Identification of the cysteine residue in apolipoprotein(a) that mediates extracellular coupling with apolipoprotein B-100.
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چکیده
منابع مشابه
Identification of a critical lysine residue in apolipoprotein B-100 that mediates noncovalent interaction with apolipoprotein(a).
We have previously shown that lipoprotein(a) (Lp(a)) assembly involves an initial noncovalent interaction between sequences within apolipoprotein(a) (apo(a)) kringle IV types 5-8 and the amino terminus of apolipoprotein B-100 (sequences between amino acids 680 and 781 in apoB-100), followed by formation of a disulfide bond. In the present study, citraconylation of lysine residues in apoB-100 ab...
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The ability of low-density lipoprotein (LDL) to inhibit the procoagulant activity of tissue factor is mediated by a direct protein-protein interaction involving apolipoprotein (apo) B-100. A lysine-rich sequence within apo B-100 (residues 3121-3217), which we have termed lysine-rich apo B-100-derived (KRAD)-98 peptide, may be responsible for its activity. Within this region, residues 3147-3160 ...
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Familial defective apolipoprotein B-100 is a genetic disorder of apolipoprotein B-100 that causes moderate to severe hypercholesterolemia. A single amino acid mutation in apolipoprotein B diminishes the ability of low density lipoproteins to bind to the low density lipoprotein receptor. Low density lipoproteins accumulate in the plasma because their efficient receptor-mediated catabolism is dis...
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Apolipoprotein B is the main structural surface protein found on all beta-lipoproteins (Chylomicrons, VLDLs, IDLs and LDLs). There is a single molecule of apoB on each of those lipoproteins. It is the only apolipoprotein that is not transferablei.e. it is with the particle from its birth till its death. Beta-lipoproteins are the lipoproteins capable of trafficking cholesterol into the artery wa...
متن کاملIdentification of the base substitution responsible for the Ag(x/y) polymorphism of apolipoprotein B-100.
The identification of the base substitution responsible for Ag(x/y) completes the description of the antigen group polymorphisms associated with the apolipoprotein B polypeptide. Surprisingly, all five antigen group polymorphisms alter restriction endonuclease cleavage sites and have associated restriction fragment length polymorphisms, thereby providing a convenient alternative for antigen gro...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)36587-1