• Journal of Oral Medicine and Pain
• /
• v.37 no.4
• /
• pp.195-203
• /
• 2012

Recurrent aphthous ulcer(RAU) is the most frequent form of oral ulceration with a prevalence in the general population ranging between 5% and 60%. The peak age of onset is between 10 and 19 years of age, and it can persist into adulthood and throughout the patient's lifespan, with no gender predilection. The disease is characterized clinically into three types: minor aphthous ulcer, major aphthous ulcer and herpeticform ulcers. The cause of RAU is unknown and thought to be multifactorial with many triggers or precipitating factors that include familial tendency or genetic predisposition, allergy, medications, hormones, stress or anxiety, and immunologic abnormalities. The need for consideration of psychological factors in the pathogenesis of oral disease has been increasingly acknowledged over the last decades and many studies have highlighted the psycho-social impact of oral conditions. In this study, we tried to evaluate the influence of emotional stress in RAU. There were thirty patients with a clinical diagnosis of RAU and other subjects who did not show any signs of systemic disorders include RAU. They are evaluated by using modified Holmes and Rahe's Social Readjustment Rating Scale (SRRS). As a result, a significantly higher level of stress was found in the RAU patients than the control group. Therefore it can be concluded that psychological stressors play an important role in the RAU.

• Korean Journal of Microbiology
• /
• v.38 no.3
• /
• pp.153-161
• /
• 2002

Sox4, a transcription factor, consists of three functional domains: an HMG-box domain as a DNA binding domain, serine rich region as a transactivation domain and glycine rich region (GRR), an unknown functional domain. Although Sox4 is known to be functionally involved in heart, B-cell and reproductive system development, its physiological function remains to be elucidated. We used pGEX expression system to develop a simple and rapid method for purifying Sox4 protein in suitable forms for biochemical studies of their functions. Unexpectedly, we observed that full-length Sox4 appears to be protease-sensitive during expression and purification in E. coli. To map the protease-sensitive site in Sox4, we generated various constructs with each of functional domains of Sox4 and purified as the GST-Sox4 fusion proteins using glutathione beads. We found that the specific cleavage site for the proteolytic enzyme, which exists in E. coli, is localized within the novel GRR of Sox4. Our study suggest that the GRR of Sox4 may a target for the cellular protease action and this cleavage in the GRR may be involved in regulating physiological function of Sox4. Additionally, our study may provide a useful method for investigating the proteolytic cleavage of the target molecule in E. coli.