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J. Biol. Chem., Vol. 261, Issue 21, 9591-9594, Jul, 1986

Human preproapolipoprotein C-II. Analysis of major plasma isoforms

SS Fojo, L Taam, T Fairwell, R Ronan, C Bishop, MS Meng, JM Hoeg, DL Sprecher and HB Brewer Jr

Apolipoprotein C-II plays a major role in lipid metabolism as a cofactor for lipoprotein lipase, the enzyme involved in the hydrolysis of triglyceride-rich lipoproteins. Apo-C-II is initially synthesized as a 101 amino acid protein that undergoes subsequent cotranslational cleavage of a signal peptide. Post-translational processing of apo-C-II has not been previously described. In this manuscript we identify four major plasma isoforms of apo-C-II by two-dimensional gel electrophoresis and immunoblot analysis that result from post- translational modification of apo-C-II. Neuraminidase studies have shown that two of these isoforms are early secreted sialic acid containing glycoproteins. Amino acid compositional and amino-terminal analysis have established that the major plasma isoform of apo-C-II is proapo-C-II. Proapo-C-II undergoes proteolytic cleavage of its amino- terminal hexapeptide to generate the mature form of apo-C-II. Thus, apo- C-II appears to be secreted as a carbohydrate containing proprotein that then undergoes deglycosylation and proteolytic cleavage to generate mature apo-C-II, a minor isoform in plasma. An improved understanding of the structural relationship of the various plasma isoforms of apo-C-II will help to elucidate the mechanisms involved in normal, as well as defective, processing of apo-C-II.
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