (vacuolar) H+-Transporting ATPases (V-ATPases) and vanadate-sensitive P (phosphate binding) ATPases (P-ATPases), the most important of these being Ca2+-ATPase, Na+/K+-ATPase and H+/K+-ATPase. The influences of numerous modulators are reviewed.
Jinlong Li - One of the best experts on this subject based on the ideXlab platform.
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transport stress induces weight loss and heart injury in chicks disruptIon of Ionic homeostasis via modulating Ion Transporting ATPases
Oncotarget, 2017Co-Authors: Zhaoyang Li, Hui Li, Xuenan Li, Jing Ge, Cong Zhang, Jinlong LiAbstract:// Zhao-Yang Li 1,* , Jia Lin 1,* , Feng Sun 1,* , Hui Li 1,2,* , Jun Xia 1,3 , Xue-Nan Li 1,4 , Jing Ge 1,4 , Cong Zhang 1,3 and Jin-Long Li 1,3,4 1 College of Veterinary Medicine, Northeast Agricultural University, Harbin, P. R. China 2 Harbin Sport University, Harbin, P. R. China 3 Department of Heilongjiang for Common Animal Disease PreventIon and Treatment, Key Laboratory of the Provincial EducatIon Northeast Agricultural University, Harbin, P. R. China 4 Heilongjiang Key Laboratory for Laboratory Animals and Comparative Medicine, Northeast Agricultural University, Harbin, P. R. China * These authors have contributed equally to this work Correspondence to: Jin-Long Li, email: // Keywords : transport stress; weight loss; heart injury; Ionic disorder; ATPase; Pathology SectIon Received : January 13, 2017 Accepted : February 24, 2017 Published : March 04, 2017 Abstract TransportatIon is inevitable in the poultry industry, and it can induce stress to chicks in varying degrees, such as mild discomfort, sometimes even death. However, the research about the effects of transport stress on the weight loss and heart injury of chicks is lacking. To elucidate the underlying mechanism of transport stress-induced effects, chicks were transported for 2h, 4h and 8h. The creatinine kinase (CK) activities, the Ionic contents, the ATPases activities and the transcriptIon of the ATPase associated subunits in chick heart were detected. The results showed that transport stress increased the weight loss and the CK activity, disturbed the Ionic (K + , Ca 2+ , Mg 2+ ) homeostasis and inhibited the ATPase (Na + -K + -ATPase, Ca 2+ -ATPase, Mg 2+ -ATPase and Ca 2+ -Mg 2+ -ATPase) activities, increased the ATP content and downregulated the gene expressIon levels of the ATPase associated subunits in heart. In conclusIon, transport stress disturbed the Ionic homeostasis via modulating Ion Transporting ATPases and the transcriptIons of the associated subunits, and ultimately induced weight loss and heart injury in chicks.
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lycopene protects against atrazine induced hepatic Ionic homeostasis disturbance by modulating Ion Transporting ATPases
Journal of Nutritional Biochemistry, 2016Co-Authors: Huashan Zhao, Xuenan Li, Jinlong Li, Lirun Xiang, Lili Wang, Ying ZhangAbstract:The aim of this study was to evaluate the possible chemoprotective role of lycopene (LYC) against atrazine (ATR)-induced Ionic disorder and hepatotoxicity in mice. Male kunming mice were treated with LYC (5mg/kg) and/or ATR (50mg/kg or 200mg/kg) by lavage administratIon for 21days. Ionic disorder was assessed by determining the Na(+), K(+) and Ca(2+) content and the alteratIon in ATP enzymes (ATPases) including Na(+)-K(+)-ATPase, Ca(2+)-ATPase, Mg(2+)-ATPase and Ca(2+)-Mg(2+)-ATPase and the mRNA levels of ATPase's subunits in liver. ATR caused the increases of alanine aminotransferase and aspartate aminotransferase activities and histological changes. LYC pretreatment significantly protected liver against ATR-caused alternatIon. The significant effect of ATR and LYC on the K(+) and Mg(2+) content in liver was not observed, but ATR increased hepatic Na(+)-K(+)-ATPase activity and decreased Mg(2+)-ATPase and Ca(2+)-Mg(2+)-ATPase activity. The mRNA expressIons of Na(+)-K(+)-ATPase subunits were regulated significantly by ATR. A significant increase of Ca(2+) content and seven down-regulated mRNA expressIons of Ca(2+)-ATPase subunits and a decrease of Ca(2+)-ATPase activity were observed in the ATR-treated mice. Notably, LYC modulated these ATR-induced alteratIons of ATPase activity and mRNA expressIon of their subunits. These results suggest that ATR presents hepatotoxicity via regulating hepatic ATPase's activities and their subunit transcriptIons and inducing Ionic disorder. LYC protects liver against ATR-induced hepatotoxicity, significantly. LYC modulated hepatic Ionic homeostasis disturbance via regulatIon of ATPase activities and their subunits' (1a1, 1b3, 1b4 and 2b4) transcriptIons. In summary, these effects play a critical role of LYC-mediated chemopreventIon against ATR-induced hepatotoxicity.
Michael J. Caplan - One of the best experts on this subject based on the ideXlab platform.
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Ion Pumps in Polarized Cells: Sorting and RegulatIon of the Na+,K+- and H+,K+-ATPases
Journal of Biological Chemistry, 2001Co-Authors: Lisa A. Dunbar, Michael J. CaplanAbstract:Abstract The physiologic functIon of an Ion transport protein is determined, in part, by its subcellular localizatIon and by the cellular mechanisms that modulate its activity. The Na+,K+-ATPase and the H+,K+-ATPases are closely related members of the P-type family of Ion Transporting ATPases. Despite their homology, these pumps are sorted to different domains in polarized epithelial cells, and their enzymatic activities are subject to distinct regulatory pathways. The molecular signals responsible for these properties have begun to be elucidated. It appears that a complex array of inter- and intramolecular interactIons govern trafficking, distributIon, and catalytic capacities of these proteins.
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The cell biology of Ion pumps: sorting and regulatIon.
European Journal of Cell Biology, 2000Co-Authors: Lisa A. Dunbar, Michael J. CaplanAbstract:Summary The physiologic functIon of an Ion pump is determined, in part, by its subcellular localizatIon and by the cellular mechanisms that modulate its activity. The Na,K-ATPase and the gastric H,K-ATPase are two closely related members of the P-type family of Ion Transporting ATPases. Despite their homology, these pumps are sorted to different domains in polarized epithelial cells and their enzymatic activities are subject to distinct regulatory pathways. The molecular signals responsible for these properties have begun to be elucidated. It appears that a complex array of inter- and intra-molecular interactIons govern these proteins' trafficking, distributIon and catalytic capacity.
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Sorting of Ion transport proteins in polarized cells
Journal of Cell Science, 1993Co-Authors: Cara J Gottardi, Grazia Pietrini, Denise L. Roush, Michael J. CaplanAbstract:SUMMARY The plasma membranes of polarized epithelial cells and neurons express distinct populatIons of Ion transport proteins in their differentiated plasma membrane domains. In order to understand the mechanisms responsible for this polarity it will be necessary to elucidate the nature both of sorting signals and of the cellular machinery which recognizes and acts upon them. In our efforts to study sorting signals we have taken advantage of two closely related families of Ion transport proteins whose members are concentrated in different epithelial plasmalemmal domains. The H + , K + -ATPase and the Na + , K + -ATPase are closely related members of the E 1 -E 2 family of Ion Transporting ATPases. Despite their high degree of structural and functIonal homology, they are concentrated on different surfaces of polarized epithelial cells and pursue distinct routes to the cell surface in cells which manifest a regulated delivery pathway. We have transfected cDNAs encoding these pumps’ subunit polypeptides, as well as chimeras derived from them, in a variety of epithlial and non-epithelial cell types. Our observatIons suggest that these pumps encode multiple sorting signals whose relative importance and functIons may depend upon the cell type in which they are expressed. Recent evidence suggests that the sorting mechanisms employed by epithelial cells may be similar to those which operate in neurons. We have examined this propositIon by studying the distributIons of Ion pumps and neurotransmitter re-uptake cotransporters expressed endogenously and by transfectIon in neurons and epithelial cells, respectively. We find that one of the classes of proteins we studied obeys the correlatIon between neuronal and epithelial sorting while another does not. Our data are consistent with the possibility that sorting signals and sorting mechanisms are extremely plastic and can be adapted to different uses in different cell types or under different physiological conditIons.
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molecular requirements for the cell surface expressIon of multisubunit Ion Transporting ATPases identificatIon of protein domains that participate in na k atpase and h k atpase subunit assembly
Journal of Biological Chemistry, 1993Co-Authors: Cara J Gottardi, Michael J. CaplanAbstract:Abstract The Ion-Transporting H,K-ATPase and Na,K-ATPase enzymes are each composed of an alpha and a beta subunit. It is known that assembly of the alpha and beta subunits of the Na,K-ATPase is necessary for the cell-surface delivery of the active enzyme. We have examined the molecular domains involved in the assembly of the H,K-ATPase and Na,K-ATPase alpha and beta subunits by expressing individual subunits and subunit chimeras in transiently transfected COS-1 cells. Our results demonstrate that the H,K-ATPase alpha subunit requires its beta subunit for efficient cell-surface expressIon, as determined by indirect immunofluorescence. The H,K-ATPase beta protein appears to be able to get to the cell surface unaccompanied by any alpha subunit and appears to localize as well to a populatIon of intracellular vesicles. We find that a transfected chimera encoding the NH2-terminal half of the H,K-ATPase alpha subunit and the COOH-terminal half of the Na,K-ATPase alpha subunit appears to assemble with the endogenous Na,K-ATPase beta subunit and to reach the plasmalemma. TransfectIon of the complementary alpha chimera requires coexpressIon with the H,K-ATPase beta subunit in order to attain surface delivery. Thus, it is the COOH-terminal half of the alpha subunit that specifies assembly with a particular beta subunit.
Xuenan Li - One of the best experts on this subject based on the ideXlab platform.
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transport stress induces weight loss and heart injury in chicks disruptIon of Ionic homeostasis via modulating Ion Transporting ATPases
Oncotarget, 2017Co-Authors: Zhaoyang Li, Hui Li, Xuenan Li, Jing Ge, Cong Zhang, Jinlong LiAbstract:// Zhao-Yang Li 1,* , Jia Lin 1,* , Feng Sun 1,* , Hui Li 1,2,* , Jun Xia 1,3 , Xue-Nan Li 1,4 , Jing Ge 1,4 , Cong Zhang 1,3 and Jin-Long Li 1,3,4 1 College of Veterinary Medicine, Northeast Agricultural University, Harbin, P. R. China 2 Harbin Sport University, Harbin, P. R. China 3 Department of Heilongjiang for Common Animal Disease PreventIon and Treatment, Key Laboratory of the Provincial EducatIon Northeast Agricultural University, Harbin, P. R. China 4 Heilongjiang Key Laboratory for Laboratory Animals and Comparative Medicine, Northeast Agricultural University, Harbin, P. R. China * These authors have contributed equally to this work Correspondence to: Jin-Long Li, email: // Keywords : transport stress; weight loss; heart injury; Ionic disorder; ATPase; Pathology SectIon Received : January 13, 2017 Accepted : February 24, 2017 Published : March 04, 2017 Abstract TransportatIon is inevitable in the poultry industry, and it can induce stress to chicks in varying degrees, such as mild discomfort, sometimes even death. However, the research about the effects of transport stress on the weight loss and heart injury of chicks is lacking. To elucidate the underlying mechanism of transport stress-induced effects, chicks were transported for 2h, 4h and 8h. The creatinine kinase (CK) activities, the Ionic contents, the ATPases activities and the transcriptIon of the ATPase associated subunits in chick heart were detected. The results showed that transport stress increased the weight loss and the CK activity, disturbed the Ionic (K + , Ca 2+ , Mg 2+ ) homeostasis and inhibited the ATPase (Na + -K + -ATPase, Ca 2+ -ATPase, Mg 2+ -ATPase and Ca 2+ -Mg 2+ -ATPase) activities, increased the ATP content and downregulated the gene expressIon levels of the ATPase associated subunits in heart. In conclusIon, transport stress disturbed the Ionic homeostasis via modulating Ion Transporting ATPases and the transcriptIons of the associated subunits, and ultimately induced weight loss and heart injury in chicks.
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lycopene protects against atrazine induced hepatic Ionic homeostasis disturbance by modulating Ion Transporting ATPases
Journal of Nutritional Biochemistry, 2016Co-Authors: Huashan Zhao, Xuenan Li, Jinlong Li, Lirun Xiang, Lili Wang, Ying ZhangAbstract:The aim of this study was to evaluate the possible chemoprotective role of lycopene (LYC) against atrazine (ATR)-induced Ionic disorder and hepatotoxicity in mice. Male kunming mice were treated with LYC (5mg/kg) and/or ATR (50mg/kg or 200mg/kg) by lavage administratIon for 21days. Ionic disorder was assessed by determining the Na(+), K(+) and Ca(2+) content and the alteratIon in ATP enzymes (ATPases) including Na(+)-K(+)-ATPase, Ca(2+)-ATPase, Mg(2+)-ATPase and Ca(2+)-Mg(2+)-ATPase and the mRNA levels of ATPase's subunits in liver. ATR caused the increases of alanine aminotransferase and aspartate aminotransferase activities and histological changes. LYC pretreatment significantly protected liver against ATR-caused alternatIon. The significant effect of ATR and LYC on the K(+) and Mg(2+) content in liver was not observed, but ATR increased hepatic Na(+)-K(+)-ATPase activity and decreased Mg(2+)-ATPase and Ca(2+)-Mg(2+)-ATPase activity. The mRNA expressIons of Na(+)-K(+)-ATPase subunits were regulated significantly by ATR. A significant increase of Ca(2+) content and seven down-regulated mRNA expressIons of Ca(2+)-ATPase subunits and a decrease of Ca(2+)-ATPase activity were observed in the ATR-treated mice. Notably, LYC modulated these ATR-induced alteratIons of ATPase activity and mRNA expressIon of their subunits. These results suggest that ATR presents hepatotoxicity via regulating hepatic ATPase's activities and their subunit transcriptIons and inducing Ionic disorder. LYC protects liver against ATR-induced hepatotoxicity, significantly. LYC modulated hepatic Ionic homeostasis disturbance via regulatIon of ATPase activities and their subunits' (1a1, 1b3, 1b4 and 2b4) transcriptIons. In summary, these effects play a critical role of LYC-mediated chemopreventIon against ATR-induced hepatotoxicity.
G. Scheiner-bobis - One of the best experts on this subject based on the ideXlab platform.
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Ion-Transporting ATPases as Ion channels
Naunyn-Schmiedeberg's Archives of Pharmacology, 1998Co-Authors: G. Scheiner-bobisAbstract:Ion-Transporting ATPases (pumps) hydrolyze ATP to maintain Ion gradients across cell membranes. A presuppositIon for the maintenance of the gradients is that the Ionophore of the pump that conducts the Ions is accessible only from one of the two surfaces of the plasma membrane at any given time. Thus, a characteristic feature of pumps is an occluded state of the transported Ions, whereas Ion channels upon stimulatIon remain open at both ends and allow Ions to flow through them down their chemical gradients. Recent experiments, however, provide evidence that a channel, simultaneously open on both sides of the plasma membrane, can also be formed within the mammalian sodium pump (Na^+,K^+-ATPase) upon its interactIon with the marine toxin palytoxin, thus underlining common structural features shared by channels and pumps. This assumptIon is further supported by the demonstratIon of structural and functIonal homology between the extracellular loop of the sodium pump α subunit connecting the M7 and M8 transmembrane spans and the P-loops of Na^+ channels. Possibly, pumps are simply channels that are able to be gated by ATP and its product phosphate.
