Nucleotide sequence of a cDNA for the beta 2 subunit isoform of Na+,K(+)-ATPase from human retina.
نویسندگان
چکیده
Using as probe the entire human liver cDNA clone coding for the beta 2 subunit isoform of the Na+,K(+)-ATPase, which lacks the initiation codon ATG, and the entire 5'-untranslated region (Martin-Vasallo, P., Dackowski, W., Emanuel, J.R. and Levenson, R. (1989) J. Biol. Chem. 264, 4613-4618), we isolated a larger clone from a directional human adult retina cDNA library (Swaroop, A. and Xu, J. (1993) Cytogenet. Cell Genet. 64, 292-294). This clone, pNH beta 2, shows 100% homology with the nucleotide sequence of the human liver cDNA clone and also contains additional 407 nucleotides in the 5'-untranslated region, the initiation codon and a poly(A) tail. Northern blot hybridization analysis reveals that the human mRNA (3.6 kb) is approx. 300 nucleotides larger than the major transcript size expressed in rat (3.3 kb). The larger human size mRNA for the human beta 2 Na+,K(+)-ATPase indicates species differences in gene processing.
منابع مشابه
Characterization of a beta subunit of the gastric H+/K(+)-transporting ATPase.
The catalytic subunit of the H+/K(+)-transporting ATPase (EC 3.6.1.3) has 62% identity to the alpha, or catalytic subunit, of the Na+/K(+)-transporting ATPase (EC 3.6.1.37); however, a homologous beta subunit was unknown until recently. Removal of the carbohydrate from purified hog H+/K(+)ATPase vesicles reveals a 35-kDa peptide that, when fragmented with protease V8, gives sequences homologous...
متن کاملPartial Cloning and Nucleotide Sequencing of Glutamate Decarboxylase Gene Isoform 65 from Human Brain
Background: Gamma -aminobutyric acid (GABA), a non-protein amino acid acts as an inhibitory neurotransmitter in the central nervous system of mammalians. The glutamate decarboxylase (GAD) is responsible for the conversion of L-glutamate to GABA. The human brain has two isoforms of this enzyme, GAD65 and GAD67 that differ in molecular weight, amino acid sequence, antigenicity, cellular location ...
متن کاملDevelopmental changes in erythrocyte Na(+),K(+)-ATPase subunit abundance and enzyme activity in neonates.
AIM To study the relation between erythrocyte Na(+),K(+)-ATPase subunit isoform composition, Na(+),K(+)-ATPase activity, and cation pump function in preterm and term neonates. DESIGN Erythrocyte Na(+),K(+)-ATPase subunit isoform abundance, Na(+),K(+)-ATPase activity, and cation pump function were studied in blood samples obtained from 56 preterm neonates of 28-32 weeks gestation (group 1), 58...
متن کاملO-10: A Marked Animal-Vegetal Polarity in The Localization of Na+,K+-ATPase Activity and Its Down-Regulation Following Progesterone-Induced Maturation
Background: Polarized cells are key to the process of differentiation. Xenopus oocyte is a polarized cell that has complete blue-print to differentiate 3 germ layers following fertilization, as key determinant molecules (Proteins and RNAs) are asymmetrically localized. The objective of this work was to localize Na+, K+-ATPase activity along animal-vegetal axis of polarized Xenopus oocyte and fo...
متن کاملSelective basolateral localization of overexpressed Na-K-ATPase beta1- and beta2- subunits is disrupted by butryate treatment of MDCK cells.
The exclusive basolateral localization of the Na-K-ATPase in kidney epithelium is a critical aspect of nephron function. It has been suggested that mislocalized delivery of the Na-K-ATPase to the apical surface in autosomal dominant polycystic kidney disease (ADPKD) is due to the inappropriate expression of an alternative isoform of the beta-subunit, the beta(2)-isoform. It has been reported th...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Biochimica et biophysica acta
دوره 1189 1 شماره
صفحات -
تاریخ انتشار 1994