Release of chemical mediators from partially purified human lung mast cells.
Human lung mast cells dispersed by enzymatic digestion of human lung fragments were concentrated to greater than 50% purity by sedimentation in isopycnic and velocity gradients. The dispersed lung mast cells had a characteristic ultrasturctural appearance including granules with a scroll or reticular structural appearance including granules with a scroll or reticular structure surrounded by perigranular membranes. Histamine and preformed eosinophilotactic activity sedimented with mast cells on isopycnic gradients, and mast cells and these mediators were separated from the bulk of the other lung cells after velocity gradient sedimentation. The histamine content of isolated lung mast cells was calculated to range from 1.0 to 5.5 pg/cell. The quantity of SRS-A generated with anti-IgE or specific antigen was relatively limited but confined to the mast cell-rich fractions and associated with release of histamine and eosinophilotactic activity.
D002500:Centrifugation, Isopycnic; D004804:Eosinophils / Q000276:immunology*; D000939:Epitopes; D006636:Histamine Release; D006801:Humans; D007073:Immunoglobulin E / Q000378:metabolism; D008168:Lung / Q000166:cytology / Q000276:immunology*; D008407:Mast Cells / Q000276:immunology*; D013189:SRS-A / Q000096:biosynthesis
D000939:Epitopes; D013189:SRS-A; D007073:Immunoglobulin E