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Apolipoprotein A-II

Apolipoprotein A-II, apoA-II
This gene encodes apolipoprotein (apo-) A-II, which is the second most abundant protein of the high density lipoprotein particles. The protein is found in plasma as a monomer, homodimer, or heterodimer with apolipoprotein D. Defects in this gene may result in apolipoprotein A-II deficiency or hypercholesterolemia. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: HDL, apolipoprotein A-I, Apo, HAD, apolipoprotein E
Papers on Apolipoprotein A-II
Activation of paraoxonase 1 after hemodialysis is associated with HDL remodeling and its increase in the HDL2 fraction and VLDL.
Kimura et al., Vallejo, United States. In Clin Chim Acta, 20 Apr 2014
No significant changes in apoAI or apoA-II the main structural HDL apolipoproteins were apparent after dialysis.
Hot spots in apolipoprotein A-II misfolding and amyloidosis in mice and men.
Gursky, Boston, United States. In Febs Lett, 18 Apr 2014
ApoA-II is the second-major protein of high-density lipoproteins.
Interaction of peptide-bound beads with lipopolysaccharide and lipoproteins.
Takagi et al., Takasaki, Japan. In J Microbiol Methods, 12 Apr 2014
Mass spectrometry analysis revealed that the 28kDa and 18kDa bands corresponded to apolipoprotein A-I (apoA-I) and apolipoprotein A-II (apoA-II), respectively.
Polymorphisms of mouse apolipoprotein A-II alter its physical and functional nature.
Reardon et al., Chicago, United States. In Plos One, Dec 2013
ApoA-II is the second most abundant protein on HDL making up ∼ 20% of the total protein but its functions have still only been partially characterized.
Serum protein signatures differentiating autoimmune pancreatitis versus pancreatic cancer.
Werner et al., Heidelberg, Germany. In Plos One, 2012
Among them apolipoprotein A-I, apolipoprotein A-II, transthyretin, and tetranectin were identified and found as 3.0-, 3.5-, 2-, and 1.6-fold decreased in PaCa sera, respectively, whereas haptoglobin and apolipoprotein E were found to be 3.8- and 1.6-fold elevated in PaCa sera.
Apolipoprotein A-II: evaluating its significance in dyslipidaemia, insulin resistance, and atherosclerosis.
Watts et al., Perth, Australia. In Ann Med, 2012
ApoA-II, a constituent apolipoprotein of certain HDL particles, plays an important role in the regulation of cholesterol efflux, HDL remodelling, and cholesteryl ester uptake via its interactions with lipid transfer proteins, lipases, and cellular HDL receptors.
Apolipoprotein A-II-mediated conformational changes of apolipoprotein A-I in discoidal high density lipoproteins.
Silva et al., Cincinnati, United States. In J Biol Chem, 2012
Apolipoprotein A-II-mediated conformational changes of apolipoprotein A-I in discoidal high density lipoproteins.
Apolipoprotein A-II polymorphism: relationships to behavioural and hormonal mediators of obesity.
Garaulet et al., Boston, United States. In Int J Obes (lond), 2012
APOA2 m265 genotype may be associated with eating behaviours and dietary modulation of plasma ghrelin.
ApoA-I deficiency in mice is associated with redistribution of apoA-II and aggravated AApoAII amyloidosis.
Higuchi et al., Matsumoto, Japan. In J Lipid Res, 2011
ApoA-I deficiency in mice is associated with redistribution of apoA-II and aggravated AApoAII amyloidosis.
Association between the APOA2 promoter polymorphism and body weight in Mediterranean and Asian populations: replication of a gene-saturated fat interaction.
Ordovas et al., Boston, United States. In Int J Obes (lond), 2011
a gene-diet interaction involving the APOA2 -265T>C SNP and saturated fat intake determines body weight in a Mediterranean and an Asian populations
Apolipoprotein A-II suppressed concanavalin A-induced hepatitis via the inhibition of CD4 T cell function.
Nakayama et al., Chiba, Japan. In J Immunol, 2011
Exacerbated hepatitis is observed in ApoA-II-deficient mice, indicating that ApoA-II plays a suppressive role in concanavalin A-induced hepatitis under physiological conditions.
Apolipoproteins and amyloid fibril formation in atherosclerosis.
Howlett et al., Melbourne, Australia. In Protein Cell, 2011
A number of plasma apolipoproteins, including apolipoprotein (apo) A-I, apoA-II, apoC-II and apoE are implicated in amyloid formation or influence amyloid formation by other proteins.
The effect of PPAR-alpha agonism on apolipoprotein metabolism in humans.
Millar et al., Philadelphia, United States. In Atherosclerosis, 2010
Fibrates also increase HDL apoA-I and apoA-II levels by enhancing apoA-I and apoA-II production, although this is partially counteracted by increasing fractional catabolism of these apolipoproteins.
HDL metabolism in context: looking on the bright side.
Chan et al., Perth, Australia. In Curr Opin Lipidol, 2008
RECENT FINDINGS: HDL-apoA-I and apoA-II may be better predictors of cardiovascular disease than HDL-cholesterol.
Structural requirements for antioxidative and anti-inflammatory properties of apolipoprotein A-I mimetic peptides.
Fogelman et al., Birmingham, United States. In J Lipid Res, 2007
Another protein component of HDL, apoA-II, has structural features similar to those of apoA-I but does not possess atheroprotective properties.
High-density lipoprotein binding to scavenger receptor-BI activates endothelial nitric oxide synthase.
Shaul et al., Dallas, United States. In Nat Med, 2001
In contrast, eNOS is not activated by purified forms of the major HDL apolipoproteins ApoA-I and ApoA-II or by low-density lipoprotein.
Linkage of familial combined hyperlipidaemia to chromosome 1q21-q23.
Peltonen et al., Helsinki, Finland. In Nat Genet, 1998
One marker, D1S104, adjacent to the apolipoprotein A-II (APOA2) gene on chromosome 1, revealed a lod score of Z = 3.50 assuming a dominant mode of inheritance.
Protein composition determines the anti-atherogenic properties of HDL in transgenic mice.
Rubin et al., Berkeley, United States. In Nature, 1993
High-density lipoprotein (HDL) contains two major proteins, apolipoprotein A-I (apoA-I) and apolipoprotein A-II (apoA-II), comprising about 70% and 20% of the total HDL protein mass, respectively.
Atherosclerosis in transgenic mice overexpressing apolipoprotein A-II.
Lusis et al., Los Angeles, United States. In Science, 1993
The two most abundant protein constituents of HDL are apolipoproteins A-I and A-II (apoA-I and apoA-II).
A multicenter comparison of lovastatin and cholestyramine therapy for severe primary hypercholesterolemia. The Lovastatin Study Group III.
In Jama, 1988
Cholestyramine resin treatment had no significant effect on very low-density lipoprotein cholesterol and apolipoprotein A-II levels and produced a median 11% increase in plasma triglyceride concentration; in contrast, administration of either 20 or 40 mg of lovastatin twice a day was associated with median reductions in very low-density lipoprotein cholesterol levels (-34% and -31%, respectively) and plasma triglyceride levels (-21% and -27%, respectively) and median increases in levels of apolipoprotein A-II (8% and 13%, respectively).
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