Apoptosis and anti-apoptotic heat shock proteins in canine cutaneous infundibular keratinizing acanthomas and squamous cell carcinomas.
Cell stress and death are linked in the neoplastic process, and heat shock proteins appear to play an important role by inhibiting apoptotic pathways. The apoptotic rates in 9 canine infundibular keratinizing acanthomas (IKAs) and 17 canine squamous cell carcinomas (SCCs) were correlated with the immunohistochemical expression of caspase-3 and the antiapoptotic heat shock proteins Hsp27, 72 and 73. Apoptosis was evaluated using the terminal deoxynucleotidyl transferase biotin-dUTP nick end labelling (TUNEL) method. The absence of a correlation between the TUNEL index and active-caspase-3 expression, a paucity of active-caspase-3-positive cells and Hsp72 over-expression were considered to be indicative of inhibition of apoptosis, and suggestive that inhibition of cell death plays a key role in oncogenesis and tumour growth of some canine skin neoplasms.
Bongiovanni
Laura
L
Department of Comparative Biomedical Sciences, Faculty of Veterinary Medicine, University of Teramo, Piazza Aldo Moro, 45-64100 Teramo, Italy.
Romanucci
Mariarita
M
Fant
Pierluigi
P
Lagadic
Marie
M
Della Salda
Leonardo
L
D049309:Acanthoma / Q000473:pathology / Q000662:veterinary*; D000818:Animals; D017209:Apoptosis / Q000235:genetics / Q000502:physiology*; D002294:Carcinoma, Squamous Cell / Q000473:pathology / Q000662:veterinary*; D004283:Dog Diseases / Q000378:metabolism*; D004285:Dogs; D005786:Gene Expression Regulation; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D007150:Immunohistochemistry / Q000662:veterinary; D020287:In Situ Nick-End Labeling
D006360:Heat-Shock Proteins