Baboon apolipoprotein A-IV. Identification of Lys76–&gt;Glu that distinguishes two common isoforms and detection of length polymorphisms at the carboxyl terminus

Hixson, James E.; Kammerer, Candace M.; Mott, Glen E.; Britten, Marjorie L.; Birnbaum, Shifra; Powers, Patricia K.; VandeBerg, John L.

doi:10.1016/s0021-9258(18)82308-0

Journal of Biological Chemistry

1993

DOI: 10.1016/s0021-9258(18)82308-0

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Baboon apolipoprotein A-IV. Identification of Lys76–>Glu that distinguishes two common isoforms and detection of length polymorphisms at the carboxyl terminus

James E. Hixson

Candace M. Kammerer

Glen E. Mott

et al.

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Cited by 12 publications

(1 citation statement)

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“…The C terminus of apoA-IV contains a unique and highly conserved tetrapeptide repeat with the sequence EQ(Q/A/V)Q (8). This region is the site of murine (16), baboon (17), and human (18,19) genetic polymorphisms that affect apoA-IV structure (12), plasma lipid levels (reviewed in ref. 20), and the response to diet (17, 21 -23).…”

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Structure and interfacial properties of chicken apolipoprotein A-IV

Weinberg

Anderson

Cook

et al. 2000

Journal of Lipid Research

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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 ␣ -helical structure in chicken apoA-IV ( ⌬ H ϭ 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 ␣ -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. -

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confidence: 99%

Structure and interfacial properties of chicken apolipoprotein A-IV

Weinberg

Anderson

Cook

et al. 2000

Journal of Lipid Research

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Cloning, characterization and comparative analysis of pig plasma apolipoprotein A-IV

Navarro¹,

Acı́n²,

Iturralde³

et al. 2004

Gene

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Identification of functional domains in the plasma apolipoproteins by analysis of inter-species sequence variability.

Weinberg

1994

Journal of Lipid Research

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Baboon apolipoprotein A-IV. Identification of Lys76–>Glu that distinguishes two common isoforms and detection of length polymorphisms at the carboxyl terminus

Cited by 12 publications

References 44 publications

Structure and interfacial properties of chicken apolipoprotein A-IV

Structure and interfacial properties of chicken apolipoprotein A-IV

Cloning, characterization and comparative analysis of pig plasma apolipoprotein A-IV

Identification of functional domains in the plasma apolipoproteins by analysis of inter-species sequence variability.

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