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  • 1
    ISSN: 1434-0879
    Keywords: S100 protein ; Rat ; Carcinogenesis ; Renal neoplasms
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Concentrations of α and β-subunits of S100 protein (S100-α and S100-β) in rat kidney neoplasms, including renal cell and mesenchymal tumors, were determined using a highly sensitive enzyme immunoassay, and both types immunohistochemically localized in tissue sections. Concentration of S100-α in each histological type of rat tumor were lower than in normal kidney, whereas levels of S100-β (mean±SE: 29.7±14.2 ng/mg protein, n=15) in renal cell tumors were significantly higher than in normal kidneys (0.55±0.06 ng/mg protein, n=7), or mesenchymal tumors (1.21±0.43 ng/mg protein, n=9). In normal rat kidney tissues S100-α was immunohistochemically positive in epithelial cells of the distal tubules, the thin limbs of loops of Henle, and the collecting ducts. No appreciable immunostaining for S100-β was found in any nephron segment. Both S100-α and S100-β were positive for renal cell tumors, indicating new appearance of the latter during renal carcinogenesis in rats.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1434-0879
    Keywords: Enolase ; Isozymes ; Rat ; Renal neoplasms
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Concentrations of enolase isozymes in normal kidney and renal cell tumors in rats were determined using a highly sensitive enzyme immunoassay, and the isozymes were immunohistochemically localized in tissue sections. Levels of α-enolase in renal cell turnors were significantly lower than in normal kidney, whereas those of γ-enolase were significantly elevated (mean ±SD:211±129 ng/mg protein, n=15, as compared to 27.1±2.9 ng/mg protein, n=7). The proportion of γ-enolase in the total enolases in the tumor tissues (1.6±0.5%) was significantly higher than in normal kidney (0.15±0.005). Immunohistochemistry revealed epithelial cells of all nephron segments to be positive for the α-isozyme, whereas γ-enolase staining was strongly positive only in the loops of Henle, being faint in the distal tubules and absent in the proximal tubules. Both α- and γ-enolases demonstrated positive immunostaining in all of the seven renal cell tumors studied. These findings indicate that an isozyme switch from α- to γ-enolase occurs during rat kidney carcinogenesis, taking into account the derivation from proximal tubules, consistent with the findings for renal cell carcinomas in man.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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