Abstract
Usually increased presence of Heat Shock Proteins (HSPs) is considered to mediate inflammation process in Oral Lichen Planus (OLP) lesions, but in contrast HSP-70 expression found to be stable or even decreased in those lesions. The purpose of this study was to detect the serum titres of the HSP-70 in patients with OLP compared to healthy individuals, which may indicate an alternative, systemic role. Serum levels of HSP- 70 were detected by sandwich-ELISA in 45 patients with reticular (n=28) and erosive (n=17) OLP, respectively. A group of 35 healthy individuals was used as control. HSP-70 was detected in significantly increased levels in OLP (p<0.05) compared to controls. The increase was prominent in reticular-OLP (p<0.05), whereas no difference was observed between serum HSP-70 in erosive OLP compared to controls. These results indicate a systemic initiation of the immune response in the pathogenesis and process of OLP. The higher titres of HSP-70 in reticular but not erosive form of OLP indicate rather an immunoregulatory role in chronicity than in the acute inflammatory process of OLP. Consequently, the evaluation of serum imbalances of HSP-70 in OLP using ELISA may be a useful marker for disease's monitoring and/or efficacy of systemic treatment.
Highlights
Heat shock proteins (HSPs) are highly conserved proteins, essential for cell protection and survival, distributed in microorganisms and mammalian cells
Taking together the extended role of Heat Shock Protein 70 (HSP-70) in immunity and its non-altered, even decreased, expression in involved tissues, this study investigates, for the first time, the serum levels of HSP70 that may indicate an alternative systemic implication in Oral Lichen Planus (OLP) pathogenesis
The serum HSP-70 values in the different forms of OLP and controls are presented in figue 1 and table 1
Summary
Heat shock proteins (HSPs) are highly conserved proteins, essential for cell protection and survival, distributed in microorganisms and mammalian cells. They are induced by temperature as well as other physiological or pathological stressful events, acting as intracellular chaperones or as cytokine-like molecules[1,2]. Exogenous (from pathogens) and native (from host cells) HSPs can initiate innate and adaptive immunity, having a proinflammatory role, but they have been considered as autoantigens via a cross-reactive immune response[3,4]. HSP-70 is normally located within the cytoplasm as chaperone, playing a role in intracellular events (constitutively expression)[2]. Unlike other members of HSPs, HSP-70, seems to have an anti-proinflammatory effect, as shown in an experimental model of arthritis[6]
Sign-in/Register to view highlights & summary 
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call