Disease relevance of APOAI

• Results also indicated that apolipoprotein A-I concentration was decreased in cows with hepatic lipidosis (fatty liver) induced by administration of ethionine, suggesting that this method is a useful tool for the pathophysiologic study of lipid metabolism and its impairment in cattle [1].
• Decreased serum apolipoprotein A-I concentrations in cows infected with Salmonella typhimurium [2].
• These results suggest that apolipoprotein A-I in cattle is in part of intestinal origin, and also that its decreased serum concentration in salmonellosis can be attributed to the reduced intestinal synthesis or secretion of this apolipoprotein [2].

High impact information on APOAI

• These results suggest that apolipoprotein A-I is involved in cholesterol efflux performed by high density lipoprotein [3].
• Cloning and sequencing of bovine apolipoprotein A-I cDNA and molecular evolution of apolipoproteins A-I and B-100 [4].
• These BSP proteins also interact with heparin, apolipoprotein A-I (apoA-I) and apoA-I associated with high-density lipoprotein (HDL) [5].
• Glycosyl-phosphatidylinositol-specific phospholipase D. Interaction with and stimulation by apolipoprotein A-I [6].
• Analytical accuracy of the method was examined by determining the amounts of NOG recovered from apolipoprotein A-I and myoglobin samples spiked with NOG [7].

Biological context of APOAI

• Apolipoprotein A-I was significantly increased in midlactation compared with concentrations in early lactation or dry period [8].
• At all stages of growth and development, the HDL apoprotein profiles showed a distinct band with a weight of about 28,000 Da, which represented apolipoprotein-A-I [9].

Anatomical context of APOAI

• By this detection procedure, we detected two apolipoprotein AI binding proteins in plasma membrane fractions from bovine liver and adrenal cortex with molecular masses of 120 kDa and 95 kDa [10].
• Binding of apolipoprotein A-I and apolipoprotein A-IV to cultured bovine aortic endothelial cells [11].

Associations of APOAI with chemical compounds

• 5. Four to six dinitrophenol groups were found to be conjugated with an apolipoprotein AI molecule without any obvious impairment of its binding activity to the binding proteins [10].
• Apolipoprotein AI-dinitrophenol was prepared by incubating the mixture of apolipoprotein AI and 2,4-dinitrobenzene sulfonic acid sodium salt at pH 8 [10].
• OBJECTIVE: To determine: whether apolipoprotein A-I (apoA-I) is secreted by calf liver parenchymal cells; the isoprotein pattern and association with lipids of secreted apoA-I; and effects of steroid hormones on apoA-I secretion [12].
• These results suggest that the decreased LCAT activity, which may be attributable to impaired hepatic secretion or to the suppression of the activity in the plasma by reduced concentrations of phosphatidylcholine and apolipoprotein A-I, resulted in the lower concentrations of cholesteryl esters [13].

Other interactions of APOAI

• The concentrations in the serum of apolipoprotein A-I, an activator of LCAT, was also reduced in cows with fatty livers [13].
• Antiserum raised against bovine apolipoprotein A-I, which does not activate lipoprotein lipase, removed the activating ability of serum [14].

Analytical, diagnostic and therapeutic context of APOAI

• Enzyme-linked immunosorbent assay for apolipoprotein A-I in the serum of cattle [1].
• A single radial immunodiffusion assay was developed to determine the concentration of the major apolipoprotein A-I in bovine serum [8].

References