PMID- 26983829
OWN - NLM
STAT- MEDLINE
DCOM- 20170206
LR  - 20181113
IS  - 1573-6830 (Electronic)
IS  - 0272-4340 (Linking)
VI  - 36
IP  - 3
DP  - 2016 Apr
TI  - Study of Exosomes Shed New Light on Physiology of Amyloidogenesis.
PG  - 327-42
LID - 10.1007/s10571-016-0357-0 [doi]
AB  - Accumulation of toxic amyloid oligomers, a key feature in the pathogenesis of 
      amyloid-related diseases, results from an imbalance between generation and 
      clearance of amyloidogenic proteins. Cell biology has brought to light the key 
      roles of multivesicular endosomes (MVEs) and their intraluminal vesicles (ILVs), 
      which can be secreted as exosomes, in amyloid generation and clearance. To better 
      understand these roles, we have investigated a relevant physiological model of 
      amyloid formation in pigment cells. These cells have tuned their endosomes to 
      optimize the formation of functional amyloid fibrils from the premelanosome 
      protein (PMEL) and to avoid potential accumulation of toxic species. The 
      functional amyloids derived from PMEL reveal striking analogies with the 
      generation of Abeta peptides. We have recently strengthened these analogies using 
      extracellular vesicles as reporters of the endosomal processes that regulate PMEL 
      melanogenesis. We have shown that in pigmented cells, apolipoprotein E (ApoE) is 
      associated with ILVs and exosomes, and regulates the formation of PMEL amyloid 
      fibrils in endosomes. This process secures the generation of amyloid fibrils by 
      exploiting ILVs as amyloid-nucleating platforms. This physiological model of 
      amyloidogenesis could shed new light on the roles of MVEs and exosomes in 
      conditions with pathological amyloid metabolism, such as Alzheimer's disease.
FAU - van Niel, Guillaume
AU  - van Niel G
AUID- ORCID: 0000-0002-8651-9705
AD  - Institut Curie, PSL Research University, UMR144, Centre de Recherche, 26 rue 
      d'ULM, 75231, Paris, France. guillaume.van-niel@curie.fr.
AD  - Centre National de la Recherche Scientifique, UMR144, 75248, Paris, France. 
      guillaume.van-niel@curie.fr.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20160317
PL  - United States
TA  - Cell Mol Neurobiol
JT  - Cellular and molecular neurobiology
JID - 8200709
RN  - 0 (Amyloid)
RN  - 0 (Amyloid beta-Peptides)
RN  - 0 (Apolipoproteins E)
RN  - 0 (Melanins)
SB  - IM
MH  - Amyloid/*metabolism
MH  - Amyloid beta-Peptides/metabolism
MH  - Animals
MH  - Apolipoproteins E/metabolism
MH  - Endosomes/metabolism
MH  - Exosomes/*metabolism
MH  - Humans
MH  - Melanins/biosynthesis
OTO - NOTNLM
OT  - Alzheimer
OT  - Amyloid
OT  - ApoE
OT  - Abeta
OT  - Endosomes
OT  - Exosomes
OT  - Intraluminal vesicles
OT  - MVB
OT  - PMEL
OT  - Pigmented cells
EDAT- 2016/03/18 06:00
MHDA- 2017/02/07 06:00
CRDT- 2016/03/18 06:00
PHST- 2015/09/25 00:00 [received]
PHST- 2016/02/27 00:00 [accepted]
PHST- 2016/03/18 06:00 [entrez]
PHST- 2016/03/18 06:00 [pubmed]
PHST- 2017/02/07 06:00 [medline]
AID - 10.1007/s10571-016-0357-0 [pii]
AID - 10.1007/s10571-016-0357-0 [doi]
PST - ppublish
SO  - Cell Mol Neurobiol. 2016 Apr;36(3):327-42. doi: 10.1007/s10571-016-0357-0. Epub 
      2016 Mar 17.