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      Renal Handling of Aluminium

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          Aluminium (Al) is absorbed from a variety of foodstuffs and medications. Its major route of elimination from the body is in the urine. However, current knowledge concerning its glomerular filtration and, more particularly, its reabsorption/secretion is fragmentary. Most (80–90%) of Al in the plasma is normally bound to protein (mainly transferrin) and is therefore unfilterable; the remainder is bound to low molecular mass compounds, of which citrate appears to be the most important. In vitro determinations using artificial membranes indicate that ∼10% of Al is filtered at normal plasma concentrations. However, when plasma Al is raised experimentally, its filterability falls, unless the excess Al is complexed with citrate; the aluminium citrate complex appears to be freely filtered. Information on tubular Al reabsorption at normal plasma concentrations is inconsistent. Filtered Al appears to be at least partially reabsorbed, although the reabsorptive mechanisms remain speculative. A consensus is emerging that elevated plasma Al concentrations result in a fall in fractional Al reabsorption, and a recent micropuncture study indicates that under these circumstances the only significant site of Al reabsorption is the loop of Henle.

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          Most cited references 13

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          cDNA cloning of MCT2, a second monocarboxylate transporter expressed in different cells than MCT1.

          Low stringency screening of a cDNA library from hamster liver yielded a cDNA encoding MCT2, a monocarboxylate transporter that is 60% identical to hamster MCT1, the first monocarboxylate transporter to be isolated. The functional properties of the two MCTs were compared by expression in Sf9 insect cells using recombinant baculovirus vectors. Like MCT1, MCT2 transported pyruvate and lactate. The two transporters were sensitive to inhibition by phloretin and by alpha-cyano-4-hydroxycinnamate. MCT1, but not MCT2, was sensitive to organomercurial thiol reagents such as p-chloromercuribenzoic acid. Immunoblotting and immunofluorescence studies revealed a strikingly different tissue distribution of the two MCTs. MCT1 was present in erythrocytes and on the basolateral surfaces of intestinal epithelial cells. MCT2 was not detectable in these tissues, but it was abundant on the surface of hepatocytes. In the stomach, MCT1 was present on the basolateral surfaces of epithelial cells; in contrast, MCT2 was expressed on parietal cells of the oxyntic gland. In the kidney, MCT1 was present on the basolateral surfaces of epithelial cells in proximal tubules, whereas MCT2 was restricted to the collecting ducts. MCT1 was expressed on sperm heads in the testis and proximal epididymis. In the distal epididymis, it disappeared from sperm and appeared on the microvillar surface of the lining epithelium. In contrast, MCT2 was present on sperm tails throughout the epididymis and not on the epithelium. Both transporters were expressed in mitochondria-rich (oxidative) skeletal muscle fibers and cardiac myocytes. These findings suggest that MCT1 and MCT2 are adapted to play different roles in monocarboxylate transport in different cells of the body.
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            Al and Si: their speciation, distribution, and toxicity.

            In dialysis patients both aluminum (AI) and silicon (Si) may accumulate. Whereas the toxic effects of AI within this population are clearly established, little is known on the role of Si in the development/protection of particular dialysis-related diseases. A clear insight in the protein binding and speciation of trace elements is important to better understand the mechanisms underlying their toxicity/essentiality. Research in this field however is complex and often prone to analytical difficulties and inaccuracies.
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              Investigation of the aluminium biokinetics in humans: a 26Al tracer study


                Author and article information

                Nephron Physiol
                Nephron Physiology
                S. Karger AG
                December 2005
                14 November 2005
                : 101
                : 4
                : p99-p103
                aDepartment of Physiology and Centre for Nephrology, University College London, London, and bDivision of Medical Sciences, University of Birmingham, Birmingham, UK
                88331 Nephron Physiol 2005;101:p99–p103
                © 2005 S. Karger AG, Basel

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                Figures: 2, References: 23, Pages: 1
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/88331


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