Complexity in the Secretory Pathway: The Assembly and Secretion of Apolipoprotein B-containing Lipoproteins
2002; Elsevier BV; Volume: 277; Issue: 20 Linguagem: Inglês
10.1074/jbc.r100068200
ISSN1083-351X
AutoresEdward A. Fisher, Henry N. Ginsberg,
Tópico(s)RNA regulation and disease
ResumoApolipoprotein B100 (apoB100) is expressed primarily in mammalian liver. It has 4536 amino acids, 25 cysteines (16 of which are in intramolecular disulfide bonds), and 20 N-linked glycosylation sites. A smaller form, apoB48, is expressed in mammalian intestine and in the livers of some non-human mammals. ApoB48 results from a post-transcriptional modification of the apoB mRNA at codon 2153 that converts a glutamine codon to a stop codon at ∼48% of the full-length coding sequence. Both forms of apoB have a complex structure that includes a globular amphipathic NH2 domain spanning the first 15–20% (using B100 as a standard length) of the polypeptide followed by an extended hydrophobic β-sheet domain from about 20 to 48%.
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