Differential properties of phosphatidate phosphohydrolase and diacylglyceride lipase activities in retinal subcellular fractions and rod outer segments

Comp Biochem Physiol B. 1993 Jan;104(1):141-8. doi: 10.1016/0305-0491(93)90350-e.

Abstract

1. The effect of magnesium and dl-propranolol on phosphatidate phosphohydrolase (PAPase) and diacylglycerol lipase (DGL) activities in isolated rod outer segments (ROS) and of the former on subcellular fractions from bovine retina was investigated. 2. Mg(2+)-independent PAPase activity was found in ROS, whereas in the other subcellular fractions PAPase activities both dependent on and independent of Mg2+ were detected. 3. The membrane-bound PAPase activity was stimulated at low concentrations of Mg2+ and inhibited at higher concentrations. The soluble activity was always stimulated by the ion. 4. dl-Propranolol (1000 microM) exerted a slight stimulatory effect on PAPase in ROS whereas total PAPase activity of microsomal fraction was not affected. 5. Mg2+ (0.2 mM) stimulated DGL activity (30%) whereas it was inhibited at higher concentration. 6. DGL lipase activities, both dependent on and independent of Mg2+, were detected in subcellular fractions of bovine retina. 7. DGL properties in ROS are also described.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Cattle
  • Cytosol / enzymology
  • Lipoprotein Lipase / metabolism*
  • Magnesium / pharmacology
  • Microsomes / enzymology
  • Mitochondria / enzymology
  • Phosphatidate Phosphatase / metabolism*
  • Propranolol / pharmacology
  • Retina / drug effects
  • Retina / enzymology*
  • Retina / ultrastructure
  • Rod Cell Outer Segment / enzymology*
  • Subcellular Fractions / enzymology*
  • Synaptosomes / enzymology

Substances

  • Propranolol
  • Lipoprotein Lipase
  • Phosphatidate Phosphatase
  • Magnesium