Published Paper Details:

Heat shock proteins (HSPs) are a conserved family of molecular chaperones that maintain protein homeostasis under physiological and stress conditions. In the oral environment, HSPs such as HSP27, HSP60, HSP70, and HSP90 are constitutively expressed in mucosa, salivary glands, and dental pulp, and their expression is upregulated by thermal, oxidative, or microbial stress. Beyond their canonical roles in protein folding and degradation, HSPs act as danger-associated molecular patterns (DAMPs) to modulate innate and adaptive immunity, participate in wound healing, and preserve tissue integrity. In oral pathology, aberrant HSP expression has been implicated in infections (e.g., Candida, Streptococcus), inflammatory conditions (periodontitis, peri-implantitis, pulpitis), and odontogenic lesions (keratocysts, ameloblastomas). In potentially malignant disorders such as leukoplakia and lichen planus, elevated HSP27 and HSP70 levels correlate with dysplastic severity, while in oral squamous cell carcinoma (OSCC), overexpression of HSP27, HSP70, and HSP90 promotes tumor cell survival, invasion, and chemoresistance. These findings underscore the diagnostic and prognostic potential of HSPs as biomarkers. Moreover, pharmacologic modulation of HSP activity--via HSP90 inhibitors (e.g., geldanamycin analogs), HSP70 ATPase blockers, or HSF-1 antagonists--offers novel therapeutic avenues. However, monotherapy may induce compensatory chaperone upregulation; thus, combination strategies targeting multiple HSPs or integrating conventional therapies may be required. Continued investigation into HSP localization, post-translational regulation, and interplay with oral microenvironmental cues will advance our understanding and enable translation into clinical practice.