Expression of β subunit isoforms of the Na+,K+‐ATPase is muscle type‐specific
- 16 August 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 328 (3), 253-258
- https://doi.org/10.1016/0014-5793(93)80938-q
Abstract
Hindlimb skeletal muscles of the rat express two isoforms of the α (αl and α2) and two isoforms of the β (β1 andβ2) subunits of the Na+,K+-ATPase. Because several muscles constitute the hindlimb, we investigated if specific isoforms are expressed in particular muscles. Northern blot analysis using isoform-specific cDNA probes demonstrated that soleus muscle expressed only the β1 transcript, whereas EDL or white gastrocnemius muscles expressed only the β2 transcript, and red gastrocnemius muscle expressed both mRNAs. All muscles tested expressed both α1 and α2 transcripts, albeit to various degrees: α1 transcripts were present to about the same extent in all muscles but α2 mRNA was 4-fold more abundant in soleus than in EDL for the same amount of total RNA. β subunit protein levels were investigated in purified plasma membrane fractions of pooled red (soleus + red gastrocnemius + red quadriceps) or white (white gastrocnemius + white quadriceps) muscles using isoform-specific antibodies. Red muscles expressed mostly the β1 protein while white muscles expressed mostly the β2 subunit. Both muscle groups had similar levels of α1 or α2 subunits, and crude membranes isolated from red muscles had 30% higher Na+,K+-ATPase activity than white muscle membranes. We conclude that oxidative muscles (slow and fast twitch) express β1 subunits, whereas glycolytic, fast twitch muscles express β2 subunits, and that both β isoforms support the Na+,K+-ATPase activity of the a subunits.Keywords
This publication has 25 references indexed in Scilit:
- The functional role of the β‐subunit in the maturation and intracellular transport of Na,K‐ATPaseFEBS Letters, 1991
- Mutual dependence of Na,K‐ATPase α‐ and β‐subunits for correct posttranslational processing and intracellular transportFEBS Letters, 1990
- Isozymes of the Na+/K+-ATPaseBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1989
- Antisera specific for the .alpha.1, .alpha.2, .alpha.3, and .beta. subunits of the sodium-potassium ATPase: differential expression of .alpha. and .beta. subunits in rat tissue membranesBiochemistry, 1989
- Maturation of the catalytic alpha-subunit of Na,K-ATPase during intracellular transport.The Journal of cell biology, 1987
- Insulin‐induced translocation of glucose transporters in rat hindlimb musclesFEBS Letters, 1987
- Effects of insulin upon ion transportBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1983
- A simple and rapid method for the determination of the number of 3H-ouabain binding sites in biopsies of skeletal muscleBiochemical and Biophysical Research Communications, 1983
- Mechanism of the Na+, K+ pump protein structure and conformations of the pureBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1982
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970