PMID: 2108716Jan 9, 1990Paper

Intracellular modification of human apolipoprotein AII (apoAII) and sites of apoAII mRNA synthesis: comparison of apoAII with apoCII and apoCIII isoproteins

Biochemistry
M M Hussain, V I Zannis

Abstract

We have studied the intracellular modifications of human apoAII by pulse-chase labeling of HepG2 cell cultures with [35S]methionine or [3H]arginine followed by two-dimensional analysis and autoradiography of the radiolabeled apoAII isoproteins. A short (5.0-min) pulse showed the presence of a precursor form of apoAII (pI = 5.75) designated proapoAII or apoAII3. A 5-10-min chase resulted in a decrease in the relative concentration of the proapoAII coupled with an increase in the relative concentration of a new form (pI = 5.3) designated modified proapoAII or apoAII1. Longer chase resulted in the appearance of the plasma apoAII form and at least five other acidic apoAII isoproteins in the cell lysate and the culture medium. Labeling with [3H]arginine showed that apoAII isoproteins designated 3, 1, -1, and -3 contained the prosegment whereas isoproteins designated 1a, 0, -1a, -2a, -3a, and -4a did not. Comparison of nascent apoAII, apoCII, and apoCIII isoproteins revealed that they were distinctly different on the two-dimensional gels. Neuraminidase treatment converted the acidic apoAII isoproteins to isoproteins 1a and 0 (modified and plasma apoAII forms). The combined data are consistent with the following intra- and/or extracel...Continue Reading

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Citations

Jul 1, 1991·The Journal of Clinical Investigation·M F LintonS G Young
Nov 1, 2007·Nutrition & Metabolism·Amanda M Gonzales, Robert A Orlando
May 29, 2012·Journal of Lipid Research·Loren E SmithGiorgio Cavigiolio
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Mar 27, 2001·Current Opinion in Lipidology·V I ZannisD Kardassis
Jun 16, 2019·Kidney International·Michèle ChabertAthina D Kalopissis

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