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Lipoteichoic acid-antilipoteichoic acid complexes induce superoxide generation by human neutrophils

dc.contributor.authorGinsburg, Isaacen_US
dc.contributor.authorFligiel, Suzanne E. G.en_US
dc.contributor.authorWard, Peter A.en_US
dc.contributor.authorVarani, Jamesen_US
dc.date.accessioned2006-09-11T14:53:48Z
dc.date.available2006-09-11T14:53:48Z
dc.date.issued1988-12en_US
dc.identifier.citationGinsburg, Isaac; Fligiel, Suzanne E. G.; Ward, Peter A.; Varani, James; (1988). "Lipoteichoic acid-antilipoteichoic acid complexes induce superoxide generation by human neutrophils." Inflammation 12(6): 525-548. <http://hdl.handle.net/2027.42/44498>en_US
dc.identifier.issn1573-2576en_US
dc.identifier.issn0360-3997en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/44498
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2851550&dopt=citationen_US
dc.description.abstractHuman neutrophils (PMNs) which have been incubated with lipoteichoic acid (LTA) from group A streptococci generated large amounts of Superoxide (O 2 − chemiluminescence and hydrogen peroxide when challenged with anti-LTA antibodies. Cytochalasin B further enhanced O 2 * generation. The onset of Of generation by the LTA-anti-LTA complexes was much faster than that induced by BSA-anti-BSA complexes. LTA-treated PMNs generated much less O 2 * when challenged with BSA complexes, suggesting that LTA might have blocked, nonspecifically, some of the Fc receptors on PMNs. PMNs treated with LTA-anti-LTA complexes further interacted with bystander nonsensitized PMNs resulting in enhanced Of generation, suggesting that small numbers of LTA-sensitized PMNs might recruit additional PMNs to participate in the generation of toxic oxygen species. Protelolytic enzyme treatment of PMNs further enhanced the generation of O 2 − by PMNs treated with LTA-anti-LTA. Superoxide generation could also be induced when PMNs and anti-LTA antibodies interacted with target cells (fibroblasts, epithelial cells) pretreated with LTA. This effect was also further enhanced by pretreatment of the target cells with proteases. PMNs incubated with LTA released lysosomal enzymes following treatment with anti-LTA antibodies. The amounts of phosphatase, Β -glucoronidase, N -acetylglucosaminidase, mannosidase, and lysozyme release by LTA-anti-LTA complexes were much smaller than those released by antibody or histone-opsonized streptococci, suggesting that opsonized particles are more efficient lysosomal enzyme releasers. However, since the amounts of O 2 − generated by the LTA complexes equaled those generated by the opsonized particles, it is assumed that the signals for triggering a respiratory burst and lysosomal enzyme secretion might be different.en_US
dc.format.extent1353911 bytes
dc.format.extent3115 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherKluwer Academic Publishers-Plenum Publishers; Plenum Publishing Corporation ; Springer Science+Business Mediaen_US
dc.subject.otherPathologyen_US
dc.subject.otherMedicine & Public Healthen_US
dc.subject.otherPharmacology/Toxicologyen_US
dc.subject.otherInternal Medicineen_US
dc.subject.otherRheumatologyen_US
dc.titleLipoteichoic acid-antilipoteichoic acid complexes induce superoxide generation by human neutrophilsen_US
dc.typeArticleen_US
dc.subject.hlbsecondlevelPathologyen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Pathology, The University of Michigan Medical School, Ann Arbor, Michiganen_US
dc.contributor.affiliationumDepartment of Pathology, The University of Michigan Medical School, Ann Arbor, Michiganen_US
dc.contributor.affiliationumDepartment of Oral Biology, Hebrew University Hadassah School of Dental Medicine Founded by Alpha Omega Fraternity, Jerusalem, Israel; The Department of Pathology, The University of Michigan, USAen_US
dc.contributor.affiliationumDepartment of Pathology, The University of Michigan Medical School, Ann Arbor, Michiganen_US
dc.contributor.affiliationumcampusAnn Arboren_US
dc.identifier.pmid2851550en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/44498/1/10753_2004_Article_BF00914316.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1007/BF00914316en_US
dc.identifier.sourceInflammationen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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