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  • American Physiological Society  (4)
  • 1995-1999  (4)
Type of Medium
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  • American Physiological Society  (4)
Language
Years
  • 1995-1999  (4)
Year
  • 1
    Online Resource
    Online Resource
    American Physiological Society ; 1997
    In:  American Journal of Physiology-Renal Physiology Vol. 273, No. 5 ( 1997-11-01), p. F801-F806
    In: American Journal of Physiology-Renal Physiology, American Physiological Society, Vol. 273, No. 5 ( 1997-11-01), p. F801-F806
    Abstract: Chronic restriction of dietary P i elicits an increased reabsorption of P i in the kidney proximal tubules, which involves a stimulation of apical Na-P i cotansport. This adaptation is in part a direct cellular response of which the mechanism(s) are poorly understood. In this study, the impact of dietary P i restriction on the differential expression of rat kidney cortex mRNAs was visualized to identify gene products regulated by the P i status. When kidney cortex mRNAs of rats fed a low- or a high-P i diet were compared by differential display-polymerase chain reaction (DD-PCR), thirty modulated cDNA bands were observed, of which four were confirmed as being regulated. We focused on one of the upregulated bands, dietary P i -regulated RNA-1 (diphor-1). A cDNA containing an open reading frame encoding a 52-kDa protein was cloned by library screening. Diphor-1 exhibits a high degree of identity to the Na/H exchanger regulatory factor and to a tyrosine kinase activating protein. Highest expression of diphor-1 mRNA was detected in the kidney (proximal tubules) and in small intestine. Expression experiments showed that diphor-1 specifically increases Na-P i cotransport in oocytes of Xenopus laevis coinjected with renal type II Na-P i cotransporter cRNA. Further characterizations of diphor-1 will show whether diphor-1 is primarily or secondarily involved in the response to dietary P i .
    Type of Medium: Online Resource
    ISSN: 1931-857X , 1522-1466
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1997
    detail.hit.zdb_id: 1477287-5
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  • 2
    Online Resource
    Online Resource
    American Physiological Society ; 1997
    In:  American Journal of Physiology-Cell Physiology Vol. 272, No. 2 ( 1997-02-01), p. C697-C706
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 272, No. 2 ( 1997-02-01), p. C697-C706
    Abstract: The contribution of ATP-generating systems to Na+ pump (Na+-K+-ATPase) function was studied in Xenopus laevis A6 kidney epithelia apically permeabilized with digitonin. The ouabain-inhibitable Na+ pump current (I(P)) was measured in the presence of otherwise impermeant inhibitors and/or substrates at Na+ and K+ concentrations that allowed near-maximal pump function. Confocal fluorescence microscopy after apical addition of sulfosuccinimidobiotin (molecular weight of 443) showed that all cells were permeabilized. Less than 15% of the endogenous lactate dehydrogenase and creatine kinase (CK) were released into the apical medium. The I(P) was approximately 5 microA/cm2 in the presence of D-glucose. Blocking glycolysis with 2-deoxy-D-glucose or oxidative phosphorylation with antimycin A decreased it by 〉 or = 50%. Exogenously added ATP prevented these decreases fully or partially, respectively. Two CK isoforms were detected, one likely being mitochondrial and the other corresponding to mammalian B isoform of CK. Phosphocreatine partially restored Na+ pump activity during inhibition of either ATP synthesis pathway. In conclusion, the ATP used by Na+ pumps of apically digitonin-permeabilized A6 epithelia is generated to a similar extent by glycolysis and oxidative phosphorylation. The CK system can partially support the ATP supply to the Na+ pumps.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1997
    detail.hit.zdb_id: 1477334-X
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    American Physiological Society ; 1999
    In:  American Journal of Physiology-Endocrinology and Metabolism Vol. 277, No. 2 ( 1999-08-01), p. E352-E360
    In: American Journal of Physiology-Endocrinology and Metabolism, American Physiological Society, Vol. 277, No. 2 ( 1999-08-01), p. E352-E360
    Abstract: We characterized the effects of calorie restriction (CR) on the expression of key glycolytic, gluconeogenic, and nitrogen-metabolizing enzymes in mice. Of the gluconeogenic enzymes investigated, liver glucose-6-phosphatase mRNA increased 1.7- and 2.3-fold in young and old CR mice. Phospho enolpyruvate carboxykinase mRNA and activity increased 2.5- and 1.7-fold in old CR mice. Of the key glycolytic enzymes, pyruvate kinase mRNA and activity decreased ∼60% in CR mice. Hepatic phosphofructokinase-1 and pyruvate dehydrogenase mRNA decreased 10–20% in CR mice. Of the genes that detoxify ammonia generated from protein catabolism, hepatic glutaminase, carbamyl phosphate synthase I, and tyrosine aminotransferase mRNAs increased 2.4-, 1.8-, and 1.8-fold with CR, respectively. Muscle glutamine synthetase mRNA increased 1.3- and 2.1-fold in young and old CR mice. Hepatic glutamine synthetase mRNA and activity each decreased 38% in CR mice. These CR-induced changes are consistent with other studies suggesting that CR may decrease enzymatic capacity for glycolysis and increase the enzymatic capacity for hepatic gluconeogenesis and the disposal of byproducts of muscle protein catabolism.
    Type of Medium: Online Resource
    ISSN: 0193-1849 , 1522-1555
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1999
    detail.hit.zdb_id: 1477331-4
    SSG: 12
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  • 4
    Online Resource
    Online Resource
    American Physiological Society ; 1999
    In:  American Journal of Physiology-Cell Physiology Vol. 276, No. 5 ( 1999-05-01), p. C1154-C1161
    In: American Journal of Physiology-Cell Physiology, American Physiological Society, Vol. 276, No. 5 ( 1999-05-01), p. C1154-C1161
    Abstract: Adrenal steroids induce an increase in transcellular Na + reabsorption across Xenopus laevis A6 cell epithelia that requires the action of transcriptionally regulated gene products. In a previous study we identified K- ras2 as an aldosterone-upregulated mRNA in A6 epithelia. Here, we show that in vivo injection of aldosterone in Xenopus (2.5 h) increases K- ras2 mRNA specifically in the kidney (2.5-fold) and that in A6 epithelia aldosterone (2.5 h) increases Ras protein synthesis (∼6-fold). Xl- ras, another ras mRNA expressed at a low level in A6 cells, was also induced (2-fold). Aldosterone was shown to regulate the mRNA levels of several transcription factors as well. After 2 h of aldosterone treatment, fra-2 mRNA was upregulated by 130%, whereas c- myc, c- jun, c- fos, and glucocorticoid receptor mRNAs were downregulated by 23–43%. After 16 h, c- fos and GR mRNAs were further decreased, whereas levels of fra-2, c- jun, and c- myc began to return to control levels. Interestingly, the downregulation of the protooncogene mRNAs was independent of transcription. These results support the view that aldosterone exerts complex pleiotropic transcriptional and nontranscriptional actions that involve the regulation of signaling cascade elements (i.e., K-Ras2) as well as that of transcription factors.
    Type of Medium: Online Resource
    ISSN: 0363-6143 , 1522-1563
    Language: English
    Publisher: American Physiological Society
    Publication Date: 1999
    detail.hit.zdb_id: 1477334-X
    SSG: 12
    Library Location Call Number Volume/Issue/Year Availability
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