PMID- 34629183
OWN - NLM
STAT- MEDLINE
DCOM- 20211229
LR  - 20221202
IS  - 1872-9452 (Electronic)
IS  - 0098-2997 (Print)
IS  - 0098-2997 (Linking)
VI  - 82
DP  - 2021 Dec
TI  - Chaperone-mediated autophagy and disease: Implications for cancer and 
      neurodegeneration.
PG  - 101025
LID - S0098-2997(21)00085-6 [pii]
LID - 10.1016/j.mam.2021.101025 [doi]
AB  - Chaperone-mediated autophagy (CMA) is a proteolytic process whereby selected 
      intracellular proteins are degraded inside lysosomes. Owing to its selectivity, 
      CMA participates in the modulation of specific regulatory proteins, thereby 
      playing an important role in multiple cellular processes. Studies conducted over 
      the last two decades have enabled the molecular characterization of this 
      autophagic pathway and the design of specific experimental models, and have 
      underscored the importance of CMA in a range of physiological processes beyond 
      mere protein quality control. Those findings also indicate that decreases in CMA 
      function with increasing age may contribute to the pathogenesis of age-associated 
      diseases, including neurodegeneration and cancer. In the context of neurological 
      diseases, CMA impairment is thought to contribute to the accumulation of 
      misfolded/aggregated proteins, a process central to the pathogenesis of 
      neurodegenerative diseases. CMA therefore constitutes a potential therapeutic 
      target, as its induction accelerates the clearance of pathogenic proteins, 
      promoting cell survival. More recent evidence has highlighted the important and 
      complex role of CMA in cancer biology. While CMA induction may limit tumor 
      development, experimental evidence also indicates that inhibition of this pathway 
      can attenuate the growth of established tumors and improve the response to cancer 
      therapeutics. Here, we describe and discuss the evidence supporting a role of 
      impaired CMA function in neurodegeneration and cancer, as well as future research 
      directions to evaluate the potential of this pathway as a target for the 
      prevention and treatment of these diseases.
CI  - Copyright (c) 2021 Elsevier Ltd. All rights reserved.
FAU - Gomez-Sintes, Raquel
AU  - Gomez-Sintes R
AD  - Department of Cellular and Molecular Biology, Centro de Investigaciones 
      Biologicas Margarita Salas CIB-CSIC, 28040, Madrid, Spain; Department of 
      Developmental and Molecular Biology & Institute for Aging Studies, Albert 
      Einstein College of Medicine, Bronx, NY, 10461, USA. Electronic address: 
      rgomez@cib.csic.es.
FAU - Arias, Esperanza
AU  - Arias E
AD  - Department of Medicine, Marion Bessin Liver Research Center & Institute for Aging 
      Studies, Albert Einstein College of Medicine, Bronx, NY, 10461, USA. Electronic 
      address: esperanza.arias-perez@einsteinmed.org.
LA  - eng
GR  - P30 AG038072/AG/NIA NIH HHS/United States
GR  - P30 DK041296/DK/NIDDK NIH HHS/United States
GR  - R01 DK124308/DK/NIDDK NIH HHS/United States
PT  - Journal Article
DEP - 20211007
PL  - England
TA  - Mol Aspects Med
JT  - Molecular aspects of medicine
JID - 7603128
RN  - 0 (Molecular Chaperones)
SB  - IM
MH  - Autophagy
MH  - *Chaperone-Mediated Autophagy
MH  - Humans
MH  - Lysosomes
MH  - Molecular Chaperones/genetics
MH  - *Neoplasms/genetics
MH  - *Neurodegenerative Diseases/genetics
PMC - PMC8711233
MID - NIHMS1760922
OTO - NOTNLM
OT  - Aggregation
OT  - Autophagy
OT  - Chaperones
OT  - Lysosomes
OT  - Protein degradation
OT  - Tumorigenesis
EDAT- 2021/10/12 06:00
MHDA- 2021/12/30 06:00
PMCR- 2022/12/01
CRDT- 2021/10/11 05:35
PHST- 2021/07/26 00:00 [received]
PHST- 2021/09/10 00:00 [revised]
PHST- 2021/09/12 00:00 [accepted]
PHST- 2021/10/12 06:00 [pubmed]
PHST- 2021/12/30 06:00 [medline]
PHST- 2021/10/11 05:35 [entrez]
PHST- 2022/12/01 00:00 [pmc-release]
AID - S0098-2997(21)00085-6 [pii]
AID - 10.1016/j.mam.2021.101025 [doi]
PST - ppublish
SO  - Mol Aspects Med. 2021 Dec;82:101025. doi: 10.1016/j.mam.2021.101025. Epub 2021 
      Oct 7.