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dc.contributor.authorBrenu, EW
dc.contributor.authorStaines, DR
dc.contributor.authorTajouri, L
dc.contributor.authorHuth, T
dc.contributor.authorAshton, KJ
dc.contributor.authorMarshall-Gradisnik, SM
dc.date.accessioned2017-05-03T16:11:03Z
dc.date.available2017-05-03T16:11:03Z
dc.date.issued2013
dc.date.modified2014-01-13T00:37:17Z
dc.identifier.issn2090-0422
dc.identifier.doi10.1155/2013/813256
dc.identifier.urihttp://hdl.handle.net/10072/55566
dc.description.abstractHeat shock proteins (HSPs) are important molecules required for ideal protein function. Extensive research on the functional properties of HSPs indicates that HSPs may be implicated in a wide range of physiological functions including immune function. In the immune system, HSPs are involved in cell proliferation, differentiation, cytokine release, and apoptosis.Therefore, the ability of the immune system, in particular immune cells, to function optimally and in unison with other physiological systems is in part dependent on signaling transduction processes, including bidirectional communication with HSPs. Regulatory T cells (Tregs) are important T cells with suppressive functions and impairments in their function have been associated with a number of autoimmune disorders. The purpose of this paper is to examine the relationship between HSPs and Tregs. The interrelationship between cells and proteins may be important in cellular functions necessary for cell survival and expansion during diseased state. 1. Introduction Optimal cellular function is regulated by several molecules including heat shock proteins (HSPs). These proteins have chaperone properties and are important in both stressed and unstressed cells. HSPs can be categorized into six diverse highly or less-conserved families. These include HSP10, HSP40, HSP60, HSP70, HSP90, and HSP100 [1-4]. HSP60 is found in themitochondria [5]. HSP70 is implicated in protein transport assembly and synthesis. It has anti-apoptotic properties that are implicated in intrinsic and extrinsic apoptotic pathways. HSP70
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent542498 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherHindawi Publishing Corporation
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrom813256-1
dc.relation.ispartofpageto813256-8
dc.relation.ispartofjournalAutoimmune Diseases
dc.relation.ispartofvolume2013
dc.rights.retentionY
dc.subject.fieldofresearchAutoimmunity
dc.subject.fieldofresearchcode320403
dc.titleHeat Shock Proteins and Regulatory T Cells
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://creativecommons.org/licenses/by-nc-sa/2.1/au/
gro.facultyGriffith Health, School of Medical Science
gro.rights.copyright© The Author(s) 2013. The attached file is posted here with permission of the copyright owner[s] for your personal use only. No further distribution permitted.For information about this journal please refer to the journal’s website. The online version of this work is licensed under a Creative Commons License, available at http://creativecommons.org/licenses/by-nc-sa/2.1/au/
gro.date.issued2013
gro.hasfulltextFull Text
gro.griffith.authorStaines, Donald R.
gro.griffith.authorMarshall-Gradisnik, Sonya M.


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