Heat shock protein paradigms in cancer progression: future therapeutic perspectives

Heat-shock proteins (HSPs), also known as stress proteins, are ubiquitously present in all forms of life. They play pivotal roles in protein folding and unfolding, the formation of multiprotein complexes, the transportation and sorting of proteins into their designated subcellular compartments, the...

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Published in:3 Biotech 2024-04, Vol.14 (4), p.96-96, Article 96
Main Authors: Tausif, Y. Mohammed, Thekkekkara, Dithu, Sai, Thummuru Ekshita, Jahagirdar, Vaishnavi, Arjun, H. R., Meheronnisha, S. K., Babu, Amrita, Banerjee, Aniruddha
Format: Article
Language:English
Subjects:
Agriculture
Angiogenesis
Bioinformatics
Biomaterials
Biotechnology
Cancer
Cancer Research
Cell cycle
Cell differentiation
Cell division
Cell migration
Cell proliferation
Cellular stress response
Cellular structure
Chemistry
Chemistry and Materials Science
Folding
Heat shock proteins
Hsp27 protein
Hsp40 protein
Hsp60 protein
Hsp70 protein
Hsp90 protein
Metastases
Pharmacology
Protein folding
Review Article
Signal transduction
Stem Cells
Stress proteins
Structure-function relationships
Therapeutic applications
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Summary:Heat-shock proteins (HSPs), also known as stress proteins, are ubiquitously present in all forms of life. They play pivotal roles in protein folding and unfolding, the formation of multiprotein complexes, the transportation and sorting of proteins into their designated subcellular compartments, the regulation of the cell cycle, and signalling processes. These HSPs encompass HSP27, HSP40, HSP70, HSP60, and HSP90, each contributing to various cellular functions. In the context of cancer, HSPs exert influence by either inhibiting or activating diverse signalling pathways, thereby impacting growth, differentiation, and cell division. This article offers an extensive exploration of the functions of HSPs within the realms of pharmacology and cancer biology. HSPs are believed to play substantial roles in the mechanisms underlying the initiation and progression of cancer. They hold promise as valuable clinical markers for cancer diagnosis, potential targets for therapeutic interventions, and indicators of disease progression. In times of cellular stress, HSPs function as molecular chaperones, safeguarding the structural and functional integrity of proteins and aiding in their proper folding. Moreover, HSPs play a crucial role in cancer growth, by regulating processes such as angiogenesis, cell proliferation, migration, invasion, and metastasis.
ISSN:2190-572X
2190-5738
DOI:10.1007/s13205-024-03951-6