PMID- 30610733
OWN - NLM
STAT- MEDLINE
DCOM- 20190606
LR  - 20200621
IS  - 1940-6029 (Electronic)
IS  - 1064-3745 (Print)
IS  - 1064-3745 (Linking)
VI  - 1880
DP  - 2019
TI  - Analysis of Chaperone-Mediated Autophagy.
PG  - 703-727
LID - 10.1007/978-1-4939-8873-0_47 [doi]
AB  - Chaperone-mediated autophagy (CMA) is a selective type of autophagy whereby a 
      specific subset of intracellular proteins is targeted to the lysosome for 
      degradation. These proteins are identified by a chaperone that targets them to 
      lysosomes. There, they are translocated into the organelle lumen through a 
      lysosomal membrane receptor/translocation complex. CMA plays an important role in 
      maintaining cellular proteostasis by eliminating damaged and altered proteins. 
      CMA also participates in the control of the cellular energetic balance through 
      recycling of amino acids resulting from lysosomal proteolysis of the substrate 
      proteins. Lastly, due to the intrinsic protein selectivity of CMA, this type of 
      autophagy exerts regulatory functions by mediating timely degradation of key 
      cellular proteins that participate in processes such as lipid and glucose 
      metabolism, cell cycle, DNA repair, and cellular reprogramming, among others. 
      Dysfunctional CMA occurs with age and has now been described in a growing list of 
      human pathologies such as metabolic disorders, neurodegeneration, cancer, 
      immunodeficiency, and diabetes. In this chapter, we describe current 
      methodologies to quantitatively analyze CMA activity in different experimental 
      models.
FAU - Juste, Y R
AU  - Juste YR
AD  - Department of Developmental and Molecular Biology, Bronx, NY, USA.
AD  - Institute for Aging Studies, Albert Einstein College of Medicine, Bronx, NY, USA.
FAU - Cuervo, A M
AU  - Cuervo AM
AD  - Department of Developmental and Molecular Biology, Bronx, NY, USA. 
      ana-maria.cuervo@einstein.yu.edu.
AD  - Institute for Aging Studies, Albert Einstein College of Medicine, Bronx, NY, USA. 
      ana-maria.cuervo@einstein.yu.edu.
LA  - eng
GR  - U54 NS100717/NS/NINDS NIH HHS/United States
GR  - R37 AG021904/AG/NIA NIH HHS/United States
GR  - RF1 AG054108/AG/NIA NIH HHS/United States
GR  - P01 AG031782/AG/NIA NIH HHS/United States
GR  - R01 DK098408/DK/NIDDK NIH HHS/United States
GR  - P01 AG017617/AG/NIA NIH HHS/United States
PT  - Journal Article
PL  - United States
TA  - Methods Mol Biol
JT  - Methods in molecular biology (Clifton, N.J.)
JID - 9214969
RN  - 0 (Leupeptins)
RN  - 0 (Molecular Chaperones)
RN  - 01Q9PC255D (Ammonium Chloride)
RN  - J97339NR3V (leupeptin)
SB  - IM
MH  - Ammonium Chloride/pharmacology
MH  - Animals
MH  - Autophagy/drug effects/*physiology
MH  - Biological Assay/instrumentation/*methods
MH  - Female
MH  - Leupeptins/pharmacology
MH  - Liver/cytology/metabolism
MH  - Lysosomes/drug effects/*metabolism
MH  - Male
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Molecular Chaperones/*metabolism
MH  - Proteolysis/drug effects
MH  - Rats
MH  - Rats, Wistar
PMC - PMC7017676
MID - NIHMS1069327
OTO - NOTNLM
OT  - Chaperones
OT  - Lysosomes
OT  - Proteolysis
OT  - Subcellular fractionation
EDAT- 2019/01/06 06:00
MHDA- 2019/06/07 06:00
PMCR- 2020/02/13
CRDT- 2019/01/06 06:00
PHST- 2019/01/06 06:00 [entrez]
PHST- 2019/01/06 06:00 [pubmed]
PHST- 2019/06/07 06:00 [medline]
PHST- 2020/02/13 00:00 [pmc-release]
AID - 10.1007/978-1-4939-8873-0_47 [doi]
PST - ppublish
SO  - Methods Mol Biol. 2019;1880:703-727. doi: 10.1007/978-1-4939-8873-0_47.