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Na+-K+ ATPase or Na-pump ATPase, a member of “P”-type ATPase superfamily, is characterized by association of multiple isoforms mainly of it’s α- and β- subunits. At present four different α- (α-1,α-2,α-3 and α-4) and three β- (β-1, β-2, and β-3) isoforms have been identified in mammalian cells and their differential expressions are tissue specific. Regulation of Na+-K+ ATPase activity is an important but a complex process, which involves short-term and long-term mechanisms. Short-term regulation of Na+-K+ ATPase is either mediated by changes in intracellular Na+ concentrations that directly affect the Na+-pump activity or by phosphorylation/dephosphorylation-mediated by some stimulants leading to changes in its expression and transport properties. On the other hand, long-term regulation of Na+-K+ ATPase is mediated by hormones, such as mineralocorticoids and thyroid hormones, which cause changes in the transcription of genes of α- and β- subunits leading to an increased expression in the level of Na+-pump. Several studies have revealed a relatively new type of regulation that involves the association of small, single span membrane proteins with this enzyme. These proteins belong to the FXYD family, the members of which share a common signature sequence encompassing the transmembrane domain adjacent to the isoform(s) of α-β subunits of Na+-K+ ATPase. Considering the extraordinary importance of Na+-K+ ATPase in cellular function, several internationally established investigators have contributed their articles in the monograph entitled “Regulation of Membrane Na+-K+ ATPase” for inspiring young scientists and graduate students to enrich their knowledge on the enzyme, and we are sure that this book will soon be considered as a comprehensive scientific literature in the area of Na+-K+ ATPase regulation in health and disease.
Biochemistry --- Chemistry --- Physical Sciences & Mathematics --- Sodium/potassium ATPase. --- Membranes (Biology) --- Biological membranes --- Biomembranes --- Pump, Sodium (Physiology) --- Sodium-potassium pump (Physiology) --- Sodium pump (Physiology) --- Biological interfaces --- Protoplasm --- Adenosine triphosphatase --- Sodium cotransport systems --- Biochemistry. --- Cell membranes. --- Medicine. --- Protein Structure. --- Membrane Biology. --- Protein Science. --- Atomic/Molecular Structure and Spectra. --- Molecular Medicine. --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Medical sciences --- Pathology --- Physicians --- Cell surfaces --- Cytoplasmic membranes --- Plasma membranes --- Plasmalemma --- Glycocalyces --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Composition --- Health Workforce --- Proteins . --- Cell membranes . --- Atomic structure . --- Molecular structure . --- Molecular biology. --- Molecular biochemistry --- Molecular biophysics --- Biophysics --- Biomolecules --- Systems biology --- Structure, Molecular --- Chemical structure --- Structural bioinformatics --- Structure, Atomic --- Atomic theory --- Proteids --- Polypeptides --- Proteomics --- Proteins. --- Biological transport. --- Atomic structure . --- Molecular structure. --- Medicine --- Membrane Trafficking. --- Protein Biochemistry. --- Atomic and Molecular Structure and Properties. --- Biomedical Research. --- Research. --- Biological research --- Biomedical research --- Membrane transport --- Passive transport, Biological --- Physiological transport --- Transport, Biological --- Diffusion --- Osmosis
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The biological membranes of cellular organization enfold an important group of membrane proteins called the ATPases, which are not only versatile in maintaining chemical gradient and electrical potential across the membrane but also bring metabolites necessary for cell metabolism and drive out toxins, waste products and solutes that otherwise can curb cell functions. ATPases are distributed virtually in all live forms starting from unicellular to multicellular and also in viruses. There are different types of ATPases, which differ in function and structure and in the type of ions they transport. The three main types of the ion pump ATPase family are: (i) P-type ATPases that transport different ions across membranes and Ca2+ATPases belongs to this catagory (ii) F-type ATPase in mitochondria, chloroplasts and bacterial plasma membranes produce ATP using the proton gradient; and (iii) V-type ATPase catalyzes ATP hydrolysis to transport solutes and maintains acidic pH in organelles like lysosomes. Genetic defects in either of the ATPases cause several diseases and a number of researches have demonstrated the involvement of the members of ATPases in the cell pathology and diseases, thereby penetrating exciting new areas of our understanding. In this book, the authors summarize recent knowledge about the molecular mechanisms associated with Ca2+-ATPase, V-ATPase and F-ATPase in intracellular and extracellular Ca2+ transport, mitochondrial ATP synthase, vesicular H+ transport, and lysosomal pH regulation. This book thereby bridges the gap between fundamental research and biomedical and pharmaceutical applications. The book provides an informative resource to improve ATPase research and modern therapeutic approaches toward different life threatening diseases that are associated with dysregulation of the ATPases.
Biochemistry --- Chemistry --- Physical Sciences & Mathematics --- Adenosine triphosphatase. --- Adenosinetriphosphatase --- Adenylopyrophosphatase --- ATP monophosphatase --- ATP phosphohydrolase --- ATP synthase --- ATP synthetase --- ATPase --- Life sciences. --- Molecular biology. --- Proteins. --- Cell membranes. --- Atomic structure. --- Molecular structure. --- Spectra. --- Life Sciences. --- Protein Structure. --- Membrane Biology. --- Protein Science. --- Atomic/Molecular Structure and Spectra. --- Molecular Medicine. --- Analysis, Spectrum --- Spectra --- Spectrochemical analysis --- Spectrochemistry --- Spectroscopy --- Chemistry, Analytic --- Interferometry --- Optics --- Radiation --- Wave-motion, Theory of --- Absorption spectra --- Light --- Spectroscope --- Structure, Molecular --- Chemical structure --- Structural bioinformatics --- Structure, Atomic --- Atomic theory --- Cell surfaces --- Cytoplasmic membranes --- Plasma membranes --- Plasmalemma --- Membranes (Biology) --- Glycocalyces --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Molecular biochemistry --- Molecular biophysics --- Biophysics --- Systems biology --- Biosciences --- Sciences, Life --- Science --- Qualitative --- Phosphatases --- Biochemistry. --- Medicine. --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Biology --- Medical sciences --- Clinical sciences --- Medical profession --- Human biology --- Life sciences --- Pathology --- Physicians --- Composition --- Health Workforce --- Proteins . --- Cell membranes . --- Atomic structure . --- Molecular structure . --- Biological transport. --- Atomic structure . --- Medicine --- Membrane Trafficking. --- Protein Biochemistry. --- Atomic and Molecular Structure and Properties. --- Biomedical Research. --- Research. --- Biological research --- Biomedical research --- Membrane transport --- Passive transport, Biological --- Physiological transport --- Transport, Biological --- Diffusion --- Osmosis
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Na+-K+ ATPase or Na-pump ATPase, a member of “P”-type ATPase superfamily, is characterized by association of multiple isoforms mainly of it’s α- and β- subunits. At present four different α- (α-1,α-2,α-3 and α-4) and three β- (β-1, β-2, and β-3) isoforms have been identified in mammalian cells and their differential expressions are tissue specific. Regulation of Na+-K+ ATPase activity is an important but a complex process, which involves short-term and long-term mechanisms. Short-term regulation of Na+-K+ ATPase is either mediated by changes in intracellular Na+ concentrations that directly affect the Na+-pump activity or by phosphorylation/dephosphorylation-mediated by some stimulants leading to changes in its expression and transport properties. On the other hand, long-term regulation of Na+-K+ ATPase is mediated by hormones, such as mineralocorticoids and thyroid hormones, which cause changes in the transcription of genes of α- and β- subunits leading to an increased expression in the level of Na+-pump. Several studies have revealed a relatively new type of regulation that involves the association of small, single span membrane proteins with this enzyme. These proteins belong to the FXYD family, the members of which share a common signature sequence encompassing the transmembrane domain adjacent to the isoform(s) of α-β subunits of Na+-K+ ATPase. Considering the extraordinary importance of Na+-K+ ATPase in cellular function, several internationally established investigators have contributed their articles in the monograph entitled “Regulation of Membrane Na+-K+ ATPase” for inspiring young scientists and graduate students to enrich their knowledge on the enzyme, and we are sure that this book will soon be considered as a comprehensive scientific literature in the area of Na+-K+ ATPase regulation in health and disease.
Chemical structure --- Chemistry --- Biomembranes --- Histology. Cytology --- Molecular biology --- Biology --- spectra (chemie) --- celmembranen --- moleculaire structuur --- membranen (biologie) --- protein-engineering --- biologie --- spectroscopie --- eiwitten --- moleculaire biologie --- atoomstructuur --- proteïnen --- enzymen
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The biological membranes of cellular organization enfold an important group of membrane proteins called the ATPases, which are not only versatile in maintaining chemical gradient and electrical potential across the membrane but also bring metabolites necessary for cell metabolism and drive out toxins, waste products and solutes that otherwise can curb cell functions. ATPases are distributed virtually in all live forms starting from unicellular to multicellular and also in viruses. There are different types of ATPases, which differ in function and structure and in the type of ions they transport. The three main types of the ion pump ATPase family are: (i) P-type ATPases that transport different ions across membranes and Ca2+ATPases belongs to this catagory (ii) F-type ATPase in mitochondria, chloroplasts and bacterial plasma membranes produce ATP using the proton gradient; and (iii) V-type ATPase catalyzes ATP hydrolysis to transport solutes and maintains acidic pH in organelles like lysosomes. Genetic defects in either of the ATPases cause several diseases and a number of researches have demonstrated the involvement of the members of ATPases in the cell pathology and diseases, thereby penetrating exciting new areas of our understanding. In this book, the authors summarize recent knowledge about the molecular mechanisms associated with Ca2+-ATPase, V-ATPase and F-ATPase in intracellular and extracellular Ca2+ transport, mitochondrial ATP synthase, vesicular H+ transport, and lysosomal pH regulation. This book thereby bridges the gap between fundamental research and biomedical and pharmaceutical applications. The book provides an informative resource to improve ATPase research and modern therapeutic approaches toward different life threatening diseases that are associated with dysregulation of the ATPases.
Chemical structure --- Chemistry --- Biomembranes --- Histology. Cytology --- Molecular biology --- Biology --- spectra (chemie) --- celmembranen --- moleculaire structuur --- membranen (biologie) --- protein-engineering --- biologie --- spectroscopie --- eiwitten --- moleculaire biologie --- atoomstructuur --- proteïnen
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