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lüll Synthesis, transport, and processing of apolipoproteins of high density lipoproteins Stoffel WJ Lipid Res 1984[Dec]; 25 (13): 1586-92Cell biology methods have greatly influenced the elucidation of the biosynthetic pathways of apolipoproteins. In vitro and tissue culture systems allow the study, to a large extent, of the process of synthesis, intracellular processing, secretion, and extracellular processing of the major high density lipoprotein apoproteins apoA-I and A-II and also of a minor component, apoA-IV. Whereas the latter apoprotein is equipped only with a signal sequence, the primary translation products of apoA-I and apoA-II carry N-terminal extensions of preprosequence of 24 amino acids for apoA-I and 23 amino acid residues for apoA-II. The pro-form of apoA-I characterized by a hexapeptide extension is completely stable intracellularly and is secreted as such. The pro-form is further processed by a serum protease specific for an unusual -Gln-Gln-Asp-Glu-sequence site. Pro-apoA-II, a pentapeptide sequence, is partially processed intracellularly to its mature form and secreted together with the residual pro-form. The cleavage site of pro-apoA-II is characterized by two basic amino acid residues Arg-Arg, present also in other known pro-proteins. The biological function of the N-terminal pro-sequences and details of their final processing by the serum protease(s) have yet to be established.|Amino Acid Sequence[MESH]|Animals[MESH]|Apolipoprotein A-I[MESH]|Apolipoprotein A-II[MESH]|Apolipoproteins A/metabolism[MESH]|Apolipoproteins/*metabolism[MESH]|Biological Transport, Active[MESH]|Humans[MESH]|In Vitro Techniques[MESH]|Intestinal Mucosa/metabolism[MESH]|Lipoproteins, HDL/*metabolism[MESH]|Liver/metabolism[MESH]|Protein Biosynthesis[MESH]|Protein Processing, Post-Translational[MESH]|RNA, Messenger/metabolism[MESH]|Rats[MESH] |