PMID- 12000969
OWN - NLM
STAT- MEDLINE
DCOM- 20020523
LR  - 20161124
IS  - 0028-0836 (Print)
IS  - 0028-0836 (Linking)
VI  - 417
IP  - 6885
DP  - 2002 May 9
TI  - Transient aggregation of ubiquitinated proteins during dendritic cell maturation.
PG  - 177-82
AB  - Dendritic cells (DCs) are antigen-presenting cells with the unique capacity to 
      initiate primary immune responses. Dendritic cells have a remarkable pattern of 
      differentiation (maturation) that exhibits highly specific mechanisms to control 
      antigen presentation restricted by major histocompatibility complex (MHC). MHC 
      class I molecules present to CD8(+) cytotoxic T cells peptides that are derived 
      mostly from cytosolic proteins, which are ubiquitinated and then degraded by the 
      proteasome. Here we show that on inflammatory stimulation, DCs accumulate newly 
      synthesized ubiquitinated proteins in large cytosolic structures. These 
      structures are similar to, but distinct from, aggresomes and inclusion bodies 
      observed in many amyloid diseases. Notably, these dendritic cell aggresome-like 
      induced structures (DALIS) are transient, require continuous protein synthesis 
      and do not affect the ubiquitin-proteasome pathway. Our observations suggest the 
      existence of an organized prioritization of protein degradation in stimulated 
      DCs, which is probably important for regulating MHC class I presentation during 
      maturation.
FAU - Lelouard, Hugues
AU  - Lelouard H
AD  - Centre d'Immunolgie de Marseille-Luminy, CNRS-INSERM-Universite Med., Marseille, 
      France.
FAU - Gatti, Evelina
AU  - Gatti E
FAU - Cappello, Fanny
AU  - Cappello F
FAU - Gresser, Olivia
AU  - Gresser O
FAU - Camosseto, Voahirana
AU  - Camosseto V
FAU - Pierre, Philippe
AU  - Pierre P
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Nature
JT  - Nature
JID - 0410462
RN  - 0 (Histocompatibility Antigens Class I)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Oligopeptides)
RN  - 0 (Protein Subunits)
RN  - 0 (Ubiquitin)
RN  - 3HZV514J4B (Canavanine)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
RN  - EC 3.4.25.1 (Proteasome Endopeptidase Complex)
RN  - SH1WY3R615 (Nocodazole)
RN  - Y0900I3U8U (epoxomicin)
SB  - IM
MH  - Animals
MH  - Antigen Presentation
MH  - Canavanine/pharmacology
MH  - Catalytic Domain
MH  - *Cell Differentiation/drug effects
MH  - Cysteine Endopeptidases/chemistry/metabolism
MH  - Cytoplasm/metabolism
MH  - Dendritic Cells/*cytology/drug effects/immunology/*metabolism
MH  - Histocompatibility Antigens Class I/biosynthesis/immunology/*metabolism
MH  - Lipopolysaccharides/pharmacology
MH  - Male
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - Multienzyme Complexes/chemistry/metabolism
MH  - Nocodazole/pharmacology
MH  - Oligopeptides/pharmacology
MH  - Proteasome Endopeptidase Complex
MH  - Protein Binding/drug effects
MH  - Protein Biosynthesis
MH  - Protein Denaturation
MH  - Protein Subunits
MH  - Protein Transport/drug effects
MH  - Ubiquitin/*metabolism
EDAT- 2002/05/10 10:00
MHDA- 2002/05/25 10:01
CRDT- 2002/05/10 10:00
PHST- 2002/05/10 10:00 [pubmed]
PHST- 2002/05/25 10:01 [medline]
PHST- 2002/05/10 10:00 [entrez]
AID - 417177a [pii]
AID - 10.1038/417177a [doi]
PST - ppublish
SO  - Nature. 2002 May 9;417(6885):177-82. doi: 10.1038/417177a.