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Review
. 2023 Nov 3;3(6):635-638.
doi: 10.21873/cdp.10265. eCollection 2023 Nov-Dec.

Heat Shock Proteins' Expression Profiles in Odontogenic Ameloblastomas and Cysts

Affiliations
Review

Heat Shock Proteins' Expression Profiles in Odontogenic Ameloblastomas and Cysts

Vasiliki Mathiou et al. Cancer Diagn Progn. .

Abstract

Tumors and cysts with odontogenic origin represent a family of lesions with specific histo-genetic and clinical characteristics. Among them, ameloblastomas are common benign neoplasms, predominantly detected in the anatomic areas of the jaws and also in the mandible and maxilla. Although they are characterized by a slow and stable growing pattern, a subset of them shows a tendency for local tissue invasiveness and partially increased recurrence rates after surgical excision. Furthermore, heat shock proteins (HSPs) are potentially implicated in ameloblastoma onset and progression. HSPs regulate the folding and refolding of proteins and are induced in response to oxidative stress. They are crucial members of the chaperone intracellular system and are categorized based on their molecular weight (i.e., HSP27, HSP60, HSP70, HSP90). In the current review, we describe HSPs origin and function, focusing on their deregulation mechanisms and impact predominantly on ameloblastomas and also on inflammatory and developmental odontogenic cystic lesions.

Keywords: Intracellular; ameloblastoma; cyst; heat shock proteins; odontogenic; review; stress.

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Conflict of interest statement

The Authors have no conflicts of interest to declare in relation to this study.

Figures

Figure 1
Figure 1. Heat shock proteins (HSPs) are mainly over-expressed in ameloblastomas and odontogenic cysts. HSPs regulate the folding and refolding of proteins and are induced in response to oxidative stress. They are crucial members of the chaperone intracellular system and are categorized based on their molecular weight (i.e., HSP27, HSP60, HSP70, HSP90).

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References

    1. Murshid A, Prince TL, Lang B, Calderwood SK. Role of heat shock factors in stress-induced transcription. Methods Mol Biol. 2018;1709:23–34. doi: 10.1007/978-1-4939-7477-1_2. - DOI - PMC - PubMed
    1. Hoter A, El-Sabban ME, Naim HY. The HSP90 family: Structure, regulation, function, and implications in health and disease. Int J Mol Sci. 2018;19(9):2560. doi: 10.3390/ijms19092560. - DOI - PMC - PubMed
    1. Sarangi U, Singh MK, Abhijnya KV, Reddy LP, Prasad BS, Pitke VV, Paithankar K, Sreedhar AS. Hsp60 chaperonin acts as barrier to pharmacologically induced oxidative stress mediated apoptosis in tumor cells with differential stress response. Drug Target Insights. 2013;7:35–51. doi: 10.4137/DTI.S12513. - DOI - PMC - PubMed
    1. Hartl FU, Bracher A, Hayer-hartl M. Molecular chaperones in protein folding and proteostasis. Nature. 2011;475(7356):324–332. doi: 10.1038/nature10317. - DOI - PubMed
    1. Szebesczyk A, Słowik J. Heat shock proteins and metal ions - Reaction or interaction. Comput Struct Biotechnol J. 2023;21:3103–3108. doi: 10.1016/j.csbj.2023.05.024. - DOI - PMC - PubMed

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