Protein homeostasis and molecular chaperones in aging

Arslan M. A., Csermely P., Soti C.

BIOGERONTOLOGY, cilt.7, sa.5-6, ss.383-389, 2006 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 7 Sayı: 5-6
  • Basım Tarihi: 2006
  • Doi Numarası: 10.1007/s10522-006-9053-7
  • Dergi Adı: BIOGERONTOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.383-389
  • Ondokuz Mayıs Üniversitesi Adresli: Hayır

Özet

Molecular chaperones are ubiquitous, highly conserved proteins responsible for the maintenance of protein folding homeostasis in cells. Environmental stress causes proteotoxic damage, which triggers chaperone induction and the subsequent reparation of cellular damage by chaperones, including disposing irreparable protein ensembles. We summarize the current view of protein damage, turnover, the stress response and chaperone function in aging, and review novel data showing that accumulation of misfolded proteins outcompete and overload the limited resources of the protein folding, maintenance and turnover system, compromising general protein homeastasis and cellular function. Possible involvement of chaperones and proteolysis in immunosenescence is highlighted. Defects in zinc metabolism are also addressed in relation to aging and changes in chaperone levels.