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APOA2Apolipoprotein A-II
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Human apolipoprotein A-II enrichement displaces paraoxonase from HDL and impairs its antioxidant properties.
Fibrates increase human apolipoprotein A-II expression through activation of the peroxisome proliferator-activated receptor.
A splice-junction mutation responsible for familial apolipoprotein A-II deficiency.
Critical to these evaluations would be the demonstration of apolipoprotein A-II induction, confirming the functional responsiveness of human cell cultures.
Protein heterogeneity of lipoprotein particles containing apolipoprotein A-I without apolipoprotein A-II and apolipoprotein A-I with apolipoprotein A-II isolated from human plasma.
Evidence for linkage of the apolipoprotein A-II locus to plasma apolipoprotein A-II and free fatty acid levels in mice and humans.
This effect has been ascribed to an antioxidant effect of the added thiol group, but it is also observed that apolipoprotein A-I Milano forms homodimers and heterodimers with apolipoprotein A-II, which may contribute to changes in function (23, 24).
Serum levels of an isoform of apolipoprotein A-II as a potential marker for prostate cancer.
Concentration, (a) Rank Protein [micro] mol/L 1 Albumin 500-800 2 IgG 40-100 3 Apolipoprotein A-I 36-72 4 Transferrin 25-45 5 Apolipoprotein A-II 22-60 6 [[alpha].
Apolipoprotein A-I containing lipoproteins, with or without apolipoprotein A-II, as progenitors of pre-[beta] high-density lipoprotein particles.
Human apolipoprotein A-II is a pro-atherogenic molecule when it is expressed in transgenic mice at a level similar to that in humans: evidence of a potentially relevant species-specific interaction with diet.