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Endocrinology Vol. 142, No. 8 3474-3482
Copyright © 2001 by The Endocrine Society

ARTICLES

Insulin- and Glucose-Induced Phosphorylation of the Na+,K+-Adenosine Triphosphatase {alpha}-Subunits in Rat Skeletal Muscle

Alexander V. Chibalin, Marina V. Kovalenko, Jeffrey W. Ryder, Eric Féraille, Harriet Wallberg-Henriksson and Juleen R. Zierath

Department of Clinical Physiology (A.V.C., J.W.R., H.W.-H., J.R.Z.), Karolinska Hospital, 171 76 Stockholm, Sweden; Department of Physiology and Pharmacology (A.V.C., J.W.R., E.F., H.W.-H., J.R.Z.), Karolinska Institute, 171 77 Stockholm, Sweden; Ludwig Institute for Cancer Research (M.V.K.), 751 24 Uppsala, Sweden; and Division de Néphrologie (E.F.), Hôpital Cantonal Universitaire, 1211 Genève 4, Switzerland

Address all correspondence and requests for reprints to: Alexander V. Chibalin, Ph.D., Department of Clinical Physiology, Karolinska Hospital M1:02, 171 76, Stockholm, Sweden.

Phosphorylation of the {alpha}-subunits of Na+,K+-adenosine triphosphatase in response to insulin, high extracellular glucose concentration, and phorbol 12-myristate 13-acetate was investigated in isolated rat soleus muscle. All three stimuli increased {alpha}-subunit phosphorylation approximately 3-fold. Phorbol 12-myristate 13-acetate- and high glucose-induced phosphorylation of the {alpha}-subunit was completely abolished by the PKC inhibitor GF109203X, whereas insulin-stimulated phosphorylation was only partially reduced. Notably, insulin stimulation resulted in phosphorylation of the {alpha}-subunit on serine, threonine, and tyrosine residues, whereas high extracellular glucose or phorbol 12-myristate 13-acetate stimulation mediated phosphorylation only on serine and threonine residues. Insulin stimulation resulted in translocation of Na+,K+-adenosine triphosphatase {alpha}2-subunit to the plasma membrane and increased Na+,K+-adenosine triphosphatase activity in the same membrane fraction. High glucose had no effect on {alpha}-subunits distribution. Immunoprecipitation with antiphosphotyrosine antibody and subsequent Western blot analysis with anti-{alpha}1- and -{alpha}2-subunit antibodies revealed that both {alpha}1- and {alpha}2-subunit isoforms underwent phosphorylation on tyrosine residues in response to insulin, although with different time course and magnitude. Thus, we show that insulin-stimulated phosphorylation of Na+,K+-adenosine triphosphatase {alpha}-subunit occurs via a PKC- and tyrosine kinase-dependent mechanism, whereas high glucose-induced phosphorylation is only PKC-dependent. Phosphorylation of Na+,K+-adenosine triphosphatase {alpha}-subunits may be involved in regulation of Na+,K+-adenosine triphosphatase activity by insulin or high extracellular glucose in skeletal muscle.




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