title: ER and aging-Protein folding and the ER stress response.
abstract: The endoplasmic reticulum (ER) is a multifunctional organelle which co-ordinates protein folding, lipid biosynthesis, calcium storage and release. Perturbations that disrupt ER homeostasis lead to the misfolding of proteins, ER stress and up-regulation of a signaling pathway called the ER stress response or the unfolded protein response (UPR). The UPR is characterized by the induction of chaperones, degradation of misfolded proteins and attenuation of protein translation. Age-related declines and activity in key molecular chaperones and folding enzymes compromise proper protein folding and the adaptive response of the UPR. This review will highlight age-related changes in the protein folding machinery and in the UPR.
authors.affiliation: Center for Sleep and Respiratory Neurobiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, United States. naidoo@mail.med.upenn.edu
authors.forename: Nirinjini
authors.initials: N
authors.lastname: Naidoo
mesh_terms: D000375:Aging / Q000378:metabolism* / Q000473:pathology; D000818:Animals; D016922:Cellular Senescence / Q000502:physiology*; D004721:Endoplasmic Reticulum / Q000378:metabolism* / Q000473:pathology; D006706:Homeostasis / Q000502:physiology; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology; D013312:Stress, Physiological / Q000502:physiology*
chemical_list: D018832:Molecular Chaperones; D011506:Proteins