Mechanism of lipid-protein interaction in the plasma lipoproteins: lipid-binding properties of synthetic fragments of apolipoprotein A-II

Biochemistry ◽  
1977 ◽  
Vol 16 (19) ◽  
pp. 4150-4156 ◽  
Author(s):  
S. J. T. Mao ◽  
J. T. Sparrow ◽  
E. B. Gilliam ◽  
A. M. Gotto ◽  
R. L. Jackson
1988 ◽  
Vol 153 (3) ◽  
pp. 1060-1067 ◽  
Author(s):  
Carlos Calvo ◽  
Corinne Talussot ◽  
Gabriel Ponsin ◽  
Francois Berthézène

1996 ◽  
Vol 242 (3) ◽  
pp. 657-664 ◽  
Author(s):  
Claire Benetollo ◽  
Gilles Lambert ◽  
Corinne Talussot ◽  
Berlinda Vanloo ◽  
Tom Cauteren ◽  
...  

Author(s):  
Masafumi Tanaka ◽  
Padmaja Dhanasekaran ◽  
David Nguyen ◽  
Margaret Nickel ◽  
Yuki Takechi ◽  
...  

2009 ◽  
Vol 15 (1) ◽  
pp. 36-42 ◽  
Author(s):  
Masafumi Tanaka ◽  
Toshitaka Tanaka ◽  
Shinya Ohta ◽  
Toru Kawakami ◽  
Hiroyuki Konno ◽  
...  

2002 ◽  
Vol 43 (8) ◽  
pp. 1283-1292 ◽  
Author(s):  
Dmitri Sviridov ◽  
Anh Hoang ◽  
Wei Huang ◽  
Jun Sasaki

Five mutants of apolipoprotein A-I (apoA-I), apoA-I(Δ63–73), apoA-I(Δ140–150), apoA-I(63–73@140–150), apoA-I(R149V), and apoA-I(P143A) were compared with human plasma apoA-I for their ability to promote cholesterol and phospholipid efflux from HepG2 cells. A significantly lower capacity to promote cholesterol and phospholipid efflux was observed with lipid-free apoA-I(Δ63–73), while mutations apoA-I(Δ140–150) and apoA-I(P143A) affected phospholipid efflux only. When added as apoA-I/palmitoyloleoyl phosphatidylcholine (POPC) complex, mutations apoA-I(63–73@140–150) and apoA-I(Δ140–150) affected cholesterol efflux. None of the mutations affected α-helicity of the lipid-free mutants or their self-association. Five natural mutations of apoA-I, apoA-I(A95D), apoA-I (Y100H), apoA-I(E110K), apoA-I(V156E), and apoA-I (H162Q) were studied for their ability to bind lipids and promote cholesterol efflux. None of the mutations affected lipid-binding properties, cholesterol efflux, or α-helicity of lipid-free mutants. Two mutations affected self-association of apoA-I: apoA-I(A95D) was more prone to self-association, while apoA-I(E100H) did not self-associate.The following conclusions could be made from the combined data: i) regions 210–243 and 63–100 are the lipid-binding sites of apoA-I and are also required for the efflux of lipids to lipid-free apoA-I, suggesting that initial lipidation of apoA-I is rate limiting in efflux; ii) in addition to the lipid-binding regions, the central region is important for cholesterol efflux to lipidated apoA-I, suggesting its possible involvement in interaction with cells.


Author(s):  
Vincent A. Rifici ◽  
Howard A. Eder ◽  
John B. Swaney

1984 ◽  
Vol 25 (2) ◽  
pp. 111-120
Author(s):  
M Rosseneu ◽  
G Assmann ◽  
M J Taveirne ◽  
G Schmitz

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