Membrane Bound Diacylglycerol Lipases in Bovine Brain: Purification and Characterization

  • Akhlaq A. Farooqui
  • W. Allen Taylor
  • Lloyd A. Horrocks
Part of the FIDIA Research Series book series (FIDIA, volume 4)

Abstract

It is becoming increasingly evident that diacylglycerols, a minor component of mammalian plasma membranes, regulate the activity of protein kinase C (Berridge, 1984). This enzyme has been implicated in the control of cell division, membrane fusion, differentiation, and signal transduction across the cell membrane (Downes, 1983; Nishizuka 1983, 1984; Das and Rand, 1984; Majerus et al., 1984). Furthermore, diacylglycerols have been reported to stimulate the activities of phospholipases by perturbing the bilayer structure of biological membranes (Dawson et al., 1983; 1984; Watson et al., 1984). In brain, diacylglycerols are either phosphorylated to phosphatidic acid by diacylglycerol kinase (Sun, 1983; Bazan, 1983) or hydrolyzed to free fatty acids and monoacylglycerol by diacylglycerol lipase (Cabot and Gatt, 1976, 1977, 1978; Rousseau et al., 1983; Rousseau and Gatt, 1984; Farooqui et al., 1985a,b).

Keywords

Bovine Brain Sodium Taurocholate Left Ordinate Monoacylglycerol Lipase Diacylglycerol Lipase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • Akhlaq A. Farooqui
    • 1
  • W. Allen Taylor
    • 1
  • Lloyd A. Horrocks
    • 1
  1. 1.Department of Physiological ChemistryThe Ohio State UniversityColumbusUSA

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