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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 |
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creator | Tausif, Y. Mohammed Thekkekkara, Dithu Sai, Thummuru Ekshita Jahagirdar, Vaishnavi Arjun, H. R. Meheronnisha, S. K. Babu, Amrita Banerjee, Aniruddha |
description | 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. |
doi_str_mv | 10.1007/s13205-024-03951-6 |
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Mohammed</creatorcontrib><creatorcontrib>Thekkekkara, Dithu</creatorcontrib><creatorcontrib>Sai, Thummuru Ekshita</creatorcontrib><creatorcontrib>Jahagirdar, Vaishnavi</creatorcontrib><creatorcontrib>Arjun, H. R.</creatorcontrib><creatorcontrib>Meheronnisha, S. K.</creatorcontrib><creatorcontrib>Babu, Amrita</creatorcontrib><creatorcontrib>Banerjee, Aniruddha</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>3 Biotech</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tausif, Y. Mohammed</au><au>Thekkekkara, Dithu</au><au>Sai, Thummuru Ekshita</au><au>Jahagirdar, Vaishnavi</au><au>Arjun, H. R.</au><au>Meheronnisha, S. 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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 |
title | Heat shock protein paradigms in cancer progression: future therapeutic perspectives |
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