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Carboxyl‐terminal truncation of apolipoproteinB‐100 inhibits lipoprotein(a) particle formation
Author(s) -
Gabel Brent,
Yao Zemin,
McLeod Roger S.,
Young Stephen G.,
Koschinsky Marlys L.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00737-3
Subject(s) - apolipoprotein b , recombinant dna , lipoprotein(a) , chemistry , lipoprotein , truncation (statistics) , microbiology and biotechnology , biochemistry , biology , cholesterol , gene , mathematics , statistics
Recombinant expression systems for both apo(a) and apoB were used to identify sequences in apoB which are required for Lp(a) formation. Incubation of a [ 35 S]Cys‐labelled 17‐kringle form of apo(a) with supernatants from rat hepatoma (McA‐RH7777) cells expressing apoB‐88, apoB‐94 and apoB‐100 resulted in covalent r‐Lp(a) formation only with apoB‐100. Additionally, apoB‐86 present in the LDL of a hypobetalipoproteinemic subject did not associate with a 12‐kringle form of recombinant apo(a) to form r‐Lp(a) complexes. Our data suggest that sequences within the C‐terminal 6% of apoB‐100 are essential for Lp(a) assembly.