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dc.contributor.authorVose, Brent M
dc.contributor.authorBlackledge, George
dc.contributor.authorCrowther, Derek
dc.contributor.authorGallagher, John T
dc.date.accessioned2011-06-21T16:46:36Z
dc.date.available2011-06-21T16:46:36Z
dc.date.issued1982-07
dc.identifier.citationLectin-binding characteristics of human natural killer cells. 1982, 46 (3):619-27 Immunologyen
dc.identifier.issn0019-2805
dc.identifier.pmid7095832
dc.identifier.urihttp://hdl.handle.net/10541/134095
dc.description.abstractHuman natural killer (NK) cells separated initially by density centrifugation of lymphocytes (E+) forming rosettes with sheep red blood cells (SRBC), were further fractionated on gradients of bovine serum albumin (BSA). Low density fractions contained effector cells which displayed high cytotoxicity against the NK-sensitive erythroleukaemic cell line, K562. These low density cells, which expressed receptors for Fc and the monoclonal antibody OKMI, showed enhanced cytotoxicity when treated with lymphoblastoid interferon (IFN-alpha). They also showed an increased response to phytomitogen in comparison with unseparated cells or those recovered from high density fractions. Two lymphocyte subsets one of high and one of low lectin binding capacity were identified in the E+ populations by their reactivity with Lens culinaris agglutinin (LCA). High LCA binding was observed only in low density fractions and was associated with a marked enrichment of NK activity. This property was used to separate the NK active population in E+ cells by fluorescence-activated cell sorting (FACS). These data add a new dimension to the cell surface properties of human NK cells and suggest the presence of LCA-reactive glycoproteins which are either enriched in, or uniquely associated with, cells of the NK subset. The experiments indicate that lectins can serve as useful probes of lymphocyte function and provide the basis for effective cell sorting.
dc.language.isoenen
dc.subject.meshAdult
dc.subject.meshAntibodies, Monoclonal
dc.subject.meshBinding Sites
dc.subject.meshCell Line
dc.subject.meshCell Separation
dc.subject.meshCentrifugation, Density Gradient
dc.subject.meshHumans
dc.subject.meshKiller Cells, Natural
dc.subject.meshLectins
dc.subject.meshLymphocyte Activation
dc.subject.meshRosette Formation
dc.titleLectin-binding characteristics of human natural killer cells.en
dc.typeArticleen
dc.contributor.departmentImmunology, Paterson Laboratories, Christie Hospital and Holt Radium Institute, Manchester, M20 9BX, UK.en
dc.identifier.journalImmunologyen
html.description.abstractHuman natural killer (NK) cells separated initially by density centrifugation of lymphocytes (E+) forming rosettes with sheep red blood cells (SRBC), were further fractionated on gradients of bovine serum albumin (BSA). Low density fractions contained effector cells which displayed high cytotoxicity against the NK-sensitive erythroleukaemic cell line, K562. These low density cells, which expressed receptors for Fc and the monoclonal antibody OKMI, showed enhanced cytotoxicity when treated with lymphoblastoid interferon (IFN-alpha). They also showed an increased response to phytomitogen in comparison with unseparated cells or those recovered from high density fractions. Two lymphocyte subsets one of high and one of low lectin binding capacity were identified in the E+ populations by their reactivity with Lens culinaris agglutinin (LCA). High LCA binding was observed only in low density fractions and was associated with a marked enrichment of NK activity. This property was used to separate the NK active population in E+ cells by fluorescence-activated cell sorting (FACS). These data add a new dimension to the cell surface properties of human NK cells and suggest the presence of LCA-reactive glycoproteins which are either enriched in, or uniquely associated with, cells of the NK subset. The experiments indicate that lectins can serve as useful probes of lymphocyte function and provide the basis for effective cell sorting.


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