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http://dx.doi.org/10.1016/0039-128x(88)90148-1 | DOI Listing |
Eur J Appl Physiol
August 2020
Institute for Health and Sport (iHeS), Victoria University, PO Box 14428, Melbourne, VIC, 8001, Australia.
Purpose: The Na, K-ATPase (NKA) is important in regulating trans-membrane ion gradients, cellular excitability and muscle function. We investigated the effects of resistance training in healthy young adults on the adaptability of NKA content and of the specific α and β isoforms in human skeletal muscle.
Methods: Twenty-one healthy young males (22.
Curr Mol Pharmacol
October 2017
Departamento de Psicobiologia, Universidade Federal de São Paulo, Escola Paulista de Medicina (UNIFESP/ EPM), Rua Botucatu 862, 1° andar, Vila Clementino, São Paulo, SP 04023-062, Brazil.
Background And Objective: Epilepsy is one of the most prevalent neurological disorders worldwide, but its underlying mechanisms have not yet been clarified. Among the possible molecular mechanisms that underlie its occurrence are those that are responsible for the neuronal ionic gradient, including the transmembrane enzyme Na+,K+;-adenosine triphosphatase (ATPase). Na+,K+-ATPase plays an important role in controlling neuronal excitability, and it is believed to be related to the pathophysiology of epilepsy.
View Article and Find Full Text PDFThe Na+-K+-ATPase is specifically inhibited by cardiac glycosides, some of which may also function as endogenous mammalian hormones. Previous studies using Xenopus oocytes, yeast cells, or purified isoforms demonstrated that affinities of various cardiac glycosides for three isoforms of the Na+-K+-ATPase (α1-α3β1) may differ, a finding with potential clinical implication. The present study investigates isoform selectivity and effects of cardiac glycosides on cultured mammalian cells under more physiological conditions.
View Article and Find Full Text PDFNeuron Glia Biol
May 2010
Department of Clinical Pharmacology, China Medical University, Shenyang, P.R. China.
Although Na+,K+-ATPase-mediated K+ uptake into astrocytes plays a major role in re-establishing resting extracellular K+ following neuronal excitation little information is available about astrocytic Na+,K+-ATPase function, let alone mechanisms returning K+ to neurons. The catalytic units of the Na+,K+-ATPase are the astrocyte-specific α2, the neuron-specific α3 and the ubiquitously expressed α1. In the present work, Bmax and KD values for α1, α2 and α3 subunits were computed in cultured cerebro-cortical mouse astrocytes and cerebellar granule neurons by non-linear regression as high-affinity (α2, α3) and low-affinity (α1) [3H]ouabain binding sites, which stoichiometrically equal transporter sites.
View Article and Find Full Text PDFActa Physiol (Oxf)
March 2007
Muscle, Ions and Exercise Group, School of Human Movement, Recreation and Performance, Centre for Ageing, Rehabilitation, Exercise and Sport Science (CARES), Victoria University, Melbourne, Vic., Australia.
Aim: This study investigated the effects of endurance training status and sex differences on skeletal muscle Na+,K+-pump mRNA expression, content and activity.
Methods: Forty-five endurance-trained males (ETM), 11 recreationally active males (RAM), and nine recreationally active females (RAF) underwent a vastus lateralis muscle biopsy. Muscle was analysed for Na+,K+-pump alpha1, alpha2, alpha3, beta1, beta2 and beta3 isoform mRNA expression (real-time reverse transcription-polymerase chain reaction), content ([3H]-ouabain-binding site) and maximal activity (3-O-methylfluorescein phosphatase, 3-O-MFPase).
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