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J Biol Chem, Vol. 274, Issue 27, 19338-19346, July 2, 1999

Characterization of Ca2+-dependent Phospholipase A2 Activity during Zebrafish Embryogenesis

Steven A. FarberDagger , Eric S. OlsonDagger , James D. Clark, and Marnie E. HalpernDagger

From the Dagger  Department of Embryology, Carnegie Institution of Washington, Baltimore, Maryland 21210 and  Genetics Institute, Cambridge, Massachusetts 02140

We have developed a simple fluorescent assay for detection of phospholipase A2 (PLA2) activity in zebrafish embryos that utilizes a fluorescent phosphatidylcholine substrate. By using this assay in conjunction with selective PLA2 inhibitors and Western blot analysis, we identified the principal activity in zebrafish embryogenesis as characteristic of the Ca2+-dependent cytosolic PLA2 (cPLA2) subtype. Embryonic cPLA2 activity remained constant from the 1-cell stage until the onset of somitogenesis, at which time it increased sharply. This increase was preceded by the expression of a previously identified zebrafish cPLA2 homologue (Nalefski, E., Sultzman, L., Martin, D., Kriz, R., Towler, P., Knopf, J., and Clark, J. (1994) J. Biol. Chem. 269, 18239-18249). By using a quenched BODIPY-labeled phosphatidylcholine that fluoresces only upon cleavage by PLA2, lipase activity was visualized in the cells of living embryos where it localized to perinuclear membranes.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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