Skip to main content
PMC home page
The American Journal of Pathology logoLink to The American Journal of Pathology
. 1983 Oct;113(1):90–94.

Release of phospholipase A2 activity from rabbit peritoneal neutrophils by f-Met-Leu-Phe.

C Lanni, E L Becker
PMCID: PMC1916300  PMID: 6624881

Abstract

Rabbit peritoneal neutrophils secrete phospholipase A2 activity in response to f-Met-Leu-Phe (FMLP). The secretion of phospholipase A2, like that of the known granule enzymes, requires cytochalasin B and is enhanced by extracellular Ca2+, and the time course of the release is rapid, being completed in less than a minute. The concentration dependence of the secretion of the phospholipase is the same as that of the known granule enzymes up to 10(-9) M FMLP. At this concentration, the release of the known granule enzymes reaches a maximum, but that of phospholipase A2 does not until 10(-8) M FMLP. The amount of enzyme activity released plus the amount of enzyme activity remaining in the pellet is distinctly greater than the total enzyme activity extractable from the cell before release. The phospholipase secreted is active in the neutral to alkaline range, requires Ca2+, is inhibited by low levels of detergent, and is of A2 specificity.

Full text

PDF
90

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Franson R., Dobrow R., Weiss J., Elsbach P., Weglicki W. B. Isolation and characterization of a phospholipase A2 from an inflammatory exudate. J Lipid Res. 1978 Jan;19(1):18–23. [PubMed] [Google Scholar]
  2. Franson R., Patriarca P., Elsbach P. Phospholipid metabolism by phagocytic cells. Phospholipases A2 associated with rabbit polymorphonuclear leukocyte granules. J Lipid Res. 1974 Jul;15(4):380–388. [PubMed] [Google Scholar]
  3. Franson R., Weiss J., Martin L., Spitznagel J. K., Elsbach P. Phospholipase A activity associated with membranes of human polymorphonuclear leucocytes. Biochem J. 1977 Dec 1;167(3):839–841. doi: 10.1042/bj1670839. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Henson P. M. The immunologic release of constituents from neutrophil leukocytes. II. Mechanisms of release during phagocytosis, and adherence to nonphagocytosable surfaces. J Immunol. 1971 Dec;107(6):1547–1557. [PubMed] [Google Scholar]
  5. Lanni C., Franson R. C. Localization and partial purification of a neutral-active phospholipase A2 from BCG-induced rabbit alveolar macrophages. Biochim Biophys Acta. 1981 Mar 13;658(1):54–63. doi: 10.1016/0005-2744(81)90249-7. [DOI] [PubMed] [Google Scholar]
  6. Sahu S., Lynn W. S. Phospholipase A in pulmonary secretions of patients with alveolar proteinosis. Biochim Biophys Acta. 1977 May 25;487(2):354–360. doi: 10.1016/0005-2760(77)90011-x. [DOI] [PubMed] [Google Scholar]
  7. Shaw J. O., Roberts M. F., Ulevitch R. J., Henson P., Dennis E. A. Phospholipase A2 contamination of cobra venom factor preparations. Biologic role in complement-dependent in vivo reactions and inactivation with p-bromophenacyl bromide. Am J Pathol. 1978 Jun;91(3):517–530. [PMC free article] [PubMed] [Google Scholar]
  8. Showell H. J., Freer R. J., Zigmond S. H., Schiffmann E., Aswanikumar S., Corcoran B., Becker E. L. The structure-activity relations of synthetic peptides as chemotactic factors and inducers of lysosomal secretion for neutrophils. J Exp Med. 1976 May 1;143(5):1154–1169. doi: 10.1084/jem.143.5.1154. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Showell H. J., Naccache P. H., Walenga R. W., Dalecki M., Feinstein M. B., Sha'afi R. I., Becker E. L. The effects of quercetin, 1-tosylamido-2-phenylethyl chloromethyl ketone, cytochalasin A and nordihydroguaiaretic acid on lysosomal enzyme secretion, arachidonic acid metabolism and Ca2+ fluxes in rabbit neutrophils. J Reticuloendothel Soc. 1981 Sep;30(3):167–181. [PubMed] [Google Scholar]
  10. Traynor J. R., Authi K. S. Phospholipase A2 activity of lysosomal origin secreted by polymorphonuclear leucocytes during phagocytosis or on treatment with calcium. Biochim Biophys Acta. 1981 Sep 24;665(3):571–577. doi: 10.1016/0005-2760(81)90272-1. [DOI] [PubMed] [Google Scholar]
  11. Vadas P., Hay J. B. The appearance and significance of phospholipase A2 in lymph draining tuberculin reactions. Am J Pathol. 1982 Jun;107(3):285–291. [PMC free article] [PubMed] [Google Scholar]
  12. Vadas P. The efficacy of anti-inflammatory agents with respect to extracellular phospholipase A2 activity. Life Sci. 1982 Jan 11;30(2):155–162. doi: 10.1016/0024-3205(82)90647-6. [DOI] [PubMed] [Google Scholar]
  13. Victor M., Weiss J., Klempner M. S., Elsbach P. Phospholipase A2 activity in the plasma membrane of human polymorphonuclear leukocytes. FEBS Lett. 1981 Dec 28;136(2):298–300. doi: 10.1016/0014-5793(81)80639-4. [DOI] [PubMed] [Google Scholar]
  14. Weiss J., Beckerdite-Quagliata S., Elsbach P. Determinants of the action of phospholipases A on the envelope phospholipids of Escherichia coli. J Biol Chem. 1979 Nov 10;254(21):11010–11014. [PubMed] [Google Scholar]

Articles from The American Journal of Pathology are provided here courtesy of American Society for Investigative Pathology

RESOURCES