## 4 Discussion
The extracellular HSPs can activate inflammatory pathways, fostering a microenvironment conducive to tumor progression [42]. Additionally, HSPs can indirectly contribute to carcinogenesis through epigenetic interactions involving HSP receptors and translation factors such as hsf-1. Moreover, a noteworthy category of cellular pathways in which these molecules participate in the carcinogenesis process involves a set of post-translational modifications, including sumoylation, methylation, and phosphorylation, which their domains, such as the AKT domain or C-terminal domain, and their receptors undergo [33]. Moreover, another avenue through which HSPs promote tumor growth and impede therapeutic intervention lies in their role in fostering resistance to chemotherapy and radiation. Indeed, empirical observations have indicated that when tumor cells are subjected to treatments such as ionizing radiation or alkylating agents, the HSP family actively undermines the efficacy of these therapies by deploying defense mechanisms designed to safeguard the structural integrity of the cell and the integrity of its DNA [39; 43]. The Hsp10-Hsp60 complex is crucial in regulating intracellular pathways related to cellular proliferation and apoptosis, and it is known that the malfunctioning of this complex can result in malignant cell transformation [38; 44; 45]. Furthermore, Hsp60 has been found to exhibit pro-angiogenic and pro-metastatic properties [37; 46]. Hsp27 also seems to be implicated in cellular apoptosis, and its involvement in this process plays a pivotal role in cancer regulation development, progression, and metastasis [47]. Additionally, Hsp27 has been identified as a contributor to the suppression of cellular senescence, enabling tumor cells to acquire an immortal phenotype [48]. Therefore, the dysregulation of Hsp90 can have significant oncogenic implications, as it is involved in numerous processes that drive cell proliferation. It is crucial to recognize that Hsp90 has a fundamental function in tumor transformation. It regulates cell adhesion processes that are critical for the development of metastatic capabilities. Additionally, it promotes neo-angiogenesis, which is the foundation of tumor growth and increases the potential for metastasis [49; 50; 51]. The examined molecules in this study are all involved in metabolic processes that enable atypical cells to deviate from normal physiological processes. The findings of this study, combined with previous research, confirm a connection between heightened levels of heat shock proteins and disorders marked by cellular imbalance and a loss of differentiation. The immunohistochemical analysis of the study detected HSPs in the vocal cord epithelium across all three morphological states (healthy, dysplastic, and squamous carcinoma tissue), with a gradual rise in tissue levels from healthy to dysplastic and cancerous forms. The gradual and consistent increase in HSP levels is most likely a result of changes in both intra- and extracellular conditions. In healthy tissues, HSPs are found at normal levels. However, in dysplasia, there is an increase in HSPs, which suggests changes in the structure of the cell and a greater need for protein expression. Cancerous tissues exhibit even higher levels of HSPs, indicating a complete disruption of cellular homeostasis and altered cellular differentiation. Our analysis also revealed a shift in the distribution of HSPs within cells, which is consistent with previous research showing elevated levels of HSPs in many cancer pathologies. Furthermore, research has demonstrated that HSPs change their localization, moving from mitochondria to the cytoplasm and sometimes even the cellular membrane [34; 35; 52]. Our study revealed that Hsp10 and Hsp27 were localizedin the cytoplasm, whereas Hsp60 and Hsp90 were present in both the cytoplasm and nucleus, with Hsp10 showing nuclear localization.