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GENERAL ARTICLES

Mild Hyperthermia Down-Regulates Receptor-Dependent Neutrophil Function

Dieter Fröhlich, MD^*, Sigrid Wittmann, MD^*, Gregor Rothe, MD, Daniel I. Sessler, MD, Peter Vogel, MD, and Kai Taeger, MD^*

Departments of *Anesthesia, Clinical Chemistry and Laboratory Medicine, and Surgery, University of Regensburg, Regensburg, Germany; and Outcomes Research^TM Institute and Departments of Anesthesiology and Pharmacology, University of Louisville, Louisville, Kentucky

Address correspondence and reprint requests to Dieter Fröhlich, MD, Department of Anesthesia, University of Regensburg, Franz-Josef-Strauß-Allee 11, Regensburg, 93053, Germany. Address e-mail to dieter.froehlich{at}klinik.uni-regensburg.de

Mild hypothermia impairs resistance to infection and, reportedly, impairs phagocytosis and oxidative killing of un-opsonized bacteria. We evaluated various functions at 33°–41°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)- 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 with opsonized bacteria. Hypothermia slightly increased N-formyl-L-methionyl-L-leucyl-phenylalanine receptors on neutrophils: hyperthermia decreased expression, especially with TNF-. N-formyl-L-methionyl-L-leucyl-phenylalanine-induced H₂O₂ production was inversely related to temperature, especially in the presence of TNF-. 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.

IMPLICATIONS: In contrast to nonreceptor-dependent phagocytosis and oxidative killing, several crucial receptor-dependent functions of neutrophils have a temperature-dependent regulation, with increased function during hypothermia and reduced function during hyperthermia.

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