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  • Title: Structure and biosynthesis of apolipoprotein B.
    Author: Olofsson SO, Boström K, Carlsson P, Borén J, Wettesten M, Bjursell G, Wiklund O, Bondjers G.
    Journal: Am Heart J; 1987 Feb; 113(2 Pt 2):446-52. PubMed ID: 3812204.
    Abstract:
    Apolipoprotein (apo) B100 copy deoxyribonucleic acid (cDNA) has been cloned and sequenced. The total sequence of apo B100 messenger ribonucleic acid has been revealed by the work from our group, as well as other groups. The sequence spans 13,689 nucleotides from the initiation to the stop codon. Thus the messenger has the capacity to code for 4563 amino acids corresponding to a molecular weight of approximately 510,000. Computer analyses revealed the presence of regions with amphipathic alpha-helix and of hydrophobic regions with a high probability of beta-structure. Regions of the molecule are characterized by continuous variations between hydrophillic and hydrophobic sequences, the latter coinciding with a high probability of beta-structure. It is suggested that this beta-structure is involved, together with the amphipathic alpha-helix, in the binding of apo B100 to the lipid. Pulse-chase studies in Hep G2 cells showed that apo B100 is synthesized as one protein, with a translation time of 14 minutes. The protein is transferred through the cell and secreted within 30 minutes without undergoing any major change in molecular mass. The residence kinetics in the endoplasmic reticulum (ER) is characterized by an increase during the first 10 to 15 minutes of chase followed by an almost linear decrease with a decay rate of 6%/min. The transfer through the ER to the Golgi apparatus accounts for one third of the time needed for the intracellular transfer of apo B100, whereas two thirds of the time is required for the transfer through the later part of the secretory pathway.(ABSTRACT TRUNCATED AT 250 WORDS)
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