Solvent Nephrotoxicity in Humans and Experimental Animals

Nelson, Nancy A.; Robins, Thomas G.; Port, Friedrich K.

doi:10.1159/000168048

Cited by 28 publications

(8 citation statements)

References 34 publications

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“…These findings suggest that very high exposures, rather than prolonged low exposures, cause severe damage in the renal system. This finding is in accordance with those of studies (15)(16) associating acute tubular necrosis with high levels of exposure to organic solvents.…”

Section: Discussionsupporting

confidence: 93%

Exposure to styrene and mortality from nonmalignant diseases of the genitourinary system

Welp

Partanen

Kogevinas

et al. 1996

Scand J Work Environ Health

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Section: Discussionsupporting

confidence: 93%

Exposure to styrene and mortality from nonmalignant diseases of the genitourinary system

Welp

Partanen

Kogevinas

et al. 1996

Scand J Work Environ Health

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“…Again, differences in the structure ofthe -56-kDa polypeptide subunit were noted. Work from several laboratories has subsequently revealed at least two isoforms for the vacuolar H+-ATPase -56-kDa subunit that are encoded by different genes (7)(8)(9). The present study examines how these isoforms might participate in the distinctive amplification and physiology of the vacuolar H+-ATPase observed in mammalian kidney.…”

mentioning

confidence: 92%

Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells.

Nelson

Guo

Masood

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

193

175

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The intercalated cells of the kidney collecting duct are specialized for physiologically regulated proton transport. In these cells, a vacuolar H+-ATPase is expressed at enormous levels in a polarized distribution on the plasma membrane, enabling it to serve in transepithelial H+ transport. In contrast, in most eukaryotic cells, vacuolar H+-ATPases reside principally in intracellular compartments to effect vacuolar acidification. To investigate the basis for the selective amplification of the proton pump in intercalated cells, we isolated and sequenced cDNA clones for two isoforms of the -56-kDa subunit of the H+-ATPase and examined their expression in various tissues. The predicted amino acid sequence of the isoforms was highly conserved in the internal region but diverged in the amino and carboxyl termini. mRNA hybridization to a cDNA probe for one isoform (the "kidney" isoformn) was detected only in kidney cortex and medulla, whereas mRNA hybridization to the other isoform of the -56-kDa subunit and to the H+-ATPase 31-kDa subunit was found in the kidney and other tissues. Immunocytochemistry of rat kidney with an antibody specific to the kidney isoform revealed intense staining only in the intercalated cells. Staining was absent from proximal tubule and thick ascending limb, where H+-ATPase was detected with a monoclonal antibody to the 31-kDa subunit of the H+-ATPase. This example ofspecific amplification ofan isoform of one subunit of the vacuolar H+-ATPase being limited to a specific cell type suggests that the selective expression of the kidney isoform of the -56-kDa subunit may confer the capacity for amplification and other specialized functions of the vacuolar H+-ATPase in the renal intercalated cell.Vacuolar H+-ATPases participate in a remarkably diverse variety of cellular functions. In the intracellular membrane compartments of eukaryotic cells, they acidify endosomes, lysosomes, and other components of the vacuolar system, serving in endocytosis and secretion (1). In cells specialized for H' transport, such as the renal intercalated cell (2, 3) and the osteoclast (4), vacuolar H+-ATPases reside in high densities in a polarized distribution on the plasma membrane, effecting transcellular proton transport. How the vacuolar class of H+-ATPases performs such diverse functions remains unknown. Accumulating evidence suggests that structural subsets of the vacuolar H+-ATPases exist that may have unique roles. In prior studies, we reported that a vacuolar H+-ATPase preparation isolated from bovine kidney microsomes could be resolved on an HPLC ion-exchange column as two peaks of activity that exhibited differences in the structure of their -56-kDa subunits on SDS/polyacrylamide gels (5). More recently, we found that H+-ATPase purified from different membrane compartments in the mammalian kidney varied in their structural and functional properties (6). Again, differences in the structure ofthe -56-kDa polypeptide subunit were noted. Work from several laboratories has subsequently revealed at least ...

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“…Previous case-control studies have primarily been conducted among patients with glomerulonephritis despite that most animal experiments have shown that solvent exposure leads to renal tubular damage (28,29). The only previous study of patients with CRF regardless of underlying disease (11) showed no more than a weak and statistically nonsignificant association with solvents overall.…”

Section: Discussionmentioning

confidence: 99%

Absence of Association between Organic Solvent Exposure and Risk of Chronic Renal Failure

Fored¹,

Nise²,

Ejerblad³

et al. 2004

Journal of the American Society of Nephrology

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Solvent Nephrotoxicity in Humans and Experimental Animals

Cited by 28 publications

References 34 publications

Exposure to styrene and mortality from nonmalignant diseases of the genitourinary system

Exposure to styrene and mortality from nonmalignant diseases of the genitourinary system

Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells.

Absence of Association between Organic Solvent Exposure and Risk of Chronic Renal Failure

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