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Gene Review

APOB  -  apolipoprotein B (including Ag(x) antigen)

Gallus gallus

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Disease relevance of APOB


High impact information on APOB

  • We have used the newly isolated clones, as well as the yolk protein cDNAs previously available [VTGII, apolipoprotein II (apoVLDLII), and apolipoprotein B], as probes to examine several aspects of the regulation of these genes by estradiol [3].
  • Comparison of the rates of movement of triacyl[3H]glycerol, apolipoprotein B, apolipoprotein II, and apolipoprotein A-I through the ER and Golgi and of their secretion in nascent VLDL suggests that assembly of triacyglycerol with apolipoproteins occurs in the Golgi [4].
  • Specific postendocytic proteolysis of apolipoprotein B in oocytes does not abolish receptor recognition [5].
  • The C to U editing of apolipoprotein B (apoB) mRNA converts a glutamine codon in apoB100 mRNA into a stop translation codon thereby generating apoB48 [6].
  • Mammalian small intestine secretes a truncated apolipoprotein B (apoB48) species as a result of tissue-specific post-transcriptional RNA editing [7].

Biological context of APOB

  • Regulation of chicken apolipoprotein B: cloning, tissue distribution, and estrogen induction of mRNA [8].
  • While all five of these genes, vitellogenins I, II, and III, very low density apolipoprotein II (apo VLDLII), and apolipoprotein B, respond to estrogen, individual controls are superimposed on their coordinate regulation with respect to the kinetics of induction, magnitude of response, and developmental expression [9].

Anatomical context of APOB


Associations of APOB with chemical compounds


Other interactions of APOB

  • Serum-free culture conditions have been established that allow expression of apolipoprotein B, very low density apolipoprotein II (apoVLDLII), serum albumin, and transferrin at levels detectable by Northern blot analysis [20].

Analytical, diagnostic and therapeutic context of APOB

  • In microalbuminuric patients, apolipoprotein B levels were lower after the chicken (113.5 +/- 36.0 mg/dl) and low-protein diets (103.5 +/- 40.1 mg/dl) than after the usual diet (134.3 +/- 30.7 mg/dl; P < 0.05) [21].
  • Plasma and egg yolk VLDL were isolated by ultracentrifugation and free epsilon-amino groups of lysines of apolipoprotein B (apo B), the protein constituent of VLDL that mediates binding to the 95-kDa oocyte membrane receptor, were biotinylated using D-biotin-N-hydroxysuccinimide ester [22].
  • Here, we demonstrate directly that the catalyst for the intraoocytic processing of both apolipoprotein B and vitellogenin is cathepsin D. The enzyme was purified from oocytic yolk, preovulatory follicle homogenates, and liver by affinity chromatography [23].


  1. Single marker and haplotype analysis of the chicken apolipoprotein B gene T123G and D9500D9- polymorphism reveals association with body growth and obesity. Zhang, S., Li, H., Shi, H. Poult. Sci. (2006) [Pubmed]
  2. Estrogen dependence of synthesis and secretion of apolipoprotein B-containing lipoproteins in the chicken hepatoma cell line, LMH-2A. Hermann, M., Seif, F., Schneider, W.J., Ivessa, N.E. J. Lipid Res. (1997) [Pubmed]
  3. Isolation of chicken vitellogenin I and III cDNAs and the developmental regulation of five estrogen-responsive genes in the embryonic liver. Evans, M.I., Silva, R., Burch, J.B. Genes Dev. (1988) [Pubmed]
  4. Possible role of the Golgi apparatus in the assembly of very low density lipoprotein. Bamberger, M.J., Lane, M.D. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  5. Specific postendocytic proteolysis of apolipoprotein B in oocytes does not abolish receptor recognition. Nimpf, J., Radosavljevic, M., Schneider, W.J. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  6. Secondary structure for the apolipoprotein B mRNA editing site. Au-binding proteins interact with a stem loop. Richardson, N., Navaratnam, N., Scott, J. J. Biol. Chem. (1998) [Pubmed]
  7. Complementation of apolipoprotein B mRNA editing by human liver accompanied by secretion of apolipoprotein B48. Giannoni, F., Bonen, D.K., Funahashi, T., Hadjiagapiou, C., Burant, C.F., Davidson, N.O. J. Biol. Chem. (1994) [Pubmed]
  8. Regulation of chicken apolipoprotein B: cloning, tissue distribution, and estrogen induction of mRNA. Kirchgessner, T.G., Heinzmann, C., Svenson, K.L., Gordon, D.A., Nicosia, M., Lebherz, H.G., Lusis, A.J., Williams, D.L. Gene (1987) [Pubmed]
  9. Functional analysis of regulatory regions upstream and in the first intron of the estrogen-responsive chicken very low density apolipoprotein II gene. Berkowitz, E.A., Evans, M.I. J. Biol. Chem. (1992) [Pubmed]
  10. Octanoate reduces very low-density lipoprotein secretion by decreasing the synthesis of apolipoprotein B in primary cultures of chicken hepatocytes. Tachibana, S., Sato, K., Cho, Y., Chiba, T., Schneider, W.J., Akiba, Y. Biochim. Biophys. Acta (2005) [Pubmed]
  11. Evolution of intestinal apolipoprotein B mRNA editing. Chicken apolipoprotein B mRNA is not edited, but chicken enterocytes contain in vitro editing enhancement factor(s). Teng, B., Davidson, N.O. J. Biol. Chem. (1992) [Pubmed]
  12. Chicken oocytes and fibroblasts express different apolipoproteins-B-specific receptors. Hayashi, K., Nimpf, J., Schneider, W.J. J. Biol. Chem. (1989) [Pubmed]
  13. Interaction of apolipoprotein B from human serum low-density lipoprotein with egg yolk phosphatidylcholine and cholesterol. Dhawan, S., Reynolds, J.A. Biochemistry (1983) [Pubmed]
  14. Receptor-mediated lipoprotein transport in laying hens. Nimpf, J., Schneider, W.J. J. Nutr. (1991) [Pubmed]
  15. Sequential assembly of very low density lipoprotein apolipoproteins, triacylglycerol, and phosphoglycerides by the intact liver cell. Janero, D.R., Lane, M.D. J. Biol. Chem. (1983) [Pubmed]
  16. C-->U editing of apolipoprotein B mRNA in marsupials: identification and characterisation of APOBEC-1 from the American opossum Monodelphus domestica. Fujino, T., Navaratnam, N., Jarmuz, A., von Haeseler, A., Scott, J. Nucleic Acids Res. (1999) [Pubmed]
  17. Apolipoprotein specificity of the chicken oocyte receptor for low and very low density lipoproteins: lack of recognition of apolipoprotein VLDL-II. Nimpf, J., George, R., Schneider, W.J. J. Lipid Res. (1988) [Pubmed]
  18. Transcriptional regulation of human microsomal triglyceride transfer protein by hepatocyte nuclear factor-4alpha. Sheena, V., Hertz, R., Nousbeck, J., Berman, I., Magenheim, J., Bar-Tana, J. J. Lipid Res. (2005) [Pubmed]
  19. Synthesis, processing, and secretion of hepatic very low density lipoprotein. Janero, D.R., Siuta-Mangano, P., Miller, K.W., Lane, M.D. J. Cell. Biochem. (1984) [Pubmed]
  20. Estrogen-dependent expression of the chicken very low density apolipoprotein II gene in serum-free cultures of LMH cells. Berkowitz, E.A., Evans, M.I. In Vitro Cell. Dev. Biol. (1992) [Pubmed]
  21. Effect of a chicken-based diet on renal function and lipid profile in patients with type 2 diabetes: a randomized crossover trial. Gross, J.L., Zelmanovitz, T., Moulin, C.C., De Mello, V., Perassolo, M., Leitão, C., Hoefel, A., Paggi, A., Azevedo, M.J. Diabetes Care (2002) [Pubmed]
  22. Visualization of the chicken oocyte lipoprotein receptor by ligand blotting with biotinylated plasma and yolk very low density lipoproteins. Elkin, R.G., Schneider, W.J. Poult. Sci. (1994) [Pubmed]
  23. Molecular cloning and functional characterization of chicken cathepsin D, a key enzyme for yolk formation. Retzek, H., Steyrer, E., Sanders, E.J., Nimpf, J., Schneider, W.J. DNA Cell Biol. (1992) [Pubmed]
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