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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    The journal of membrane biology 131 (1993), S. 43-53 
    ISSN: 1432-1424
    Keywords: erythrocytes (red blood cells) ; amiloride ; hypothermia (cold) ; cold-storage ; Na-H exchange ; Na-Mg exchange
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary Previous work showed that amiloride partially inhibits the net gain of Na in cold-stored red cells of guinea pig and that the proportion of unidirectional Na influx sensitive to amiloride increases dramatically with cooling. This study shows that at 37°C amiloride-sensitive (AS) Na influx in guinea pig red blood cells is activated by cytoplasmic H+, hypertonic incubation, phorbol ester in the presence of extracellular Cat2+ and is correlated with cation-dependent H+ loss from acidified cells. Cytoplasmic acidification increases AS Na efflux into Na-free medium. These properties are consistent with the presence of a Na-H exchanger with a H+ regulatory site. Elevation of cytoplasmic free Mg2− above 3 mm greatly increases AS Na influx: this correlates with a Na-dependent loss of Mg2−, indicating the presence of a Na-Mg exchanger. At 20°C activators of Na-H exchange have little or no further stimulatory effect on the already elevated AS Na influx. AS Na influx is much larger than either Na-dependent H+ loss or AS Na efflux at 20°C. The affinity of the AS Na influx for cytoplasmic H+ is greater at 20°C than at 37°C. Depletion of cytoplasmic Mg2+ does not abolish the high AS Na influx at 20°C. Thus, elevation of AS Na influx with cooling appears to be due to increased activity of a Na-H exchanger (operating in a “slippage” mode) caused by greater sensitivity to H+ at a regulatory site.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 99 (1979), S. 427-439 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Activities related to Na-K transport were measured in cell cultures of ground squirrel kidney cortex in order to compare these cells with those of intact kidney and of continuous cell lines. A microsomal preparation containing plasma membrane Na,K-ATPase from fresh kidney showed twice the activity of a similar preparation from 72-hour cultured cells. Na,K-ATPase of homogenates of 72-hour cells showed one-third to one-fourth the specific activity of that from 6-hour cultured cells. The associated K-dependent phosphatase activity also declined as a function of time in culture. The ouabain-sensitive influx of K into 6-hour cultured cells was twice as great as the K influx into 72-hour cells. The number of sites binding 3H-ouabain in intact cultured cells declined 81% on a cell protein basis between 6 and 72 hours in culture. This decline in ouabain binding sites was relatively greater than that of K influx, so that the K turnover number increased over this same time period.The decline in ouabain-sensitive K influx during culture was complementary to an increase in furosemide-sensitive K influx. Measurements of unidirectional and net K fluxes showed that there were three components of K influx into 3-day cultured cells: ouabain-sensitive Na:K exchange, furosemide-sensitive K:K exchange, and K diffusion. In the 6-hour cultures, however, there was no furosemide-sensitive K:K exchange.Thus, after three days in culture ground squirrel kidney cells lose a feature characteristic of the original parent cells (high Na,K-ATPase activity), and gain a feature common to many undifferentiated cultured cells (furosemidesensitive K:K exchange).
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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