Document Detail


Mild hyperthermia down-regulates receptor-dependent neutrophil function.
MedLine Citation:
PMID:  15281545     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mild hypothermia impairs resistance to infection and, reportedly, impairs phagocytosis and oxidative killing of unopsonized bacteria. We evaluated various functions at 33 degrees-41 degrees C in neutrophils taken from volunteers. Adhesion on endothelial cells was determined using light microscopy. Adhesion molecule expression and receptors, phagocytosis, and release of reactive oxidants were assessed using flow cytometric assays. Adhesion protein CD11b expression on resting neutrophils was temperature-independent. However, up-regulation of CD11b with tumor necrosis factor (TNF)-alpha was increased by hypothermia and decreased with hyperthermia. Neutrophil adhesion to either resting or activated endothelial cells was not temperature-dependent. Bacterial uptake was inversely related to temperature, more so with Escherichia coli than Staphylococcus aureus. Temperature dependence of phagocytosis occurred only wi thopsonized bacteria. Hypothermia slightly increased N-formyl-L-methionyl-L-leucyl-phenylalanine receptors on neutrophils: hyperthermia decreased expression, especially with TNF-alpha. N-formyl-L-methionyl-L-leucyl-phenylalanine-induced H2O2 production was inversely related to temperature, especially in the presence of TNF-alpha. Conversely, phorbol-13-myristate-12-acetate, an activator of protein kinase C, induced an extreme and homogenous release of reactive oxidants that increased with temperature. In contrast to nonreceptor-dependent phagocytosis and oxidative killing, several crucial receptor-dependent neutrophil activities show temperature-dependent regulation, with hypothermia increasing function. The temperature dependence of neutrophil function is thus more complicated than previously appreciated.
Authors:
Dieter Fröhlich; Sigrid Wittmann; Gregor Rothe; Daniel I Sessler; Peter Vogel; Kai Taeger
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Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Anesthesia and analgesia     Volume:  99     ISSN:  0003-2999     ISO Abbreviation:  Anesth. Analg.     Publication Date:  2004 Jul 
Date Detail:
Created Date:  2004-07-29     Completed Date:  2004-08-26     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  1310650     Medline TA:  Anesth Analg     Country:  United States    
Other Details:
Languages:  eng     Pagination:  284-92     Citation Subset:  AIM; IM    
Affiliation:
Department of Anesthesia, University of Regensburg, Regensburg, Germany. dieter.froehlich@klinik.uni-regensburg.de
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MeSH Terms
Descriptor/Qualifier:
Adult
Antigens, CD11b / biosynthesis
Cell Adhesion Molecules / metabolism
Down-Regulation / physiology*
Enzyme Activators / pharmacology
Fever / physiopathology*
Humans
Hydrogen Peroxide / blood
N-Formylmethionine Leucyl-Phenylalanine / metabolism
Neutrophils / physiology*
Oxidants / blood
Oxidative Stress / drug effects
Phagocytosis / drug effects,  physiology
Protein Kinase C / metabolism
Receptors, Leukocyte-Adhesion / drug effects
Temperature
Tetradecanoylphorbol Acetate / pharmacology
Tumor Necrosis Factor-alpha / biosynthesis
Grant Support
ID/Acronym/Agency:
GM 061655/GM/NIGMS NIH HHS; R01 GM061655-02/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Antigens, CD11b; 0/Cell Adhesion Molecules; 0/Enzyme Activators; 0/Oxidants; 0/Receptors, Leukocyte-Adhesion; 0/Tumor Necrosis Factor-alpha; 16561-29-8/Tetradecanoylphorbol Acetate; 59880-97-6/N-Formylmethionine Leucyl-Phenylalanine; 7722-84-1/Hydrogen Peroxide; EC 2.7.11.13/Protein Kinase C
Comments/Corrections

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