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(Journal of Leukocyte Biology. 2003;73:511-524.)
© 2003 by Society for Leukocyte Biology

Lysophosphatidylcholines prime the NADPH oxidase and stimulate multiple neutrophil functions through changes in cytosolic calcium

Christopher C. Silliman*,{dagger},{ddagger}, David J. Elzi*,{dagger}, Daniel R. Ambruso*,{dagger}, Rene J. Musters{ddagger}, Christine Hamiel{ddagger}, Ronald J. Harbeck§, Andrew J. Paterson*,{dagger}, A. Jason Bjornsen{dagger}, Travis H. Wyman{dagger}, Marguerite Kelher{ddagger}, Kelly M. England{dagger}, Nathan McLaughlin-Malaxecheberria{dagger}, Carlton C. Barnett{ddagger}, Junichi Aiboshi{ddagger} and Anirban Bannerjee{ddagger}

* Bonfils Blood Center and Departments of
{dagger} Pediatrics and
{ddagger} Surgery, University of Colorado School of Medicine, Denver; and
§ Department of Laboratory Medicine, National Jewish Center for Allergy and Respiratory Medicine, Denver, Colorado

Correspondence: Christopher C. Silliman, M.D., Ph.D., Associate Medical Director, Bonfils Blood Center, 717 Yosemite Circle, Denver, CO 80230. E-mail: Christopher.Silliman{at}uchsc.edu

A mixture of lysophosphatidylcholines (lyso-PCs) are generated during blood storage and are etiologic in models of acute lung injury. We hypothesize that lyso-PCs stimulate polymorphonuclear neutrophils (PMNs) through Ca2+-dependent signaling. The lyso-PC mix (0.45–14.5 µM) and the individual lyso-PCs primed formyl-Met-Leu-Phe (fMLP) activation of the oxidase (1.8- to 15.7-fold and 1.7- to 14.8-fold; P<0.05). Labeled lyso-PCs demonstrated a membrane association with PMNs and caused rapid increases in cytosolic Ca2+. Receptor desensitization studies implicated a common receptor or a family of receptors for the observed lyso-PC-mediated changes in PMN priming, and cytosolic Ca2+ functions were pertussis toxin-sensitive. Lyso-PCs caused rapid serine phosphorylation of a 68-kD protein but did not activate mitogen-activated protein kinases or cause changes in tyrosine phosphorylation. With respect to alterations in PMN function, lyso-PCs caused PMN adherence, increased expression of CD11b and the fMLP receptor, reduced chemotaxis, provoked changes in morphology, elicited degranulation, and augmented fMLP-induced azurophilic degranulation (P<0.05). Cytosolic Ca2+ chelation inhibited lyso-PC-mediated priming of the oxidase, CD11b surface expression, changes in PMN morphology, and serine phosphorylation of the 68-kD protein. In conclusion, lyso-PCs affect multiple PMN functions in a Ca2+-dependent manner that involves the activation of a pertussis toxin-sensitive G-protein.

Key Words: adhesion • chemotaxis • morphology




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