The non-venom insect phospholipases A2.
Phospholipases A(2) (PLA(2)s) are responsible for releasing the fatty acid moiety from the sn-2 position of phospholipids. These enzymes are virtually ubiquitous proteins known from all major biological taxa. Various PLA(2)s act in a wide array of biological processes, including digestion of dietary lipids, cellular homeostasis, intra- and intercellular signaling, host defense and at least a few ecological interactions. PLA(2) activities have been recorded in a small number of insect species, which can be taken to represent the broad group, Insecta. Within insects, PLA(2)s act in functions expected from the background on these enzymes. So far, we know PLA(2)s act in lipid digestion, cellular host defense signaling, reproduction and in organismal-level metabolism. Additional PLA(2) actions are certain to emerge. This is the first article devoted to assembling the known information on insect PLA(2)s. I review the scant information available on the biological actions of PLA(2)s in insects, relate new findings on insect pathogens that disrupt insect immune functions by inhibiting PLA(2)s and mention the few reports of sequence information on insect PLA(2)s. Finally, I offer a brief prospectus on future research into insect PLA(2)s. There are two overarching points in this paper. One, there remains a great deal to learn about insect PLA(2)s and two, some of the findings on insect PLA(2)s will have meaningful practical significance.
Stanley
David
D
USDA/Agricultural Research Service, Biological Control of Insects Research Laboratory, 1503 S. Providence Road, Columbia, MO 65203, USA. stanleyd@missouri.edu
D000818:Animals; D006706:Homeostasis / Q000502:physiology; D019476:Insect Proteins / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D007313:Insecta / Q000201:enzymology* / Q000235:genetics / Q000276:immunology; D050356:Lipid Metabolism / Q000502:physiology*; D010741:Phospholipases A / Q000235:genetics / Q000276:immunology / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*; D014688:Venoms / Q000378:metabolism
D019476:Insect Proteins; D014688:Venoms; D010741:Phospholipases A