Rabbit neutrophils incubated in low-ionic-strength media were stimulated by ATP to secrete lysosomal enzymes. This was greatly enhanced in the presence of cytochalasin B. ATP in these circumstances induced the cell to form large cytoplasmic extensions that were largely devoid of granules. In the presence of both ATP and cytochalasin B, however, the projections contained granules in close proximity to the cell membrane. Neutrophils in low-ionic-strength buffer were capable of binding to zymosan particles coated with C3b but not of phagocytizing them. Release of granule enzymes was observed and exocytosis of granules appeared to occur at sites distant from those portions of the plasma membrane adherent to the particle.
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Support was provided by U.S.P.H.S. grant A1-07007 and GMS 19322-03 and by U.S.P.H.S. Career Development Award 1-KO4GM-42567-05 to Dr. P.M. Henson. This is publication no. 873 from the Department of Immunopathology, Scripps Clinic and Research Foundation, La Jolla, California.
Support was provided by U.S.P.H.S. grant A1-09648.
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Henson, P.M., Henson, J.E. & Becker, E.L. Ultrastructural alterations during ATP-induced secretion of lysosomal enzymes from rabbit polymorphonuclear leukocytes. Inflammation 1, 85–91 (1975). https://doi.org/10.1007/BF00918061
- Public Health
- Cell Membrane
- Internal Medicine
- Lysosomal Enzyme