Show simple item record

dc.contributor.advisorWilliams, John H. H.
dc.contributor.advisorAndrew, Sarah M.
dc.contributor.authorLeoni, Francesca*
dc.date.accessioned2010-03-08T12:07:46Z
dc.date.available2010-03-08T12:07:46Z
dc.date.issued2009-03
dc.identifieruk.bl.ethos.511049
dc.identifier.citationIreland, H.E., Leoni, F., Altaie, O., Birch, C.S., Coleman, R.C., Hunter-Lavin, C., & Williams, J.H.H. (2007). Measuring the secretion of heat shock proteins from cells. Methods, 42, 176-183
dc.identifier.citationDempsey, N.C., Leoni, F., Ireland, H.E., Hoyle, C., & Williams, J.H.H. (2009). Differential heat shock protein localisation in chronic lymphocytic leukaemia. Journal of Leukocyte Biology
dc.identifier.urihttp://hdl.handle.net/10034/93835
dc.description.abstractEvidence suggesting that Hsp72 is actively participating in cellular signalling as well interacting with immune system dynamics has been increasing. This is true in healthy, stressed and diseased cells but to different degrees. Modulation of the plasma membrane association and secretion in the extracellular environment by different types of stressors is the key event that leads to different degrees of immune system activation. Hence a better understanding of the mechanisms of Hsp72 secretion and association with plasma membrane is crucial. This thesis investigated the tissue source and mechanism of Hsp72 surface presentation to plasma membrane structures and release in relation with different cellular and physiological stressors. In vivo models confirmed that different tissue types determine specific Hsp72 responses following the same stress and increase serum Hsp72 dependant on intensity and duration of the stress. Diseases models confirm that Hsp72 responses in specific cell populations is related to disease progression, while in vitro models clearly showed that there are multiple mechanisms of secretion and surface presentation, dependent on the nature of the stressor as well as the intensity and duration. This observations clearly change the view of extracellular Hsp72 as a danger signal and lead to a revision of the original danger model. It also suggests that manipulation of Hsp72 translocation through the different pathways involved may prove effective therapeutically.
dc.language.isoenen
dc.publisherUniversity of Liverpool (Chester College of Higher Education)
dc.subjectheat shock proteinsen
dc.titleHsp72 translocation and secretion in in vivo and in vitro modelsen
dc.typeThesis or dissertationen
dc.type.qualificationnamePhDen
dc.type.qualificationlevelDoctoralen
html.description.abstractEvidence suggesting that Hsp72 is actively participating in cellular signalling as well interacting with immune system dynamics has been increasing. This is true in healthy, stressed and diseased cells but to different degrees. Modulation of the plasma membrane association and secretion in the extracellular environment by different types of stressors is the key event that leads to different degrees of immune system activation. Hence a better understanding of the mechanisms of Hsp72 secretion and association with plasma membrane is crucial. This thesis investigated the tissue source and mechanism of Hsp72 surface presentation to plasma membrane structures and release in relation with different cellular and physiological stressors. In vivo models confirmed that different tissue types determine specific Hsp72 responses following the same stress and increase serum Hsp72 dependant on intensity and duration of the stress. Diseases models confirm that Hsp72 responses in specific cell populations is related to disease progression, while in vitro models clearly showed that there are multiple mechanisms of secretion and surface presentation, dependent on the nature of the stressor as well as the intensity and duration. This observations clearly change the view of extracellular Hsp72 as a danger signal and lead to a revision of the original danger model. It also suggests that manipulation of Hsp72 translocation through the different pathways involved may prove effective therapeutically.
dc.rights.usageThe full-text may be used and/or reproduced in any format or medium, without prior permission or charge, for personal research or study, educational, or not-for-profit purposes provided that: - A full bibliographic reference is made to the original source - A link is made to the metadata record in ChesterRep - The full-text is not changed in any way - The full-text must not be sold in any format or medium without the formal permission of the copyright holders. - For more information please email researchsupport.lis@chester.ac.uk


Files in this item

Thumbnail
Name:
introductory materials.pdf
Size:
137.2Kb
Format:
PDF
Request:
Introductory Materials
Thumbnail
Name:
chapter 1.pdf
Size:
457.9Kb
Format:
PDF
Request:
Introduction
Thumbnail
Name:
chapter 2.pdf
Size:
285.2Kb
Format:
PDF
Request:
Material and Methods
Thumbnail
Name:
chapter 3.pdf
Size:
437.7Kb
Format:
PDF
Request:
Hsp72 Expression and Movement ...
Thumbnail
Name:
chapter 4.pdf
Size:
472.7Kb
Format:
PDF
Request:
Exercise and Regulation of Hsp72 ...
Thumbnail
Name:
chapter 5.pdf
Size:
210.4Kb
Format:
PDF
Request:
Surface and Intracellular Hsp72 ...
Thumbnail
Name:
chapter 6.pdf
Size:
638.8Kb
Format:
PDF
Request:
Surface Hsp72 Expression and ...
Thumbnail
Name:
chapter 7.pdf
Size:
426.7Kb
Format:
PDF
Request:
Manipulation of Hsp72 Expression ...
Thumbnail
Name:
chapter 8.pdf
Size:
562.4Kb
Format:
PDF
Request:
Modulation of Hsp72 Protein ...
Thumbnail
Name:
chapter 9.pdf
Size:
560.9Kb
Format:
PDF
Request:
Discussion
Thumbnail
Name:
references.pdf
Size:
175.2Kb
Format:
PDF
Request:
References

This item appears in the following Collection(s)

Show simple item record