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Gene Review

Cd320  -  CD320 antigen

Mus musculus

Synonyms: 425O18-1, 8D6, CD320-002, D17Ertd716e, NG29, ...
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Disease relevance of Cd320


High impact information on Cd320

  • However, unlike SREBP itself, PGC-1beta reduces fat accumulation in the liver while greatly increasing circulating triglycerides and cholesterol in VLDL particles [6].
  • Remnants of lipoproteins, intestinal chylomicrons, and very low density lipoprotein (VLDL), are rapidly cleared from plasma and enter hepatocytes [7].
  • Triglyceride and apoB production rates were normal, as were plasma lipase activity, VLDL glycosaminoglycan binding, and VLDL lipolysis [8].
  • It is not clear, for instance, whether MTP is required to move the bulk of triglycerides into the lumen of the endoplasmic reticulum (ER) during the assembly of VLDL particles [9].
  • Using S-sphingomyelinase, an enzyme secreted by macrophages and endothelial cells, we found that VLDL and LDL from apoE0, but not from Wt or LDLr0 mice, were significantly aggregated, and that aggregation was not prevented by adding back apoE [10].

Chemical compound and disease context of Cd320


Biological context of Cd320

  • Lipolysis of isolated lipoprotein fractions (either HTG or normal) allowed localization of cytotoxicity to postlipolysis remnant VLDL and chylomicron particles [15].
  • In summary, it appears that liver LPL shunts circulating triglycerides to the liver, which results in a futile cycle of enhanced VLDL production and increased ketone production, and subsequently spares glucose [16].
  • Thus, our data reveal a pathway through which dietary triglycerides and VLDL can directly regulate gene expression in atherosclerotic lesions [11].
  • This unique transcriptional mechanism assures a tight control of the homeostasis of VLDL-derived fatty acid and provides a therapeutic target for other lipid-related disorders, including dyslipidemia and diabetes, in addition to coronary artery disease [17].
  • Especially in zinc-treated homozygotes, VLDL had almost disappeared, and a remarkable decrease in LDL and a slight decrease in high density lipoprotein were also observed [18].

Anatomical context of Cd320

  • Both formulas induced the formation of d less than 1.006 lipoproteins that were approximately 3.5-fold more active than fasting very low density lipoproteins (VLDL) in binding to the receptor for beta-VLDL on macrophages [3].
  • When incubated with mouse peritoneal macrophages, the VLDL from WHHL rabbit (WHHL-VLDL) stimulated cholesteryl [14C]oleate synthesis 124-fold more than did VLDL from the normal Japanese White rabbit (control-VLDL) [19].
  • To eliminate the possibility that impaired VLDL secretion is caused by aspecific changes in hepatic function due to hypercholesterolemia, VLDL-TG production rates were also measured in apo E-deficient mice after transplantation of wild-type mouse bone marrow [20].
  • Its high level expression in muscle and adipose tissue suggests a role in VLDL triacylglycerol delivery [21].
  • We have previously demonstrated peroxisome proliferator-activated receptor (PPAR)delta, but not PPARgamma, is the major nuclear VLDL sensor in the macrophage, which is a crucial component of the atherosclerotic lesion [17].

Associations of Cd320 with chemical compounds

  • The decrease in serum triglycerides in aP2/DTA mice was due to a marked reduction in VLDL- and LDL-associated triglyceride [22].
  • Additional in vivo studies with Triton-treated mice showed increased VLDL triglyceride, but not apo B, production in the HuCIIITg mice compared with controls [23].
  • The phosphatidylcholine/sphingomyelin (PC/SM) ratio was reduced in all lipoproteins in apoE0 mice compared with wild-type (Wt) mice (2.0+/-0.2 vs. 4.7+/-0.5; 2.8+/-0.5 vs. 5.5+/-0.9; 1.9+/-0. 5 vs. 4.6+/-0.5 for VLDL, LDL, and HDL), reflecting 400 and 179% increases in plasma pools of SM and PC, respectively [10].
  • Electron microscopic evaluation revealed a smaller average size for VLDL particles produced by apo E-deficient cells compared with control cells in the presence of oleate (38 and 49 nm, respectively) [20].
  • However, elevated amounts of vitamin E were subsequently observed in the VLDL of the HuAIVTg mice [24].

Physical interactions of Cd320

  • Addition of LPL resulted in a significant increase in apoER2 binding for all VLDL fractions used in this study [25].

Other interactions of Cd320

  • In conclusion, lipoprotein binding of VLDL to the apoER2 is enhanced in the presence of LPL, and is not restricted to apoE-containing lipoproteins [25].

Analytical, diagnostic and therapeutic context of Cd320

  • Chromatography on a Sephadex G-200 column, prior to or following ultracentrifugation, resulted in the isolation of very low-density lipoprotein (VLDL) and low-density lipoprotein (LDL) that prevented tumor cell destruction by M phi [26].
  • The results suggest that the presence of unusual VLDL particles in diabetic cholesterol-fed rabbits is responsible, at least in part, for the reduced incidence of atherosclerosis in this animal model [27].
  • Under electron microscopy, VLDL particles from low and high expressor mice were found to have a larger mean diameter, 55.2 +/- 16.6 and 58.2 +/- 17.8 nm, respectively, compared with 51.0 +/- 13.4 nm from control mice [23].
  • Subfractionation of postprandial d less than 1.006 lipoproteins by agarose chromatography yielded two subfractions, fraction I (chylomicron remnants) and fraction II (hepatic VLDL remnants), which bound to receptors on macrophages [3].
  • Gel filtration chromatography showed that lipid reduction was mainly due to decreased very low density lipoproteins (VLDL) and LDL [18].


  1. A mouse model with features of familial combined hyperlipidemia. Masucci-Magoulas, L., Goldberg, I.J., Bisgaier, C.L., Serajuddin, H., Francone, O.L., Breslow, J.L., Tall, A.R. Science (1997) [Pubmed]
  2. Bile acids lower triglyceride levels via a pathway involving FXR, SHP, and SREBP-1c. Watanabe, M., Houten, S.M., Wang, L., Moschetta, A., Mangelsdorf, D.J., Heyman, R.A., Moore, D.D., Auwerx, J. J. Clin. Invest. (2004) [Pubmed]
  3. Fat feeding in humans induces lipoproteins of density less than 1.006 that are enriched in apolipoprotein [a] and that cause lipid accumulation in macrophages. Bersot, T.P., Innerarity, T.L., Pitas, R.E., Rall, S.C., Weisgraber, K.H., Mahley, R.W. J. Clin. Invest. (1986) [Pubmed]
  4. Diet-induced hyperlipoproteinemia and atherosclerosis in apolipoprotein E3-Leiden transgenic mice. van Vlijmen, B.J., van den Maagdenberg, A.M., Gijbels, M.J., van der Boom, H., HogenEsch, H., Frants, R.R., Hofker, M.H., Havekes, L.M. J. Clin. Invest. (1994) [Pubmed]
  5. Apolipoprotein E deficiency in mice: gene replacement and prevention of atherosclerosis using adenovirus vectors. Kashyap, V.S., Santamarina-Fojo, S., Brown, D.R., Parrott, C.L., Applebaum-Bowden, D., Meyn, S., Talley, G., Paigen, B., Maeda, N., Brewer, H.B. J. Clin. Invest. (1995) [Pubmed]
  6. Hyperlipidemic effects of dietary saturated fats mediated through PGC-1beta coactivation of SREBP. Lin, J., Yang, R., Tarr, P.T., Wu, P.H., Handschin, C., Li, S., Yang, W., Pei, L., Uldry, M., Tontonoz, P., Newgard, C.B., Spiegelman, B.M. Cell (2005) [Pubmed]
  7. Remnant lipoproteins inhibit malaria sporozoite invasion of hepatocytes. Sinnis, P., Willnow, T.E., Briones, M.R., Herz, J., Nussenzweig, V. J. Exp. Med. (1996) [Pubmed]
  8. Delayed catabolism of apoB-48 lipoproteins due to decreased heparan sulfate proteoglycan production in diabetic mice. Ebara, T., Conde, K., Kako, Y., Liu, Y., Xu, Y., Ramakrishnan, R., Goldberg, I.J., Shachter, N.S. J. Clin. Invest. (2000) [Pubmed]
  9. Analysis of the role of microsomal triglyceride transfer protein in the liver of tissue-specific knockout mice. Raabe, M., Véniant, M.M., Sullivan, M.A., Zlot, C.H., Björkegren, J., Nielsen, L.B., Wong, J.S., Hamilton, R.L., Young, S.G. J. Clin. Invest. (1999) [Pubmed]
  10. Increased sphingomyelin content of plasma lipoproteins in apolipoprotein E knockout mice reflects combined production and catabolic defects and enhances reactivity with mammalian sphingomyelinase. Jeong, T.s., Schissel, S.L., Tabas, I., Pownall, H.J., Tall, A.R., Jiang, X. J. Clin. Invest. (1998) [Pubmed]
  11. PPARdelta is a very low-density lipoprotein sensor in macrophages. Chawla, A., Lee, C.H., Barak, Y., He, W., Rosenfeld, J., Liao, D., Han, J., Kang, H., Evans, R.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  12. Transgenic mice expressing human lipoprotein lipase driven by the mouse metallothionein promoter. A phenotype associated with increased perinatal mortality and reduced plasma very low density lipoprotein of normal size. Zsigmond, E., Scheffler, E., Forte, T.M., Potenz, R., Wu, W., Chan, L. J. Biol. Chem. (1994) [Pubmed]
  13. An immunosuppressive lipoprotein fraction from TEPC-183 bearing mice. Wolfe, L., Havas, H.F., Fenton, M.R. Clin. Exp. Immunol. (1983) [Pubmed]
  14. Pathway of biogenesis of apolipoprotein E-containing HDL in vivo with the participation of ABCA1 and LCAT. Kypreos, K.E., Zannis, V.I. Biochem. J. (2007) [Pubmed]
  15. Lipolytic surface remnants of triglyceride-rich lipoproteins are cytotoxic to macrophages but not in the presence of high density lipoprotein. A possible mechanism of atherogenesis? Chung, B.H., Segrest, J.P., Smith, K., Griffin, F.M., Brouillette, C.G. J. Clin. Invest. (1989) [Pubmed]
  16. Lipoprotein lipase expression exclusively in liver. A mouse model for metabolism in the neonatal period and during cachexia. Merkel, M., Weinstock, P.H., Chajek-Shaul, T., Radner, H., Yin, B., Breslow, J.L., Goldberg, I.J. J. Clin. Invest. (1998) [Pubmed]
  17. Peroxisome proliferator-activated receptor delta promotes very low-density lipoprotein-derived fatty acid catabolism in the macrophage. Lee, C.H., Kang, K., Mehl, I.R., Nofsinger, R., Alaynick, W.A., Chong, L.W., Rosenfeld, J.M., Evans, R.M. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  18. Overexpression of apolipoprotein E in transgenic mice: marked reduction in plasma lipoproteins except high density lipoprotein and resistance against diet-induced hypercholesterolemia. Shimano, H., Yamada, N., Katsuki, M., Shimada, M., Gotoda, T., Harada, K., Murase, T., Fukazawa, C., Takaku, F., Yazaki, Y. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  19. Stimulation of cholesteryl ester synthesis in mouse peritoneal macrophages by cholesterol-rich very low density lipoproteins from the Watanabe heritable hyperlipidemic rabbit, an animal model of familial hypercholesterolemia. Kita, T., Yokode, M., Watanabe, Y., Narumiya, S., Kawai, C. J. Clin. Invest. (1986) [Pubmed]
  20. Impaired secretion of very low density lipoprotein-triglycerides by apolipoprotein E- deficient mouse hepatocytes. Kuipers, F., Jong, M.C., Lin, Y., Eck, M., Havinga, R., Bloks, V., Verkade, H.J., Hofker, M.H., Moshage, H., Berkel, T.J., Vonk, R.J., Havekes, L.M. J. Clin. Invest. (1997) [Pubmed]
  21. Normal plasma lipoproteins and fertility in gene-targeted mice homozygous for a disruption in the gene encoding very low density lipoprotein receptor. Frykman, P.K., Brown, M.S., Yamamoto, T., Goldstein, J.L., Herz, J. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  22. Troglitazone action is independent of adipose tissue. Burant, C.F., Sreenan, S., Hirano, K., Tai, T.A., Lohmiller, J., Lukens, J., Davidson, N.O., Ross, S., Graves, R.A. J. Clin. Invest. (1997) [Pubmed]
  23. Mechanism of hypertriglyceridemia in human apolipoprotein (apo) CIII transgenic mice. Diminished very low density lipoprotein fractional catabolic rate associated with increased apo CIII and reduced apo E on the particles. Aalto-Setälä, K., Fisher, E.A., Chen, X., Chajek-Shaul, T., Hayek, T., Zechner, R., Walsh, A., Ramakrishnan, R., Ginsberg, H.N., Breslow, J.L. J. Clin. Invest. (1992) [Pubmed]
  24. Intestinal expression of human apolipoprotein A-IV in transgenic mice fails to influence dietary lipid absorption or feeding behavior. Aalto-Setälä, K., Bisgaier, C.L., Ho, A., Kieft, K.A., Traber, M.G., Kayden, H.J., Ramakrishnan, R., Walsh, A., Essenburg, A.D., Breslow, J.L. J. Clin. Invest. (1994) [Pubmed]
  25. Very-low-density lipoprotein binding to the apolipoprotein E receptor 2 is enhanced by lipoprotein lipase, and does not require apolipoprotein E. Tacken, P.J., Beer, F.D., Vark, L.C., Havekes, L.M., Hofker, M.H., Willems Van Dijk K, n.u.l.l. Biochem. J. (2000) [Pubmed]
  26. Inhibition of macrophage-mediated tumor cell destruction by oxidized lipoproteins. Justement, L.B., Patel, S.T., Newman, H.A., Zwilling, B.S. J. Natl. Cancer Inst. (1984) [Pubmed]
  27. Relationship of an abnormal plasma lipoprotein to protection from atherosclerosis in the cholesterol-fed diabetic rabbit. Brecher, P., Chobanian, A.V., Small, D.M., Van Sickle, W., Tercyak, A., Lazzari, A., Baler, J. J. Clin. Invest. (1983) [Pubmed]
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