PMID- 20393136
OWN - NLM
STAT- MEDLINE
DCOM- 20100719
LR  - 20181201
IS  - 1550-6606 (Electronic)
IS  - 0022-1767 (Linking)
VI  - 184
IP  - 10
DP  - 2010 May 15
TI  - TLR2 utilization of Borrelia does not induce p38- and IFN-beta autocrine 
      loop-dependent expression of CD38, resulting in poor migration and weak IL-12 
      secretion of dendritic cells.
PG  - 5732-42
LID - 10.4049/jimmunol.0803944 [doi]
AB  - Lyme borreliosis is a tick-borne bacterial infection that in many cases is 
      limited to the skin. However, in some patients the bacterium evades the immune 
      response and disseminates into various organs. Dendritic cells (DCs) are among 
      the first cells to meet invading pathogens in the skin. We have previously shown 
      that CD38, an ectoenzyme involved in the migration of DCs and generally 
      upregulated by microbial stimuli, is not upregulated in Borrelia 
      garinii-stimulated DCs. In this paper, we characterize the cellular events that 
      lead to the absence of CD38 on the DC surface after B. garinii stimulation and 
      investigate the consequences of absent CD38 expression for the migration of DCs 
      in vitro and in vivo. The data show that 1) effective signaling via p38 MAPK (and 
      STAT1 and NF-kappaB) is needed for CD38 expression and 2) TLR2 stimulation, as 
      opposed to TLR4 stimulation, does not induce IFN-beta autocrine loop-dependent 
      expression of CD38 and secretion of IL-12. Further, we show that 3) B. 
      garinii-stimulated DCs do not migrate effectively toward CCL19 and CCL21 and 4) 
      after B. garinii infection of mice, the number of DCs migrating from the 
      infection site to draining lymph nodes is only half that induced by Escherichia 
      coli infection. Our results provide evidence for the first time that different 
      TLR use results in different CD38 expression, which correlates with the migratory 
      potential of DCs.
FAU - Hartiala, Pauliina
AU  - Hartiala P
AD  - Department of Medical Microbiology and Immunology, University of Turku, Finland. 
      pauliina.hartiala@utu.fi
FAU - Hytonen, Jukka
AU  - Hytonen J
FAU - Yrjanainen, Heta
AU  - Yrjanainen H
FAU - Honkinen, Maria
AU  - Honkinen M
FAU - Terho, Perttu
AU  - Terho P
FAU - Soderstrom, Mirva
AU  - Soderstrom M
FAU - Penttinen, Markus A
AU  - Penttinen MA
FAU - Viljanen, Matti K
AU  - Viljanen MK
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100414
PL  - United States
TA  - J Immunol
JT  - Journal of immunology (Baltimore, Md. : 1950)
JID - 2985117R
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (TLR2 protein, human)
RN  - 0 (Tlr2 protein, mouse)
RN  - 0 (Toll-Like Receptor 2)
RN  - 187348-17-0 (Interleukin-12)
RN  - 77238-31-4 (Interferon-beta)
RN  - EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
RN  - EC 3.2.2.5 (CD38 protein, human)
RN  - EC 3.2.2.5 (Cd38 protein, mouse)
RN  - EC 3.2.2.6 (ADP-ribosyl Cyclase 1)
SB  - IM
MH  - *ADP-ribosyl Cyclase 1/biosynthesis/deficiency
MH  - Animals
MH  - Autocrine Communication/immunology
MH  - Borrelia burgdorferi Group/*immunology
MH  - *Cell Movement/immunology
MH  - Cells, Cultured
MH  - Dendritic Cells/*immunology/metabolism
MH  - Escherichia coli/immunology
MH  - Humans
MH  - *Interferon-beta/physiology
MH  - *Interleukin-12/metabolism
MH  - Lipopolysaccharides/physiology
MH  - *Membrane Glycoproteins/biosynthesis/deficiency
MH  - Mice
MH  - Mice, Inbred BALB C
MH  - Toll-Like Receptor 2/*metabolism/physiology
MH  - *p38 Mitogen-Activated Protein Kinases/biosynthesis/physiology
EDAT- 2010/04/16 06:00
MHDA- 2010/07/20 06:00
CRDT- 2010/04/16 06:00
PHST- 2010/04/16 06:00 [entrez]
PHST- 2010/04/16 06:00 [pubmed]
PHST- 2010/07/20 06:00 [medline]
AID - jimmunol.0803944 [pii]
AID - 10.4049/jimmunol.0803944 [doi]
PST - ppublish
SO  - J Immunol. 2010 May 15;184(10):5732-42. doi: 10.4049/jimmunol.0803944. Epub 2010 
      Apr 14.