PMID- 12117913
OWN - NLM
STAT- MEDLINE
DCOM- 20020904
LR  - 20210526
IS  - 0019-9567 (Print)
IS  - 1098-5522 (Electronic)
IS  - 0019-9567 (Linking)
VI  - 70
IP  - 8
DP  - 2002 Aug
TI  - Lipopolysaccharide-binding protein- and CD14-dependent activation of 
      mitogen-activated protein kinase p38 by lipopolysaccharide in human neutrophils 
      is associated with priming of respiratory burst.
PG  - 4068-74
AB  - Neutrophil (PMN) functions can be primed for greatly increased oxidative radical 
      release by exposure to certain agents such as lipopolysaccharide (LPS). Although 
      a variety of signaling pathways involving both tyrosine kinases and 
      mitogen-activated protein (MAP) kinases may be operative, the mechanisms of PMN 
      priming are still not understood. We found that PMN priming was not achieved by 
      treatment of cells with a very low concentration (5 ng/ml) of LPS unless 
      additional "helper" factors were present in plasma (5%). Under these conditions, 
      LPS induced tyrosine phosphorylation of a 38-kDa protein, which was coincident 
      with the MAP kinase p38 action in this situation. LPS-mediated activation of p38 
      in human PMNs was dependent on the presence of LPS binding protein from plasma 
      and CD14 on the surfaces of the cells. Phosphorylation of p38 was highly 
      correlated with LPS priming of a formyl-methionyl-leucyl-phenylalanine 
      (fMLP)-stimulated PMN respiratory burst. Treatment of PMN with the p38-specific 
      inhibitor SB203580 significantly attenuated the respiratory burst in cells primed 
      by LPS and stimulated by fMLP. These results suggest that the LPS signaling 
      pathway leading to p38 activation may be an important mechanism in regulation of 
      PMN priming. The mediator(s) linking CD14 to p38 involves proteins that are 
      functionally sensitive to genistein but insensitive to tyrphostin AG126 and to 
      Src- and Syk-family kinase, protein kinase C, and phosphatidylinositol 3-kinase 
      inhibitors. Elucidating this pathway will provide insight into possible 
      regulation of PMN priming by LPS.
FAU - Yan, Sen Rong
AU  - Yan SR
AD  - Department of Pediatrics, Dalhousie University and IWK Health Centre, Halifax, 
      Nova Scotia, Canada.
FAU - Al-Hertani, Walla
AU  - Al-Hertani W
FAU - Byers, David
AU  - Byers D
FAU - Bortolussi, Robert
AU  - Bortolussi R
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Infect Immun
JT  - Infection and immunity
JID - 0246127
RN  - 0 (Acute-Phase Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Lipopolysaccharide Receptors)
RN  - 0 (Lipopolysaccharides)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (lipopolysaccharide-binding protein)
RN  - 42HK56048U (Tyrosine)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (HCK protein, human)
RN  - EC 2.7.10.2 (Proto-Oncogene Proteins c-hck)
RN  - EC 2.7.10.2 (lyn protein-tyrosine kinase)
RN  - EC 2.7.10.2 (src-Family Kinases)
RN  - EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
RN  - EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases)
SB  - IM
MH  - *Acute-Phase Proteins
MH  - Carrier Proteins/*immunology
MH  - Cells, Cultured
MH  - Enzyme Activation
MH  - Humans
MH  - Lipopolysaccharide Receptors/*immunology
MH  - Lipopolysaccharides/*immunology/pharmacology
MH  - *Membrane Glycoproteins
MH  - Mitogen-Activated Protein Kinases/*immunology
MH  - Neutrophils/cytology/drug effects/*immunology
MH  - Phosphorylation
MH  - Protein-Tyrosine Kinases/immunology
MH  - Proto-Oncogene Proteins/immunology
MH  - Proto-Oncogene Proteins c-hck
MH  - Respiratory Burst/*immunology
MH  - Signal Transduction/*immunology
MH  - Tyrosine/metabolism
MH  - p38 Mitogen-Activated Protein Kinases
MH  - src-Family Kinases/immunology
PMC - PMC128158
EDAT- 2002/07/16 10:00
MHDA- 2002/09/06 10:01
PMCR- 2002/08/01
CRDT- 2002/07/16 10:00
PHST- 2002/07/16 10:00 [pubmed]
PHST- 2002/09/06 10:01 [medline]
PHST- 2002/07/16 10:00 [entrez]
PHST- 2002/08/01 00:00 [pmc-release]
AID - 0246 [pii]
AID - 10.1128/IAI.70.8.4068-4074.2002 [doi]
PST - ppublish
SO  - Infect Immun. 2002 Aug;70(8):4068-74. doi: 10.1128/IAI.70.8.4068-4074.2002.