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Mod Pathol. 1997 Sep;10(9):895-900.

Antibodies to desmin identify the blastemal component of nephroblastoma.

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University of Washington, Seattle, USA.


The blastemal component of Wilms' tumor (WT) might be indistinguishable histologically from other small, blue, round-cell tumors of childhood, including alveolar rhabdomyosarcoma (RMS), particularly in small biopsy specimens and in the setting of metastatic disease. Furthermore, there are currently no reliable blastemal markers. Deparaffinized sections of 9 formalin-fixed blastema-predominant WTs and 46 RMSs were immunostained with antibodies to desmin (D33), myogenin (F5D), MyoD1 (5.8A), and muscle-specific actins (HHF35), after heat-induced epitope retrieval. WE defined as positive those cases with more than 5% of cells immunostained (only nuclear staining was considered as positive for myogenin and MyoD1). Antibodies to desmin were positive in eight (89%) of nine cases of blastema-predominant WT; in contrast, no case was positive for any of the other muscle-associated proteins. Of the 46 cases of RMS, all were positive for desmin, 42 were positive for myogenin and MyoD1, and 43 were positive for muscle actins. Desmin immunoreactivity, of and by itself, cannot be considered specific for RMS, but when accompanied by immunoreactivity for other myogenic proteins, it is highly characteristic of RMS. Our data also suggest that desmin immunoreactivity, in the absence of other muscle-associated protein expression, might be considered a clue to the diagnosis of the blastemal WT. Particularly in the context of small biopsy specimens or in metastatic settings, the use of a panel of antibodies to desmin as well as to other myogenic proteins, such as MyoD1 or myogenin, can help to discriminate between WT and RMS. Additional studies are required to determine whether desmin immunoreactivity in the blastemal component of WT represents true desmin expression.

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