Expression and conservation of apolipoprotein AIV in an avian species.

The Journal of Biological Chemistry
A SteinmetzW J Schneider

Abstract

In birds, intestinally derived lipoproteins are thought to be secreted directly into the portal vein rather than to enter the circulation via the lymphatic system as in mammals. Hepatic clearance of these so-called portomicrons must be rapid, but the protein(s) mediating their catabolism, presumably analogues of the 36-kDa mammalian apolipoprotein E, have not been identified. In searching for such a mediator(s), we have isolated a hitherto unknown 38-kDa protein from chicken serum, which we identified by microsequencing and molecular cloning as a counterpart to mammalian apolipoprotein AIV (apoAIV). Mature chicken apoAIV consists of 347 amino acids, lacks cysteine residues, and displays 57% sequence identity with human apoAIV and, to a significantly lesser extent, with apoAIVs of rodents. This first nonmammalian apoAIV characterized is the smallest homologue reported so far, because of the lack of repeated motifs at the carboxyl terminus with the consensus sequence Glu-Gln-Glu/Ala-Gln, a hallmark of mammalian apoAIVs. Chicken apoAIV (isoelectric point, 4.65) is also considerably more acidic than its human counterpart. Agarose gel electrophoresis revealed that unlike human apoAIV, which migrates to a pre-alpha-position, chicken ...Continue Reading

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Citations

Aug 2, 2001·The Journal of Experimental Zoology·A E Duggan, I P Callard
Jan 20, 2000·Trends in Cardiovascular Medicine·A Steinmetz, W J Schneider
Mar 30, 2001·Biochimica Et Biophysica Acta·H KondoS Watabe
Sep 21, 2013·Biochimie·Birgit NikolayMarcela Hermann
Apr 3, 2007·Journal of Lipid Research·Andrea DichlbergerWolfgang J Schneider
Jun 3, 2017·Proteome Science·Emily L O'ReillyP David Eckersall

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