HSP32 and HSP90 Immunoexpression, in Relation to Kit Pattern, Grading, and Mitotic Count in Canine Cutaneous Mast

M Romanucci1, M Massimini1, A Ciccarelli2

  • 11 Faculty of Veterinary Medicine, University of Teramo, Teramo, Italy.

Veterinary Pathology
|September 16, 2016
PubMed

Insights

Heat shock proteins (Hsp) 32 and 90 were studied in canine mast cell tumors (MCTs). Reduced Hsp32 was seen in high-grade MCTs, suggesting potential in poorly differentiated tumors.

Area of Science:

  • Veterinary Pathology
  • Oncology
  • Molecular Biology

Background:

  • Heat shock proteins (Hsp) 32 and 90 are implicated as molecular targets in canine neoplastic mast cells (MCs).
  • Immunohistochemical patterns of Hsp32 and Hsp90 in canine mast cell tumors (MCTs) remain uninvestigated.

Purpose of the Study:

  • To evaluate the immunohistochemical expression of Hsp32 and Hsp90 in canine cutaneous MCTs.
  • To correlate Hsp expression with KIT immunolabeling, histological grade, and mitotic count.

Main Methods:

  • Immunohistochemistry was performed on 22 canine cutaneous MCT samples.
  • Analysis focused on cytoplasmic, nuclear, and membranous labeling patterns of Hsp32 and Hsp90.
  • Correlations were assessed against KIT patterns, histological grade, and mitotic counts.

Main Results:

  • All cases exhibited cytoplasmic Hsp90 labeling, with variable nuclear/membranous co-expression.
  • No significant relationships were found between Hsp90 or Hsp32 expression and KIT pattern, mitotic count, or tumor grade.
  • A trend towards reduced Hsp32 immunoexpression was observed in high-grade (grade III) MCTs.

Conclusions:

  • Reduced Hsp32 expression in high-grade MCTs suggests potential loss of immunosignal in poorly differentiated mast cells.
  • Heterogeneity in Hsp90 expression may complicate predicting the efficacy of Hsp90 inhibitors in canine MCTs.
  • Further research is needed to elucidate the precise roles of Hsp32 and Hsp90 in canine MCT pathogenesis and treatment.

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