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  • 1
    Electronic Resource
    Electronic Resource
    Elevated concentrations of the β-subunit of S100 protein in renal cell tumors in rats (1994)
    Springer
    Urological research 22 (1994), S. 251-255 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00541902
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  • 2
    Electronic Resource
    Electronic Resource
    Elevated concentrations of the small stress protein HSP27 in rat renal tumors (1997)
    Springer
    Urological research 25 (1997), S. 173-177 
    Details
    ISSN: 1434-0879
    Keywords: αB crystallin ; Heat shock protein ; Rat ; Kidney neoplasms
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The expression of two small stress proteins, αB crystallin and the 27-kDa heat shock protein (HSP27), was studied quantitatively and immunohistochemically in normal kidney and renal tumors in rats. Levels of αB crystallin in renal cell tumors tended to be higher than in normal kidney (P = 0.07), but with a wide range of values, whereas they were significantly lower in mesenchymal tumors (P 〈 0.0001). In contrast, HSP27 concentrations in both renal cell (mean ± SD: 1790 ± 940 ng/mg protein,n = 15) and mesenchymal (1260 ± 1080 ng/mg protein,n = 10) tumors were significantly higher than the normal kidney value (142 ± 30 ng/mg protein,n = 10,P 〈 0.0001). A positive correlation was found between αB crystallin and HSP27 levels limited to the renal cell tumor case (Pearson's correlation coefficient,r = 0.68,P 〈 0.01). Immunohistochemistry revealed the loops of Henle to be positive for αB crystallin, whereas HSP27 staining was positive in glomerular and interstitial vascular walls and epithelial cells of proximal and distal tubules. Positive immunostaining for αB crystallin was demonstrated in six of nine renal cell tumors (67%) studied and for HSP27 in all of the nine cases (100%).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00941978
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Elevated concentrations of γ-enolase in renal cell tumors in rats: similarity to renal cell carcinoma in man (1996)
    Springer
    Urological research 24 (1996), S. 375-379 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00389796
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    Paper (German National Licenses)
    Fulltext
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