Loading…

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...

Full description

Saved in:
Bibliographic Details
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:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c375t-70dba166875131b44e4cdaccdd23527fdafd537cc229629543da35175cc05c653
cites cdi_FETCH-LOGICAL-c375t-70dba166875131b44e4cdaccdd23527fdafd537cc229629543da35175cc05c653
container_end_page 96
container_issue 4
container_start_page 96
container_title 3 Biotech
container_volume 14
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
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2942189771</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2937357706</sourcerecordid><originalsourceid>FETCH-LOGICAL-c375t-70dba166875131b44e4cdaccdd23527fdafd537cc229629543da35175cc05c653</originalsourceid><addsrcrecordid>eNp9kM9LwzAUx4Mobsz9Ax6k4MVLNT-apvEmQ50w8KCCt5Alr1vn1tYkFfzvzeyc4MFckvA-7_seH4ROCb4kGIsrTxjFPMU0SzGTnKT5ARpSInHKBSsO92_6OkBj71c4Hk64JPgYDViRZVJgOURPU9Ah8cvGvCWtawJUddJqp2212PgkfoyuDbhtbeHA-6qpr5OyC52DJCzB6Ra6UJmkBedbMKH6AH-Cjkq99jDe3SP0cnf7PJmms8f7h8nNLDVM8JAKbOea5HkhOGFknmWQGauNsZYyTkVpdWk5E8ZQKnMqecasZpwIbgzmJudshC763Ljcewc-qE3lDazXuoam84rKjJJCCkEiev4HXTWdq-N2kWKCcSFwHinaU8Y13jsoVeuqjXafimC1ta566ypaV9_W1bbpbBfdzTdg9y0_jiPAesDHUr0A9zv7n9gvlFCM-g</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2937357706</pqid></control><display><type>article</type><title>Heat shock protein paradigms in cancer progression: future therapeutic perspectives</title><source>Springer Link</source><creator>Tausif, Y. Mohammed ; Thekkekkara, Dithu ; Sai, Thummuru Ekshita ; Jahagirdar, Vaishnavi ; Arjun, H. R. ; Meheronnisha, S. K. ; Babu, Amrita ; Banerjee, Aniruddha</creator><creatorcontrib>Tausif, Y. Mohammed ; Thekkekkara, Dithu ; Sai, Thummuru Ekshita ; Jahagirdar, Vaishnavi ; Arjun, H. R. ; Meheronnisha, S. K. ; Babu, Amrita ; Banerjee, Aniruddha</creatorcontrib><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.</description><identifier>ISSN: 2190-572X</identifier><identifier>EISSN: 2190-5738</identifier><identifier>DOI: 10.1007/s13205-024-03951-6</identifier><identifier>PMID: 38449709</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>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</subject><ispartof>3 Biotech, 2024-04, Vol.14 (4), p.96-96, Article 96</ispartof><rights>King Abdulaziz City for Science and Technology 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-70dba166875131b44e4cdaccdd23527fdafd537cc229629543da35175cc05c653</citedby><cites>FETCH-LOGICAL-c375t-70dba166875131b44e4cdaccdd23527fdafd537cc229629543da35175cc05c653</cites><orcidid>0000-0003-1313-7500</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38449709$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tausif, Y. 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><title>Heat shock protein paradigms in cancer progression: future therapeutic perspectives</title><title>3 Biotech</title><addtitle>3 Biotech</addtitle><addtitle>3 Biotech</addtitle><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.</description><subject>Agriculture</subject><subject>Angiogenesis</subject><subject>Bioinformatics</subject><subject>Biomaterials</subject><subject>Biotechnology</subject><subject>Cancer</subject><subject>Cancer Research</subject><subject>Cell cycle</subject><subject>Cell differentiation</subject><subject>Cell division</subject><subject>Cell migration</subject><subject>Cell proliferation</subject><subject>Cellular stress response</subject><subject>Cellular structure</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Folding</subject><subject>Heat shock proteins</subject><subject>Hsp27 protein</subject><subject>Hsp40 protein</subject><subject>Hsp60 protein</subject><subject>Hsp70 protein</subject><subject>Hsp90 protein</subject><subject>Metastases</subject><subject>Pharmacology</subject><subject>Protein folding</subject><subject>Review Article</subject><subject>Signal transduction</subject><subject>Stem Cells</subject><subject>Stress proteins</subject><subject>Structure-function relationships</subject><subject>Therapeutic applications</subject><issn>2190-572X</issn><issn>2190-5738</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><recordid>eNp9kM9LwzAUx4Mobsz9Ax6k4MVLNT-apvEmQ50w8KCCt5Alr1vn1tYkFfzvzeyc4MFckvA-7_seH4ROCb4kGIsrTxjFPMU0SzGTnKT5ARpSInHKBSsO92_6OkBj71c4Hk64JPgYDViRZVJgOURPU9Ah8cvGvCWtawJUddJqp2212PgkfoyuDbhtbeHA-6qpr5OyC52DJCzB6Ra6UJmkBedbMKH6AH-Cjkq99jDe3SP0cnf7PJmms8f7h8nNLDVM8JAKbOea5HkhOGFknmWQGauNsZYyTkVpdWk5E8ZQKnMqecasZpwIbgzmJudshC763Ljcewc-qE3lDazXuoam84rKjJJCCkEiev4HXTWdq-N2kWKCcSFwHinaU8Y13jsoVeuqjXafimC1ta566ypaV9_W1bbpbBfdzTdg9y0_jiPAesDHUr0A9zv7n9gvlFCM-g</recordid><startdate>20240401</startdate><enddate>20240401</enddate><creator>Tausif, Y. Mohammed</creator><creator>Thekkekkara, Dithu</creator><creator>Sai, Thummuru Ekshita</creator><creator>Jahagirdar, Vaishnavi</creator><creator>Arjun, H. R.</creator><creator>Meheronnisha, S. K.</creator><creator>Babu, Amrita</creator><creator>Banerjee, Aniruddha</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-1313-7500</orcidid></search><sort><creationdate>20240401</creationdate><title>Heat shock protein paradigms in cancer progression: future therapeutic perspectives</title><author>Tausif, Y. Mohammed ; Thekkekkara, Dithu ; Sai, Thummuru Ekshita ; Jahagirdar, Vaishnavi ; Arjun, H. R. ; Meheronnisha, S. K. ; Babu, Amrita ; Banerjee, Aniruddha</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c375t-70dba166875131b44e4cdaccdd23527fdafd537cc229629543da35175cc05c653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Agriculture</topic><topic>Angiogenesis</topic><topic>Bioinformatics</topic><topic>Biomaterials</topic><topic>Biotechnology</topic><topic>Cancer</topic><topic>Cancer Research</topic><topic>Cell cycle</topic><topic>Cell differentiation</topic><topic>Cell division</topic><topic>Cell migration</topic><topic>Cell proliferation</topic><topic>Cellular stress response</topic><topic>Cellular structure</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Folding</topic><topic>Heat shock proteins</topic><topic>Hsp27 protein</topic><topic>Hsp40 protein</topic><topic>Hsp60 protein</topic><topic>Hsp70 protein</topic><topic>Hsp90 protein</topic><topic>Metastases</topic><topic>Pharmacology</topic><topic>Protein folding</topic><topic>Review Article</topic><topic>Signal transduction</topic><topic>Stem Cells</topic><topic>Stress proteins</topic><topic>Structure-function relationships</topic><topic>Therapeutic applications</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tausif, Y. 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. K.</au><au>Babu, Amrita</au><au>Banerjee, Aniruddha</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heat shock protein paradigms in cancer progression: future therapeutic perspectives</atitle><jtitle>3 Biotech</jtitle><stitle>3 Biotech</stitle><addtitle>3 Biotech</addtitle><date>2024-04-01</date><risdate>2024</risdate><volume>14</volume><issue>4</issue><spage>96</spage><epage>96</epage><pages>96-96</pages><artnum>96</artnum><issn>2190-572X</issn><eissn>2190-5738</eissn><abstract>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.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>38449709</pmid><doi>10.1007/s13205-024-03951-6</doi><tpages>1</tpages><orcidid>https://orcid.org/0000-0003-1313-7500</orcidid></addata></record>
fulltext fulltext
identifier ISSN: 2190-572X
ispartof 3 Biotech, 2024-04, Vol.14 (4), p.96-96, Article 96
issn 2190-572X
2190-5738
language eng
recordid cdi_proquest_miscellaneous_2942189771
source Springer Link
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
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-05T10%3A50%3A56IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Heat%20shock%20protein%20paradigms%20in%20cancer%20progression:%20future%20therapeutic%20perspectives&rft.jtitle=3%20Biotech&rft.au=Tausif,%20Y.%20Mohammed&rft.date=2024-04-01&rft.volume=14&rft.issue=4&rft.spage=96&rft.epage=96&rft.pages=96-96&rft.artnum=96&rft.issn=2190-572X&rft.eissn=2190-5738&rft_id=info:doi/10.1007/s13205-024-03951-6&rft_dat=%3Cproquest_cross%3E2937357706%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c375t-70dba166875131b44e4cdaccdd23527fdafd537cc229629543da35175cc05c653%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2937357706&rft_id=info:pmid/38449709&rfr_iscdi=true