Influence of Divalent Cations upon Complement-Mediated Enzyme Release from Human Polymorphonuclear Leukocytes

Autor: Ira M. Goldstein, Sylvia T. Hoffstein, Gerald Weissmann
Rok vydání: 1975
Předmět:
Zdroj: The Journal of Immunology. 115:665-670
ISSN: 1550-6606
0022-1767
DOI: 10.4049/jimmunol.115.3.665
Popis: The complement component, C5a provokes the selective release of granule-associated enzymes from intact, viable cytochalasin B-treated human polymorphonuclear leukocytes (PMN) in the absence of phagocytosis or cellular adherence to surfaces. Consequently, in this experimental system the influence of divalent cations on these two processes can be disregarded and their effects on enzyme secretion can be studied directly. Cytochalasin B-treated PMN exposed to C5a in calcium and magnesium-free media consistently secreted significant amounts of the granule-associated enzymes, β-glucuronidase and lysozyme. This basal secretory response was not diminished if cells were preincubated with 5.0 mM EDTA, nor was it influenced if 1.0 mM or 2.0 mM EDTA were present in the reaction mixtures. The addition of calcium (up to 1.5 to 2.0 mM) produced a concentration-dependent enhancement of β-glucuronidase release, whereas increasing amounts of calcium (above 2.0 mM) inhibited secretion of this enzyme. Lysozyme release was similarly enhanced by the addition of calcium, but inhibition with high concentrations was not observed. Calcium per se, in the absence of C5a, provoked only the release of lysozyme from these cells. The effects of calcium upon enzyme release were not associated with alterations in the state of assembly of cytoplasmic microtubules. These findings provide another example of the role of calcium in “stimulus-secretion coupling” and provide evidence that exocytosis of various granules in human PMN is regulated by independent mechanisms involving calcium.
Databáze: OpenAIRE