Aging and molecular chaperones

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

Chaperone function plays a key role in sequestering damaged proteins and in repairing proteotoxic damage. Chaperones are induced by environmental stress and are called as stress or heat shock proteins. Here, we summarize the current knowledge about protein damage in aged organisms, about changes in proteolytic degradation, chaperone expression and function in the aging process, as well as the involvement of chaperones in longevity and cellular senescence. The role of chaperones in aging diseases, such as in Alzheimer's disease, Parkinson's disease, Huntington's disease and in other neurodegenerative diseases as well as in atherosclerosis and in cancer is discussed. We also describe how the balance between chaperone requirement and availability becomes disturbed in aged organisms, or in other words, how chaperone overload develops. The consequences of chaperone overload are also outlined together with several new research strategies to assess the functional status of chaperones in the aging process.

Original languageEnglish
Pages (from-to)1037-1040
Number of pages4
JournalExperimental Gerontology
Volume38
Issue number10
DOIs
Publication statusPublished - Oct 2003

Fingerprint

Molecular Chaperones
Aging of materials
Cell Aging
Huntington Disease
Heat-Shock Proteins
Neurodegenerative Diseases
Parkinson Disease
Atherosclerosis
Alzheimer Disease
Proteins
Neurodegenerative diseases
Research
Neoplasms
Availability
Degradation

Keywords

  • Chaperone overload
  • Heat shock proteins
  • Hsp70
  • Hsp90
  • Molecular chaperones
  • Protein aggregation
  • Protein denaturation
  • Stress proteins

ASJC Scopus subject areas

  • Ageing
  • Medicine(all)

Cite this

Aging and molecular chaperones. / Söti, C.; Csermely, P.

In: Experimental Gerontology, Vol. 38, No. 10, 10.2003, p. 1037-1040.

Research output: Contribution to journalArticle

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