PMID- 24485032
OWN - NLM
STAT- MEDLINE
DCOM- 20141118
LR  - 20211021
IS  - 1558-4488 (Electronic)
IS  - 0270-9295 (Print)
IS  - 0270-9295 (Linking)
VI  - 34
IP  - 1
DP  - 2014 Jan
TI  - Chaperone-mediated autophagy in the kidney: the road more traveled.
PG  - 72-83
LID - S0270-9295(13)00226-X [pii]
LID - 10.1016/j.semnephrol.2013.11.010 [doi]
AB  - Chaperone-mediated autophagy (CMA) is a lysosomal proteolytic pathway in which 
      cytosolic substrate proteins contain specific chaperone recognition sequences 
      required for degradation and are translocated directly across the lysosomal 
      membrane for destruction. CMA proteolytic activity has a reciprocal relationship 
      with macroautophagy: CMA is most active in cells in which macroautophagy is least 
      active. Normal renal proximal tubular cells have low levels of macroautophagy, 
      but high basal levels of CMA activity. CMA activity is regulated by starvation, 
      growth factors, oxidative stress, lipids, aging, and retinoic acid signaling. The 
      physiological consequences of changes in CMA activity depend on the substrate 
      proteins present in a given cell type. In the proximal tubule, increased CMA 
      results from protein or calorie starvation and from oxidative stress. 
      Overactivity of CMA can be associated with tubular lysosomal pathology and 
      certain cancers. Reduced CMA activity contributes to protein accumulation in 
      renal tubular hypertrophy, but may contribute to oxidative tissue damage in 
      diabetes and aging. Although there are more questions than answers about the role 
      of high basal CMA activity, this remarkable feature of tubular protein metabolism 
      appears to influence a variety of chronic diseases.
CI  - Published by Elsevier Inc.
FAU - Franch, Harold A
AU  - Franch HA
AD  - Research Service, Atlanta Veterans Affairs Medical Center, Decatur, GA; and Renal 
      Division, Department of Medicine, Emory University School of Medicine, Atlanta, 
      GA. Electronic address: hfranch@emory.edu.
LA  - eng
GR  - R01 DK073476/DK/NIDDK NIH HHS/United States
GR  - R01DK073476/DK/NIDDK NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Review
DEP - 20131122
PL  - United States
TA  - Semin Nephrol
JT  - Seminars in nephrology
JID - 8110298
RN  - 0 (Lysosomal-Associated Membrane Protein 2)
RN  - 0 (Molecular Chaperones)
SB  - IM
MH  - Aging
MH  - Animals
MH  - Autophagy/*physiology
MH  - Diabetes Mellitus/pathology
MH  - Humans
MH  - Kidney/*pathology
MH  - Kidney Tubules/pathology
MH  - Lysosomal-Associated Membrane Protein 2/physiology
MH  - Molecular Chaperones/*physiology
MH  - Neoplasms/pathology
MH  - Oxidative Stress
PMC - PMC4532379
MID - NIHMS543918
OTO - NOTNLM
OT  - Hypertrophy
OT  - cancer
OT  - diabetes
OT  - starvation
COIS- Conflict of interest statement: none.
EDAT- 2014/02/04 06:00
MHDA- 2014/11/19 06:00
PMCR- 2015/08/11
CRDT- 2014/02/04 06:00
PHST- 2014/02/04 06:00 [entrez]
PHST- 2014/02/04 06:00 [pubmed]
PHST- 2014/11/19 06:00 [medline]
PHST- 2015/08/11 00:00 [pmc-release]
AID - S0270-9295(13)00226-X [pii]
AID - 10.1016/j.semnephrol.2013.11.010 [doi]
PST - ppublish
SO  - Semin Nephrol. 2014 Jan;34(1):72-83. doi: 10.1016/j.semnephrol.2013.11.010. Epub 
      2013 Nov 22.