Disease relevance of ApoC3

• Decreases in serum apolipoprotein C-III concentration in cows with ethionine-induced fatty liver [1].
• Decreased apolipoprotein C-III concentration in the high-density lipoprotein fraction from calves inoculated with Pasteurella haemolytica and bovine herpes virus-1 [2].
• Decreased concentration of serum apolipoprotein C-III in cows with fatty liver, ketosis, left displacement of the abomasum, milk fever and retained placenta [3].

High impact information on ApoC3

• The activity of c-LPL was more sensitive to inhibition by other lipid-binding proteins, e.g. apolipoprotein CIII (apo CIII), than was the intact enzyme [4].
• I speculate that apo C-III may act by inhibiting the apo C-II-LPL interaction [5].
• CONCLUSIONS: The role of apolipoprotein C-III in cows may involve a function related to lactation [6].
• PROCEDURE: Apolipoprotein C-III was identified by use of amino-terminal amino acid sequence analysis of bands separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis [6].
• Concentration of apoC-III was significantly (P < 0.05) higher in cows during midlactation than in cows during the nonlactating stage and was correlated negatively with serum triglyceride concentration (r = -0.479; P < 0.01) and positively with total cholesterol (r = 0.421; P< 0.05) and phospholipids (r= 0.415; P< 0.05) concentrations [7].

Biological context of ApoC3

• ApoC-III concentrations in 17 cows were monitored during the peripartum period (-48 to +12 days from parturition) [8].

Associations of ApoC3 with chemical compounds

• Serum apolipoprotein C-III concentration was significantly (P < 0.05) higher in cows during lactation than in nonlactating cows and was negatively correlated with serum triglyceride concentration (r = -0.620, P < 0.01) [6].
• In the ELISA for serum apoC-III concentration, addition of 2-mercaptoethanol to the coating buffer (50 mM sodium carbonate buffer, pH 9.6) was required [7].
• The distinct difference in change between apoC-III and apoB-100 suggests that apoC-III may be regulated by other pathways, in addition to inhibiting the synthesis of apoproteins by ethionine [1].

Other interactions of ApoC3

• Activation of lipoprotein lipase by apolipoprotein C-II is modulated by the COOH terminal region of apolipoprotein C-III [5].
• A 3-fold molar apo C-III excess decreased the lipoprotein lipase activity by 25% [5].

Analytical, diagnostic and therapeutic context of ApoC3

• Evaluation of serum apolipoprotein C-III concentration by enzyme-linked immunosorbent assay and its higher concentration in cows during midlactation than during the nonlactating stage [7].

References