Role of the Arg123-Tyr166 paired helix of apolipoprotein A-I in lecithin:cholesterol acyltransferase activation.

The Journal of Biological Chemistry
A DhoestP Holvoet

Abstract

The Arg123-Tyr166 central and Ala190-Gln243 carboxyl-terminal pairs of helices of apoA-I were substituted with the pair of helices of apoA-II, resulting in the apoA-I(Delta(Arg123-Tyr166), nablaA-II(Ser12-Ala75)) and apoA-I(Delta(Ala190-Gln243), nablaA-II(Ser12-Gln77)) chimeras, respectively. The structures of these chimeras in aqueous solution and in reconstituted high density lipoproteins (rHDL) and the lecithin:cholesterol acyltransferase (LCAT) activation properties of the rHDL were studied. Recombinant human apoA-I and the chimeras were expressed in Escherichia coli and purified from the periplasmic space. Binding of the apolipoproteins with palmitoyloleoylphosphatidylcholine was associated with a similar shift of Trp fluorescence maxima from 337 to 332 nm, from 339 to 334 nm, and from 337 to 333 nm, respectively. All rHDL had a Stokes radius of 4.8 nm and contained 2 apolipoprotein molecules/particle. Circular dichroism measurements revealed eight alpha-helices per apoA-I and per chimera molecule. The catalytic efficiencies of LCAT activation were 1.5 +/- 0.33 (mean +/- S.D.; n = 3), 0.054 +/- 0.009 (p < 0.001 versus apoA-I), and 1.3 +/- 0.32 (p = not significant versus apoA-I) nmol of cholesteryl ester/h/microM, respecti...Continue Reading

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Citations

May 15, 2002·Trends in Cardiovascular Medicine·Mary G Sorci-Thomas, Michael J Thomas
Dec 9, 2000·Biochimica Et Biophysica Acta·A Jonas
Mar 30, 2001·Biochimica Et Biophysica Acta·C G BrouilletteD W Borhani
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Jan 23, 2016·Frontiers in Pharmacology·Valentin Gogonea
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Apr 10, 2003·The Journal of Biological Chemistry·Robert S KissRobert O Ryan
Jun 7, 2011·Journal of Proteomics·Mutay Aslan, Serdar Dogan

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