PubMed · 7061714
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A M Lessells, R P Honan, N Y Haboubi, H H Ali, M J Greene. 1982. Death during prostatectomy.. https://doi.org/10.1136/jcp.35.1.117-a
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The hypothesis was tested that the absorption of labile Al in rats will increase when the Al-binding capacity of food components in the stomach is saturated. Male rats were exposed to 0, 10, 50, or 500 mg labile Al/L in acidic drinking water (pH 3) for 9 wk. The results show that labile Al in drinking water is complexed by feed constituents in the stomach of the rat in vivo, thus causing a nondetectable absorption of Al at 10 mg Al/L. An increased absorption of Al at 50 and 500 mg Al/L was associated with a saturation of the Al-binding capacity of feed components in the lumen of the stomach, causing the appearance of labile Al. Thus, the presence of labile Al in drinking water does not necessarily result in a high Al absorption when the water is ingested, since the bioavailability of labile Al is dependent both on the amount and composition of Al-binding components present in the gastrointestinal tract at the time of ingestion of the water. It is thus not possible to predict the body burden of Al in humans just by measuring the Al concentrations in drinking water. Even a further refining of the exposure measurement to include speciation of Al in the water may not markedly improve the prediction of the Al body burden. Future epidemiological studies must therefore be based on actual measurements of Al concentration in tissues or fluids from the study subjects.
Nerve growth factor (NGF) inhibits transepithelial HCO3- absorption in the rat medullary thick ascending limb (MTAL). To investigate the mechanism of this inhibition, MTALs were perfused in vitro in Na+-free solutions, and apical and basolateral membrane Na+/H+ exchange activities were determined from rates of pHi recovery after lumen or bath Na+ addition. NGF (0.7 nM in the bath) had no effect on apical Na+/H+ exchange activity, but inhibited basolateral Na+/H+ exchange activity by 50%. Inhibition of basolateral Na+/H+ exchange activity with ethylisopropyl amiloride (EIPA) secondarily reduces apical Na+/H+ exchange activity and HCO3- absorption in the MTAL (Good, D. W., George, T., and Watts, B. A., III (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 12525-12529). To determine whether a similar mechanism could explain inhibition of HCO3- absorption by NGF, apical Na+/H+ exchange activity was assessed in physiological solutions (146 mM Na+) by measurement of the initial rate of cell acidification after lumen EIPA addition. Under these conditions, in which basolateral Na+/H+ exchange activity is present, NGF inhibited apical Na+/H+ exchange activity. Inhibition of HCO3- absorption by NGF was eliminated in the presence of bath EIPA or in the absence of bath Na+. Also, NGF blocked inhibition of HCO3- absorption by bath EIPA. We conclude that NGF inhibits basolateral Na+/H+ exchange activity in the MTAL, an effect opposite from the stimulation of Na+/H+ exchange by growth factors in other systems. NGF inhibits transepithelial HCO3- absorption through inhibition of basolateral Na+/H+ exchange, most likely as the result of functional coupling in which primary inhibition of basolateral Na+/H+ exchange activity results secondarily in inhibition of apical Na+/H+ exchange activity. These findings establish a role for basolateral Na+/H+ exchange in the regulation of renal tubule HCO3- absorption.
Using surface enhanced Raman spectroscopy (SERS) which enables us to specifically detect traces of monomeric amphotericin B (AmB), we were able to show that in a 10(-5) M AmB suspension, the concentration of free drug was below 10(-8) M in the presence of low density lipoproteins (LDL) or plasma. The affinity constant of AmB for LDL determined from electronic absorption data, was found to be 4 x 10(6) M(-1). Therefore, since AmB appears to be in the majority bound to lipoproteins under in vivo conditions, its toxicity should not result from the induction of host-cell transmembrane permeability but rather from the internalization of the AmB-LDL complex.