Abstract
Lecithins: cholesterol acyl transferase (LCAT) is an enzyme of man and many animal species which catalyzes the formation of cholesteryl esters (CE) in plasma. Glomset(l) was first to describe in 1962 that phosphatidyl choline (lecithin) and free cholesterol (FC) are involved in this reactions LCAT transfers the fatty acid of position -2 of lecithin to the -OH group of free cholesterol yielding in lysolecithin and CE.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
J.A. Glomset and J.L. Wright, Some properties of a cholesterol esterifying enzyme in human plasma, Biochim. Biophys. Acta 89: 266 (1964).
J.A. Glomset, An exercise in comparative biology. In: Progr. Biochem. Pharmacol. S. Eisenberg ed, Karger Basel (1979) 41pp.
M. Dobiasova, Lecithins cholesterol acyltransferase and the regulation of endogenous cholesterol transport, Adv-Lipid Res. 20: 107 (1983).
G.M. Kostner, LCAT and the cholesterol transfer, Proc. of the IVth. Dresdener Lipid Symposium, VEB Dresden (1982) 640.
J. Kostner, Studies on the cofactor requirements of LCAT, Scand. J. Clin. Lab. Invest. 33,Suppl.137: 19 (1974).
H. Dieplinger and G.M. Kostner, The determination of LCAT. Ins Handbook of Electrophoresis, L.A. Lewis, J.J. Opplt eds CRC press N.Y., (1983) 57pp.
P.J. Barter, G.J. Hopkins, G.D. Calvert and Y.C. Ha, A model of plasma esterified cholesterol metabolism: The role of esterified cholesterol transfer and exchanges between plasma lipoproteins, In: Lipoprotein Kinetics and Modeling, Acad. Press N.Y.,(1982) 351pp.
D.B. Zilversmit, Lipid transfer proteinss Overview and applications, Methods in Enzymology 98: 565 (1983).
Y.C. Ha, and P.J. Barter, Differences in plasma cholesteryl ester transfer activity in sixteen vertebrate species, Comp. Biochem, Physiol. 71B: 265 (1982).
R.L. Hamilton, M.C. Williams, C.J. Fielding and R.J. Havel, Discoidal bilayer structure of nascent HDL from perfused rat liver, J. Clin. Invest. 58: 667 (1976).
J.A. Glomset, K.R. Norurn, E. Gjone, Plasma lipoproteins in familial LCAT deficiency: Effects of dietary manipulations, Scand. J. Clin. Lab, Invest. 35,Suppl.142: 3 (1975).
A.V. Nichols, E.L. Gong and P.J. Blanche, Interconversion of HDL during incubation of human plasma, Biochim. Biophys. Res. Commun. 100: 391 (1981).
J.R. Patsch, A.M. Botto, T. Olivecrona and S. Eisenberg, Formation of HDL-like particles during lipolysis of VLDL in vitro. Proc. Natl. Acad. Sci. USA 75: 4519 (1978).
H. Dieplinger, R. Zechner and G.M. Kostner, The in vitro formation of HDL-2 during the action of LCAT: the role of triglyceride rich lipoproteins, J. Lipid Res. 26: 273 (1985).
G. Knipping, R. Zechner, G.M. Kostner and A. Holasek, Factors affecting the conversion of HDL: experiments with pig and human plasma, Biochim. Biophys. Acta 835: 244 (1985).
G.M. Kostner, The influence of various lipoproteins and apo-lipoproteins on the in vitro esterification of cholesterol in human serum by the enzyme LCAT, Scand.J. Cl in. Lab. Invest. 38,Suppl. 150: 66 (1978).
R. Zechner, H. Dieplinger, A. Roscher and G.M. Kostner, The LDL pathway of native and chemically modified LDL isolated from plasma incubated in vitro, Biochem. J. 224: 569 (1984).
G.M. Kostner, F. Krempler, H. Dieplinger, R. Zechner, I. Teubl and F. Sandhofer, Alterd metabolism of low density lipoprotein in humans after prolonged incubation in plasma, Clin. Sci. 68: 411 (1985).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1987 Plenum Press, New York
About this chapter
Cite this chapter
Kostner, G.M., Knipping, G., Groener, J.E.M., Zechner, R., Dieplinger, H. (1987). The Role of LCAT and Cholesteryl Ester Transfer Proteins for the HDL and LDL Structure and Metabolism. In: Malmendier, C.L., Alaupovic, P. (eds) Lipoproteins and Atherosclerosis. Advances in Experimental Medicine and Biology, vol 210. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1268-0_12
Download citation
DOI: https://doi.org/10.1007/978-1-4684-1268-0_12
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-1270-3
Online ISBN: 978-1-4684-1268-0
eBook Packages: Springer Book Archive