Hydrolysis of phospholipids by purified milk lipoprotein lipase. Effect of apoprotein CII, CIII, A and E, and synthetic fragments

Daniel A. Lambert, Louis C. Smith, Henry J. Pownall, John T. Sparrow, Jean Pierre Nicolas, Antonio Gotto

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

Different pyrene-labeled phospholipid monolayer vesicles were used as substrates for the bovine milk lipoprotein lipase activity. The effects of synthetic fragments of apoprotein C II were measured on the hydrolysis of 1-myristoyl-2[9(1pyrenyl)-nonanoyl] phosphatidylcholine in vesicles: The activating capacity of fragments 30-78 and 43-78, 50-78 and 55-78, compared to entire apo CII, were similar to that obtained with hydrolysable triglycerides. Our study shows that the longer the carboxy terminal fragment is, the higher is the activation. The phospholipid hydrolysis activity represents in the presence of apo C II, 36% of the triglycerides hydrolysis activity. Phospholipid hydrolysis is less dependent on activator than triglycerides hydrolysis (100% and 300% of increase with apo CII for phosphatidyl-choline and triglycerides respectively). The ratio hydrolysis without apo C II/hydrolysis with apo CII was different when other phospholipids than myrystoyl-phospatidylcholine were assayed: phosphatidyl-serine, ethanolamine, -choline, -glycerol, or diglycerides and butanoylglycerols. Fragment CIII1 (1-40) which did not bind to lipids, had no inhibitory effect. The entire sugar moiety and the first 40 amino acids are not required for the total inhibition of LPL. Inhibition was also obtained with Apo A I, A II,C I and fragments of apo E. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)19-33
Number of pages15
JournalClinica Chimica Acta
Volume291
Issue number1
DOIs
StatePublished - Jan 20 2000

Keywords

  • Apolipoproteins
  • Hyperlipoproteinemia
  • Lipoprotein lipase
  • Protein cofactors

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry

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