AOKI Y. KANAZAWA MEDICAL UNIVERSITY, Department of Medicine, Assistant Professor, 医学部, 助手 (90319054)
YOSHIDA J. KANAZAWA MEDICAL UNIVERSITY, Department of Medicine, Assistant Professor, 医学部, 助手 (40257473)
|Budget Amount *help
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 2002: ¥1,300,000 (Direct Cost: ¥1,300,000)
Fiscal Year 2001: ¥900,000 (Direct Cost: ¥900,000)
Human scar and Keloid tissues collected on plastic surgery were harvested for immunohistochemistry. For cytoskeleton, antibodies against human alpha smooth muscle actin, alpha actinin, vinculin, paxillin, and FAK were used. For small G proteins, antibodies against human Rho and Ras were used. Immunolocalization of several factors such as Egr-1, p38, ERK-2 which may contribute to the activities of small G proteins were also investigated. Furthermore, immunolicalization RGSs were investigated to determine the possibilities of cross talk between small G proteins and heterotrimeric G proteins. As a result, immunoreactivities of most of the antibodies were weak in normal skin and atrophic scar tissues. In hypertrophic scar tissues, FAK were detected diffusely in dermal fibroblasts. Vinculin and alpha actinin were detected weakly in scar fibroblasts. Among a mall molecular weight G proteins, Immunostaining against Rho subfamilies such as RhoA, RhoB, and RhoG were constantly positive in hypertrophic scar fibroblasts. Similar findings were seen in Immunostaining against Ras subfamilies. Furthermore, strong positive staining against Ras subfamilies were seen in inflammatory cells in granulation tissue. Among the RGSs tested in this study, RGS7 was positively stained in hypertrophic scar fibroblasts as well as some fibroblasts in nodule of keloid tissues. From these findings, some positive correlations among hypertrophic scarring, small molecular weight G protein Rho, and cytoskeleton were indicated. Furthermore, it is also speculated that heterotrimeric G proteins may have some influence upon scarring via under control of RGS7.