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Gene Review

APOC3  -  apolipoprotein C-III

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Disease relevance of ApoC3


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


Analytical, diagnostic and therapeutic context of ApoC3


  1. Decreases in serum apolipoprotein C-III concentration in cows with ethionine-induced fatty liver. Nitanai, A., Katoh, N., Oikawa, S., Saitoh, M., Hamada, M., Kutsuzawa, A., Mohamed, T., Uchida, E., Endoh, D., Kurosawa, T., Sato, H. J. Vet. Med. Sci. (2004) [Pubmed]
  2. Decreased apolipoprotein C-III concentration in the high-density lipoprotein fraction from calves inoculated with Pasteurella haemolytica and bovine herpes virus-1. Yamamoto, M., Katoh, N. J. Vet. Med. Sci. (2000) [Pubmed]
  3. Decreased concentration of serum apolipoprotein C-III in cows with fatty liver, ketosis, left displacement of the abomasum, milk fever and retained placenta. Yamamoto, M., Nakagawa-Ueta, H., Katoh, N., Oikawa, S. J. Vet. Med. Sci. (2001) [Pubmed]
  4. Chymotryptic cleavage of lipoprotein lipase. Identification of cleavage sites and functional studies of the truncated molecule. Lookene, A., Bengtsson-Olivecrona, G. Eur. J. Biochem. (1993) [Pubmed]
  5. Activation of lipoprotein lipase by apolipoprotein C-II is modulated by the COOH terminal region of apolipoprotein C-III. Catapano, A.L. Chem. Phys. Lipids (1987) [Pubmed]
  6. Identification and purification of apolipoprotein C-III from the serum of cows. Yamamoto, M., Katoh, N., Adachi, Y., Oikawa, S. Am. J. Vet. Res. (1998) [Pubmed]
  7. 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. Yamamoto, M., Katoh, N., Oikawa, S. Am. J. Vet. Res. (1998) [Pubmed]
  8. Concentrations of apolipoprotein C-III in healthy cows during the peripartum period and cows with milk fever. Katoh, N., Nakagawa-Ueta, H. J. Vet. Med. Sci. (2001) [Pubmed]
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