Proteomic analysis of plasma membrane and secretory vesicles from human neutrophils |
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| Authors: | Deepa Jethwaney Md Rafiqul Islam Kevin G Leidal Daniel Beltran-Valero de Bernabe Kevin P Campbell William M Nauseef and Bradford W Gibson |
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| Institution: | (1) Buck Institute for Age Research, Novato, CA 94945, USA;(2) Inflammation Program, Department of Medicine, University of Iowa and Veterans Administration Medical Center, Iowa City, IA 52240, USA;(3) Department of Molecular Physiology and Biophysics, Department of Neurology, andDepartment of Internal Medicine, Howard Hughes Medical Institute, Senator Paul D. Wellstone Muscular Dystrophy Cooperative Research Center, University of Iowa, Iowa City, IA 52240, USA |
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| Abstract: | Background Polymorphonuclear neutrophils (PMN) constitute an essential cellular component of innate host defense against microbial invasion
and exhibit a wide array of responses both to particulate and soluble stimuli. As the cells recruited earliest during acute
inflammation, PMN respond rapidly and release a variety of potent cytotoxic agents within minutes of exposure to microbes
or their products. PMN rely on the redistribution of functionally important proteins, from intracellular compartments to the
plasma membrane and phagosome, as the means by which to respond quickly. To determine the range of membrane proteins available
for rapid recruitment during PMN activation, we analyzed the proteins in subcellular fractions enriched for plasma membrane
and secretory vesicles recovered from the light membrane fraction of resting PMN after Percoll gradient centrifugation and
free-flow electrophoresis purification using mass spectrometry-based proteomics methods. |
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