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Activation of lecithin cholesterol acyltransferase by human apolipoprotein E in discoidal complexes with lipids.

Zorich, N, Jonas, A, Pownall, H J·1985·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(17)39427-9
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Abstract

In a continued investigation of lecithin cholesterol acyltransferase reaction with micellar discoidal complexes of phosphatidylcholine, cholesterol, and various water soluble apolipoproteins, we prepared complexes containing human apo-E by the cholate dialysis method. These complexes were systematically compared to apo-A-I complexes synthesized under the same reaction conditions. Apo-E complexes (134 A in diameter) were slightly larger than apo-A-I complexes (110 A) but were very similar in terms of their protein and lipid content (2.4:0.10:1.0, egg phosphatidylcholine/cholesterol/apolipoprotein, w/w) and in the percentage of apolipoprotein in alpha-helical structure (72-74%). Concentration and temperature-dependence experiments on the velocity of the lecithin cholesterol acyltransferase reaction revealed differences in apparent Km values and small differences in apparent Vmax but very similar activation energies (18-20 kcal/mol). These observations suggest that differences in lecithin cholesterol acyltransferase activation by apo-A-I and apo-E are primarily a result of different affinities of the enzyme for the particles but that the rate-limiting step of the reaction is comparable for both complexes. Apo-E was found to be 18% as effective as apo-A-I in activating purified human lecithin cholesterol acyltransferase. Addition of free apo-A-I to apo-E complexes resulted in the exchange of bound for free apolipoprotein causing a slight increase in the reactivity with the enzyme…

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Metadata

Authors
Zorich, N., Jonas, A., & Pownall, H. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1985-07
Volume
260
Issue
15
Pages
8831-8837
ISSN
0021-9258
DOI
10.1016/s0021-9258(17)39427-9
Cited by
62
References
0
Language
en
Licence

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