Sj. Newsholme et Dm. Zimmerman, IMMUNOHISTOCHEMICAL EVALUATION OF CHEMICALLY-INDUCED RHABDOMYOSARCOMAS IN RATS - DIAGNOSTIC UTILITY OF MYOD1, Toxicologic pathology, 25(5), 1997, pp. 470-474
Monoclonal antibodies (mAbs) to selected muscle proteins were assessed
as potential immunohistochemical markers to assist in the definitive
diagnosis of poorly differentiated soft tissue sarcomas in rats. A ser
ies of 7 rat rhabdomyosarcomas (RMS) induced with nickel subsulfide we
re studied by light microscopy and were evaluated for immunoreactivity
to desmin, vimentin, fast (type II isoform) skeletal myosin, alpha-ac
tin (smooth muscle isoform), or MyoD1 (myogenic regulatory protein) mA
bs using an avidin-biotin-chromogen technique. Consecutive RMS slices
were fixed in 10% neutral buffered formalin (the fixative routinely us
ed in carcinogenicity bioassays) for periods of 3 days or 2 mo prior t
o paraffin embedding to determine the effect ol fixation time on immun
oreactivity. Desmin and vimentin mAbs bound to many cells of all tumor
s, but fixation for 2 mo resulted in irretrievable loss of desmin and
vimentin binding. Fast myosin and a-actin mAbs bound to many cells in
1 RMS but to <1% of the cells in the remainder. MyoD1 mAb bound to tum
or cell nuclei in 5/7 RMS with no loss of staining in tissue fixed for
2 mo. Results indicate that MyoD1 immunostaining, in contrast to desm
in, maintains its sensitivity following prolonged formalin fixation an
d may be of value to distinguish RMS from other soft tissue sarcomas i
n the rat.