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  • 1
    Electronic Resource
    Electronic Resource
    Primary sequence and functional expression of a novel β subunit of the P-ATPase gene family (1993)
    Springer
    Pflügers Archiv 425 (1993), S. 446-452 
    Details
    ISSN: 1432-2013
    Keywords: Na/K-ATPase ; H/K-ATPase ; P-ATPase ; β subunit isoforms ; Sodium pump current
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The cortical collecting tubule (CCT) of the mammalian kidney reabsorbs sodium and potassium, processes that are mediated by Na/K-ATPase and H/K-ATPase. CCT is also an important site for proton secretion, which is driven, in part, by H/K-ATPase. Na/K-ATPase and H/K-ATPase are members of the ion-motive P-ATPase gene family. They are closely related plasma membrane proteins which consist of αβ heterodimers. The urinary bladder of the toad Bufo marinus is the amphibian counterpart of mammalian CCT. We have previously characterized a ouabain-resistant Na/K-ATPase [see ref. 17], from TBM cells, a clonal cell line derived from the toad bladder, which expresses transepithelial sodium transport. In the present study, we report the primary sequence and functional expression of a novel β subunit (β bladder=β bl) isolated from a toad bladder epithelial cell cDNA library. The deduced polypeptide is 299 amino acids in length and has a predicted molecular mass of 33 kDa. The β bl protein exhibits 35% amino acid identity to the previously characterized β 1 of B. marinus Na/K-ATPase and 39% identity with β 3 of B. marinus Na/K-ATPase. It shares 38% identity with the mammalian β gastric H/K-ATPase and 52% with the mammalian β 2 Na/K-ATPase. Northern blot analysis shows that a 1.4×103-base mRNA is expressed at a high level in bladder epithelial cells and eye and at a trace level in kidney; it is not detectable in significant amounts in the stomach, colon and small intestine. The β bl subunit can associate with the α 1 subunit of B. marinus Na/K-ATPase to form a functional sodium pump in the Xenopus laevis oocyte. Our data indicate that, in addition to the known β 1 and β 3 isoforms, a third distinct isoform of the β subunit is present in the bladder epithelium. This new isoform could be functionally associated with α subunits of either Na/K- or H/K-ATPase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00374871
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  • 2
    Electronic Resource
    Electronic Resource
    Thyroid hormone antagonizes an aldosterone-induced protein: A candidate mediator for the late mineralocorticoid response (1986)
    Springer
    The journal of membrane biology 89 (1986), S. 173-183 
    Details
    ISSN: 1432-1424
    Keywords: Bufo marinus ; triiodothyronine ; hormonal domain ; aldosterone ; sodium butyrate ; transepithelial sodium transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary In the urinary bladder of the toadBufo marinus, the basal rate of synthesis of a number of proteins was modulated in a bidirectional way (i.e., induced or repressed) by aldosterone and by triiodothyronine (T3). Each hormone was therefore characterized by a distinct domain of response. When both hormones were added simultaneously, the two domains consistently overlapped at least for one protein, termed AIP-1, or aldosterone-induced protein 1 (M r≈65 kilodaltons,p i=6.7, as analyzed by two-dimension gel electrophoresis). The physiological role of AIP-1 is unknown, but could be related to the late mineralocorticoid response. In five experiments, T3 (60nm, 18-hr incubation) consistently repressed AIP-1, while aldosterone-dependent sodium transport (late response) was significantly inhibited, as previously described. The repression of AIP-1 was also observed as early as 6 hr after aldosterone addition. In addition, sodium butyrate (3mm), which was previously shown to also selectively inhibit the late mineralocorticoid response, was also able to repress AIP-1. Our results suggest that AIP-1, is one of the proteins involved in the mediation of the late mineralocorticoid response.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01869713
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    Paper (German National Licenses)
    Fulltext
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