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Journal of Lipid Research, Vol. 41, 1410-1418, September 2000
Copyright © 2000 by Lipid Research, Inc.

Original Article

Structure and interfacial properties of chicken apolipoprotein A-IV

Richard B. Weinberga, Rachel A. Andersona, Victoria R. Cooka, Florence Emmanuelb, Patrice Deneflec, Marcela Hermannd, and Armin Steinmetzd
a Section of Gastroenterology, Department of Internal Medicine, Wake Forest University School of Medicine, Winston-Salem, NC 27157
b Cardiovascular Department, Aventis Pharma, 94403 Vitry sur Seine, France
c Gencell Division, and Evry Genomics Center, Aventis Pharma, 94403 Vitry sur Seine, France
d Department of Molecular Genetics, Institute of Medical Biochemistry, University and Biocenter Vienna, A-1030 Vienna, Austria

Correspondence to: Richard B. Weinberg

To gain insight into the evolution and function of apolipoprotein A-IV (apoA-IV) we compared structural and interfacial properties of chicken apoA-IV, human apoA-IV, and a recombinant human apoA-IV truncation mutant lacking the carboxyl terminus. Circular dichroism thermal denaturation studies revealed that the thermodynamic stability of the {alpha}-helical structure in chicken apoA-IV ({Delta}H = 71.0 kcal/mol) was greater than that of human apoA-IV (63.6 kcal/mol), but similar to that of human apoA-I (73.1 kcal/mol). Fluorescence chemical denaturation studies revealed a multiphasic red shift with a 65% increase in relative quantum yield that preceded loss of {alpha}-helical structure, a phenomenon previously noted for human apoA-IV. The elastic modulus of chicken apoA-IV at the air/water interface was 13.7 mN/m, versus 21.7 mN/m for human apoA-IV and 7.6 mN/m for apoA-I. The interfacial exclusion pressure of chicken apoA-IV for phospholipid monolayers was 31.1 mN/m, versus 33.0 mN/m for human A-I and 28.5 mN/m for apoA-IV.

We conclude that the secondary structural features of chicken apoA-IV more closely resemble those of human apoA-I, which may reflect the evolution of apoA-IV by intraexonic duplication of the apoA-I gene. However, the interfacial properties of chicken apoA-IV are intermediate between those of human apoA-I and apoA-IV, which suggests that chicken apoA-IV may represent an ancestral prototype of mammalian apoA-IV, which subsequently underwent further structural change as an evolutionary response to the requisites of mammalian lipoprotein metabolism.—Weinberg, R. B., R. A. Anderson, V. R. Cook, F. Emmanuel, P. Denefle, M. Hermann, and A. Steinmetz. Structure and interfacial properties of chicken apolipoprotein A-IV. J. Lipid Res. 2000. 41: 1410;–1418.

Supplementary key words: surface tension, interfacial elasticity, monolayers, fluorescence, spectroscopy, molecular evolution


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