Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1991 Oct 1;88(19):8539–8543. doi: 10.1073/pnas.88.19.8539

Vitamin D3 binding protein (group-specific component) is a precursor for the macrophage-activating signal factor from lysophosphatidylcholine-treated lymphocytes.

N Yamamoto 1, S Homma 1
PMCID: PMC52544  PMID: 1924312

Abstract

A brief (30 min) treatment of mouse peritoneal cells (mixture of nonadherent lymphocytes and adherent macrophages) with 1-20 micrograms of lysophosphatidylcholine (lyso-PC) per ml in serum-supplemented RPMI medium 1640, followed by a 3-hr cultivation of the adherent cells alone, results in a greatly enhanced Fc receptor-mediated phagocytic activity of macrophages. This rapid process of macrophage activation was found to require a serum factor, the vitamin D3 binding protein (the human protein is known as group-specific component; Gc). Efficient activation of macrophages was achieved by using medium containing purified human Gc protein. Analysis of intercellular signal transmission among nonadherent (B and T) cells revealed that lyso-PC-treated B cells modify Gc protein to yield a proactivating factor, which can be converted by T cells to the macrophage-activating factor. This rapid generation process of the macrophage-activating factor was also demonstrated by stepwise incubation of Gc protein with lyso-PC-treated B-cell ghosts and untreated T-cell ghosts, suggesting that Gc protein is modified by preexisting membranous enzymes to yield the macrophage-activating factor. Incubation of Gc protein with a mixture of beta-galactosidase and sialidase efficiently generated the macrophage-activating factor. Stepwise incubation of Gc protein with B- or T-cell ghosts and sialidase or beta-galactosidase revealed that Gc protein is modified by beta-galactosidase of B cells and sialidase of T cells to yield the macrophage-activating factor. Administration to mice of a minute amount (4-10 pg per mouse) of in vitro, enzymatically generated macrophage-activating factor resulted in a greatly enhanced (3- to 7-fold) ingestion activity of macrophages.

Full text

PDF
8539

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. AIDS and the Gc protein. Lancet. 1987 Jun 13;1(8546):1377–1378. [PubMed] [Google Scholar]
  2. Bianco C., Griffin F. M., Jr, Silverstein S. C. Studies of the macrophage complement receptor. Alteration of receptor function upon macrophage activation. J Exp Med. 1975 Jun 1;141(6):1278–1290. doi: 10.1084/jem.141.6.1278. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Coppenhaver D. H., Sollenne N. P., Bowman B. H. Post-translational heterogeneity of the human vitamin D-binding protein (group-specific component). Arch Biochem Biophys. 1983 Oct 1;226(1):218–223. doi: 10.1016/0003-9861(83)90287-4. [DOI] [PubMed] [Google Scholar]
  4. Homma S., Millman I., Yamamoto N. A serum factor for macrophage activation after in vitro dodecylglycerol treatment of mouse lymphocytes. Immunol Cell Biol. 1990 Apr;68(Pt 2):137–142. doi: 10.1038/icb.1990.19. [DOI] [PubMed] [Google Scholar]
  5. Homma S., Yamamoto N. Activation process of macrophages after in vitro treatment of mouse lymphocytes with dodecylglycerol. Clin Exp Immunol. 1990 Feb;79(2):307–313. doi: 10.1111/j.1365-2249.1990.tb05195.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Howard B. V., Morris H. P., Bailey J. M. Ether-lipids, -glycerol phosphate dehydrogenase, and growth rate in tumors and cultured cells. Cancer Res. 1972 Jul;32(7):1533–1538. [PubMed] [Google Scholar]
  7. Kimura H., Saheki S., Yoshida K., Ohsawa M. Characterization of purified group-specific components (Gc 1 and Gc 2 proteins) from human plasma. Nihon Hoigaku Zasshi. 1985 Apr;39(2):113–123. [PubMed] [Google Scholar]
  8. Landolfi N. F., Leone J., Womack J. E., Cook R. G. Activation of T lymphocytes results in an increase in H-2-encoded neuraminidase. Immunogenetics. 1985;22(2):159–167. doi: 10.1007/BF00563513. [DOI] [PubMed] [Google Scholar]
  9. Ngwenya B. Z., Yamamoto N. Activation of peritoneal macrophages by lysophosphatidylcholine. Biochim Biophys Acta. 1985 Mar 29;839(1):9–15. doi: 10.1016/0304-4165(85)90175-8. [DOI] [PubMed] [Google Scholar]
  10. Ngwenya B. Z., Yamamoto N. Contribution of lysophosphatidylcholine-treated nonadherent cells to mechanism of macrophage activation. Proc Soc Exp Biol Med. 1990 Feb;193(2):118–124. doi: 10.3181/00379727-193-43011. [DOI] [PubMed] [Google Scholar]
  11. Potier M., Lu Shun Yan D., Womack J. E. Neuraminidase deficiency in the mouse. FEBS Lett. 1979 Dec 15;108(2):345–348. doi: 10.1016/0014-5793(79)80560-8. [DOI] [PubMed] [Google Scholar]
  12. Snyder F., Wood R. Alkyl and alk-1-enyl ethers of glycerol in lipids from normal and neoplastic human tissues. Cancer Res. 1969 Jan;29(1):251–257. [PubMed] [Google Scholar]
  13. Svasti J., Bowman B. H. Human group-specific component. Changes in electrophoretic mobility resulting from vitamin D binding and from neuraminidase digestion. J Biol Chem. 1978 Jun 25;253(12):4188–4194. [PubMed] [Google Scholar]
  14. Taira S., Nariuchi H. Possible role of neuraminidase in activated T cells in the recognition of allogeneic Ia. J Immunol. 1988 Jul 15;141(2):440–446. [PubMed] [Google Scholar]
  15. Viau M., Constans J., Debray H., Montreuil J. Isolation and characterization of the O-glycan chain of the human vitamin-D binding protein. Biochem Biophys Res Commun. 1983 Nov 30;117(1):324–331. doi: 10.1016/0006-291x(83)91579-6. [DOI] [PubMed] [Google Scholar]
  16. Yamamoto N., Homma S., Millman I. Identification of the serum factor required for in vitro activation of macrophages. Role of vitamin D3-binding protein (group specific component, Gc) in lysophospholipid activation of mouse peritoneal macrophages. J Immunol. 1991 Jul 1;147(1):273–280. [PubMed] [Google Scholar]
  17. Yamamoto N., Ngwenya B. Z. Activation of mouse peritoneal macrophages by lysophospholipids and ether derivatives of neutral lipids and phospholipids. Cancer Res. 1987 Apr 15;47(8):2008–2013. [PubMed] [Google Scholar]
  18. Yamamoto N., Ngwenya B. Z., Sery T. W., Pieringer R. A. Activation of macrophages by ether analogues of lysophospholipids. Cancer Immunol Immunother. 1987;25(3):185–192. doi: 10.1007/BF00199146. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Yamamoto N., St Claire D. A., Jr, Homma S., Ngwenya B. Z. Activation of mouse macrophages by alkylglycerols, inflammation products of cancerous tissues. Cancer Res. 1988 Nov 1;48(21):6044–6049. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES