RESUMO
UNLABELLED: Heat shock proteins (HSPs) are conservative protective proteins responsible for protein integrity during transcription in the cell under stress. Hsp47 is one of the most important chaperonins for collagen synthesis and release, and is up-regulated during wound repair. The aim of this study was to verify whether defocused high-energy diode laser (DDL) causes sufficient increase in local temperature to cause Hsp47 up-regulation during repair of oral ulcers. Chemically-induced ulcers in the rat tongue, and non-ulcerated tongue mucosa were irradiated using a high energy diode laser (non-contact - 4mm from surface, 500 mW, 10 Hz for 40s, energy density 80 J/cm(2), fixed ulcer area of 0.25 cm(2)). Afterwards the specimens were submitted to immunohistochemical test for Hsp47. Temperature oscillation during DDL irradiation was also measured using a thermographic camera. Irradiated specimens exhibited transient mild increase in local temperature and significant up-regulation of Hsp47 in the mucosa from the superficial region (p=0.035) to 1.7 mm deep (p=0.049). In the deepest region of the mucosa Hsp47 was up-regulated only in ulcerated specimens mainly at 24h (p=0.049) and 72 h (p=0.029) after ulcer induction. CONCLUSION: DDL increases local temperature and Hsp47 expression, which may contribute to wound repair by improvement collagen synthesis and release.
Assuntos
Proteínas de Choque Térmico HSP47/biossíntese , Úlceras Orais/radioterapia , Cicatrização/fisiologia , Animais , Feminino , Lasers Semicondutores , Mucosa Bucal/metabolismo , Mucosa Bucal/efeitos da radiação , Úlceras Orais/metabolismo , Ratos , Temperatura , Regulação para Cima , Cicatrização/efeitos da radiaçãoRESUMO
OBJECTIVE: The purpose of the present study was to investigate the expression of the α2-integrin subunit and heat shock protein 47 (Hsp47) in two families with isolated gingival fibromatosis (GF) form and one family with GF associated with dental abnormalities and normal gingival (NG). STUDY DESIGN: Immunohistochemistry was performed with antibodies against α2-integrin and Hsp47 in specimens from two unrelated families with hereditary gingival fibromatosis (Families 1 and 2) and from one family with a gingival fibromatosis-associated dental abnormality (Family 3); NG samples were used for comparison. The results were analysed statistically. RESULTS: Immunoreactivity for α2-integrin and Hsp47 was observed in the nucleus of epithelial cells of both the basal and suprabasal layer and a more discreet signal was noted in connective tissue in all study samples. Hsp47 showed higher immunoreactivity in Family 2 compared with the other families (p ≤ 0.05). Despite the markup α2-integrin was higher in Family 3 there was no statistically significant difference between the families studied (p ≥ 0.05). CONCLUSIONS: Our results confirmed the heterogeneity of GF, such that similar patterns of expression of the condition may show differences in the expression of proteins such as Hsp47. Although no difference in α2-integrin expression was observed between GF and NG groups, future studies are necessary to determine the exact role of this protein in the various forms of GF and whether it contributes to GF pathogenesis.