Proctor2005 - Actions of chaperones and their role in ageing

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Proctor2005 - Actions of chaperones and their role in ageing

This model is described in the article:

Proctor CJ, Soti C, Boys RJ, Gillespie CS, Shanley DP, Wilkinson DJ, Kirkwood TB.
Mech. Ageing Dev. 2005 Jan; 126(1): 119-131

Abstract:

Many molecular chaperones are also known as heat shock proteins because they are synthesised in increased amounts after brief exposure of cells to elevated temperatures. They have many cellular functions and are involved in the folding of nascent proteins, the re-folding of denatured proteins, the prevention of protein aggregation, and assisting the targeting of proteins for degradation by the proteasome and lysosomes. They also have a role in apoptosis and are involved in modulating signals for immune and inflammatory responses. Stress-induced transcription of heat shock proteins requires the activation of heat shock factor (HSF). Under normal conditions, HSF is bound to heat shock proteins resulting in feedback repression. During stress, cellular proteins undergo denaturation and sequester heat shock proteins bound to HSF, which is then able to become transcriptionally active. The induction of heat shock proteins is impaired with age and there is also a decline in chaperone function. Aberrant/damaged proteins accumulate with age and are implicated in several important age-related conditions (e.g. Alzheimer's disease, Parkinson's disease, and cataract). Therefore, the balance between damaged proteins and available free chaperones may be greatly disturbed during ageing. We have developed a mathematical model to describe the heat shock system. The aim of the model is two-fold: to explore the heat shock system and its implications in ageing; and to demonstrate how to build a model of a biological system using our simulation system (biology of ageing e-science integration and simulation (BASIS)).

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Format
SBML (L2V1)
Related Publication
  • Modelling the actions of chaperones and their role in ageing.
  • Proctor CJ, Soti C, Boys RJ, Gillespie CS, Shanley DP, Wilkinson DJ, Kirkwood TB
  • Mechanisms of ageing and development , 1/ 2005 , Volume 126 , pages: 119-131
  • Henry Wellcome Laboratory for Biogerontology Research, School of Clinical and Medical Sciences-Gerontology, University of Newcastle, Newcastle upon Tyne NE4 6BE, UK. c.j.proctor@ncl.ac.uk
  • Many molecular chaperones are also known as heat shock proteins because they are synthesised in increased amounts after brief exposure of cells to elevated temperatures. They have many cellular functions and are involved in the folding of nascent proteins, the re-folding of denatured proteins, the prevention of protein aggregation, and assisting the targeting of proteins for degradation by the proteasome and lysosomes. They also have a role in apoptosis and are involved in modulating signals for immune and inflammatory responses. Stress-induced transcription of heat shock proteins requires the activation of heat shock factor (HSF). Under normal conditions, HSF is bound to heat shock proteins resulting in feedback repression. During stress, cellular proteins undergo denaturation and sequester heat shock proteins bound to HSF, which is then able to become transcriptionally active. The induction of heat shock proteins is impaired with age and there is also a decline in chaperone function. Aberrant/damaged proteins accumulate with age and are implicated in several important age-related conditions (e.g. Alzheimer's disease, Parkinson's disease, and cataract). Therefore, the balance between damaged proteins and available free chaperones may be greatly disturbed during ageing. We have developed a mathematical model to describe the heat shock system. The aim of the model is two-fold: to explore the heat shock system and its implications in ageing; and to demonstrate how to build a model of a biological system using our simulation system (biology of ageing e-science integration and simulation (BASIS)).
Contributors
Carole Proctor

Metadata information

is
BioModels Database MODEL2223638385
BioModels Database BIOMD0000000091
isDescribedBy
PubMed 15610770
hasTaxon
Taxonomy Homo sapiens
isVersionOf
hasVersion
Human Disease Ontology Parkinson's disease
Human Disease Ontology Alzheimer's disease
Human Disease Ontology cataract
Curation status
Curated
  • Model originally submitted by : Carole Proctor
  • Submitted: 08-Mar-2007 19:29:11
  • Last Modified: 03-Jun-2014 21:38:41
Revisions
  • Version: 2 public model Download this version
    • Submitted on: 03-Jun-2014 21:38:41
    • Submitted by: Carole Proctor
    • With comment: Current version of Proctor2005 - Actions of chaperones and their role in ageing
  • Version: 1 public model Download this version
    • Submitted on: 08-Mar-2007 19:29:11
    • Submitted by: Carole Proctor
    • With comment: Original import of Hsp90model_basis510
Curator's comment:
(added: 28 Feb 2007, 15:55:51, updated: 28 Feb 2007, 15:55:51)
Figure2A has been reproduced by Gillespie2.