Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-2-6
pubmed:abstractText
Oxygen-dependent antimicrobial activity of human polymorphonuclear leukocytes (PMNs) relies on the phagocyte nicotinamide adenine dinucleotide phosphate (NADPH) oxidase to generate oxidants. As the oxidase transfers electrons from NADPH the membrane will depolarize and concomitantly terminate oxidase activity, unless there is charge translocation to compensate. Most experimental data implicate proton channels as the effectors of this charge compensation, although large-conductance Ca2+-activated K+ (BK) channels have been suggested to be essential for normal PMN antimicrobial activity. To test this latter notion, we directly assessed the role of BK channels in phagocyte function, including the NADPH oxidase. PMNs genetically lacking BK channels (BK(-/-)) had normal intracellular and extracellular NADPH oxidase activity in response to both receptor-independent and phagocytic challenges. Furthermore, NADPH oxidase activity of human PMNs and macrophages was normal after treatment with BK channel inhibitors. Although BK channel inhibitors suppressed endotoxin-mediated tumor necrosis factor-alpha secretion by bone marrow-derived macrophages (BMDMs), BMDMs of BK(-/-) and wild-type mice responded identically and exhibited the same ERK, PI3K/Akt, and nuclear factor-kappaB activation. Based on these data, we conclude that the BK channel is not required for NADPH oxidase activity in PMNs or macrophages or for endotoxin-triggered tumor necrosis factor-alpha release and signal transduction BMDMs.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-11145680, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-11390995, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-11559775, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-11907569, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-12089369, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-12673252, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-14734109, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-14985765, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-15194823, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-15361657, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-15901769, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-16702353, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-16951373, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-17673505, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-17850484, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-18826950, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-2460627, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-6273471, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-6330272, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-7829869, http://linkedlifedata.com/resource/pubmed/commentcorrection/19074007-9139125
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Indoles, http://linkedlifedata.com/resource/pubmed/chemical/Large-Conductance..., http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 1, http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 3, http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/NF-kappa B, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt, http://linkedlifedata.com/resource/pubmed/chemical/Superoxides, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha, http://linkedlifedata.com/resource/pubmed/chemical/p38 Mitogen-Activated Protein..., http://linkedlifedata.com/resource/pubmed/chemical/paxilline
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1528-0020
pubmed:author
pubmed:issnType
Electronic
pubmed:day
5
pubmed:volume
113
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1326-31
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:19074007-Animals, pubmed-meshheading:19074007-Female, pubmed-meshheading:19074007-Flow Cytometry, pubmed-meshheading:19074007-Immunity, Innate, pubmed-meshheading:19074007-Indoles, pubmed-meshheading:19074007-Large-Conductance Calcium-Activated Potassium Channels, pubmed-meshheading:19074007-Lipopolysaccharides, pubmed-meshheading:19074007-Macrophages, pubmed-meshheading:19074007-Male, pubmed-meshheading:19074007-Mice, pubmed-meshheading:19074007-Mice, Inbred C57BL, pubmed-meshheading:19074007-Mice, Knockout, pubmed-meshheading:19074007-Mitogen-Activated Protein Kinase 1, pubmed-meshheading:19074007-Mitogen-Activated Protein Kinase 3, pubmed-meshheading:19074007-Muscle, Smooth, Vascular, pubmed-meshheading:19074007-NADPH Oxidase, pubmed-meshheading:19074007-NF-kappa B, pubmed-meshheading:19074007-Neutrophils, pubmed-meshheading:19074007-Phagocytes, pubmed-meshheading:19074007-Phosphatidylinositol 3-Kinases, pubmed-meshheading:19074007-Proto-Oncogene Proteins c-akt, pubmed-meshheading:19074007-Respiratory Burst, pubmed-meshheading:19074007-Signal Transduction, pubmed-meshheading:19074007-Superoxides, pubmed-meshheading:19074007-Tibial Arteries, pubmed-meshheading:19074007-Tumor Necrosis Factor-alpha, pubmed-meshheading:19074007-p38 Mitogen-Activated Protein Kinases
pubmed:year
2009
pubmed:articleTitle
BK channels in innate immune functions of neutrophils and macrophages.
pubmed:affiliation
Department of Nephrology, Campus-Virchow, Medical Faculty of the Charité, Experimental and Clinical Research Center at the Max Delbrück Center for Molecular Medicine, Berlin, Germany.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.
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