JBC Focus on PI3-Kinase with Echelon

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Volume 271, Number 37, Issue of September 13, 1996 pp. 22754-22758
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Identification of the Mammalian Na,K-ATPase beta 3 Subunit

(Received for publication, April 23, 1996, and in revised form, June 21, 1996)

Nasir Malik Dagger , Victor A. Canfield Dagger , Marie-Claire Beckers § , Philippe Gros § and Robert Levenson Dagger

From the Dagger  Department of Pharmacology, Penn State College of Medicine, Milton S. Hershey Medical Center, Hershey, Pennsylvania 17033 and the § Department of Biochemistry, McGill University, Montreal, Quebec, Canada H3G 1Y6

We have isolated and characterized cDNA clones encoding the human and rat Na,K-ATPase beta 3 subunit isoform. The human cDNA encodes a polypeptide of 279 amino acids that exhibits primary sequence and secondary structure similarities to Na,K-ATPase beta  subunit isoforms. Sequence comparisons showed that the human beta 3 subunit closely resembles the beta 3 subunit of Xenopus laevis (59% amino acid identity) and is less similar to the human Na,K-ATPase beta 1 and beta 2 subunits (38% and 48% amino acid identity, respectively). By analyzing the segregation of restriction fragment length polymorphisms among recombinant inbred strains of mice, we localized the beta 3 subunit gene to murine chromosome 7. Northern blot analysis revealed that the beta 3 subunit gene encodes two transcripts that are expressed in a variety of rat tissues including testis, brain, kidney, lung, stomach, small intestine, colon, spleen, and liver. Identification of the mammalian beta 3 subunit suggests an even greater potential for Na,K-ATPase isoenzyme diversity than previously realized.


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