The multifunctional glycolytic protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a novel macrophage lactoferrin receptor

Biochemistry and Cell Biology

Volumn 90, Issue 3, 2012, Pages 329-338

  Rawat, Pooja ^a   Kumar, Santosh ^a   Sheokand, Navdeep ^a   Raje, Chaaya Iyengar ^b   Raje, Manoj ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

^b NATIONAL INSTITUTE OF PHARMACEUTICAL EDUCATION AND RESEARCH NIPER   (India)

Author keywords

GAPDH; Lactoferrin; Macrophage; Receptor

Indexed keywords

CELL TYPES; CO-IMMUNOPRECIPITATIONS; ENDOSOMAL COMPARTMENTS; EXPRESSION LEVELS; GAPDH; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; INTESTINAL CELLS; IRON DEPLETION; LACTOFERRIN; LIPOPROTEIN RECEPTOR-RELATED PROTEINS; MACROPHAGE CELLS; MOONLIGHTING PROTEINS; RECEPTOR;

CELL MEMBRANES; ELECTRON MICROSCOPY; PROTEINS;

MACROPHAGES;

ASIALOGLYCOPROTEIN RECEPTOR; CD14 ANTIGEN; CELL SURFACE RECEPTOR; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; INTELECTIN; IRON; LACTOFERRIN; LOW DENSITY LIPOPROTEIN RECEPTOR RELATED PROTEIN; PROTEIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL SURFACE; COMPLEX FORMATION; CONFOCAL MICROSCOPY; CONTROLLED STUDY; ENDOSOME; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE TEST; IMMUNOGOLD ELECTRON MICROSCOPY; IMMUNOPRECIPITATION; INTERNALIZATION; ISOTHERMAL TITRATION CALORIMETRY; MACROPHAGE; MOUSE; NONHUMAN; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; WESTERN BLOTTING;

ANIMALS; ANTIGENS, CD14; CALORIMETRY; CHO CELLS; CRICETINAE; ENDOSOMES; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES; HUMANS; IMMUNOPRECIPITATION; IRON; LACTOFERRIN; LDL-RECEPTOR RELATED PROTEINS; MACROPHAGES; MICE; PROTEIN BINDING; PROTEIN TRANSPORT; RECEPTORS, CELL SURFACE;

EID: 84861386961     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/o11-058     Document Type: Article

References (42)

1. Adlerova L. Bartoskova A. Faldyna M. 2008. Lactoferrin: a review. Vet. Med. (Praha), 53 (9): 457-468.
2. Artym J. 2006. Antitumor and chemopreventive activity of lactoferrin. Postepy Hig. Med. Dosw. (Online), 60: 352-369. 16885906
3. Ashida K. Sasaki H. Suzuki Y.A. Lönnerdal B. 2004. Cellular internalization of lactoferrin in intestinal epithelial cells. Biometals, 17 (3): 311-315. 10.1023/B:BIOM.0000027710.13543.3f 15222483
4. Baveye S. Elass E. Fernig D.G. Blanquart C. Mazurier J. Legrand D. 2000. Human lactoferrin interacts with soluble CD14 and inhibits expression of endothelial adhesion molecules, E-selectin and ICAM-1, induced by the CD14-lipopolysaccharide complex. Infect. Immun. 68 (12): 6519-6525. 10.1128/IAI.68.12.6519-6525.2000 11083760
5. Bennatt D.J. McAbee D.D. 1997. Identification and isolation of a 45-kDa calcium-dependent lactoferrin receptor from rat hepatocytes. Biochemistry, 36 (27): 8359-8366. 10.1021/bi963078u 9204883
6. Bennatt D.J. Ling Y.Y. McAbee D.D. 1997. Isolated rat hepatocytes bind lactoferrins by the RHL-1 subunit of the asialoglycoprotein receptor in a galactose-independent manner. Biochemistry, 36 (27): 8367-8376. 10.1021/bi963079m 9204884
7. Bi B.Y. Lefebvre A.M. Duś D. Spik G. Mazurier J. 1997. Effect of lactoferrin on proliferation and differentiation of the Jurkat human lymphoblastic T cell line. Arch. Immunol. Ther. Exp. (Warsz.), 45 (4): 315-320. 9523007
8. Bianchi L. Tacchini L. Cairo G. 1999. HIF-1-mediated activation of transferrin receptor gene transcription by iron chelation. Nucleic Acids Res. 27 (21): 4223-4227. 10.1093/nar/27.21.4223 10518614
9. Birgens H.S. 1991. The interaction of lactoferrin with human monocytes. Dan. Med. Bull. 38 (3): 244-252. 1651217
10. Birgens H.S. 1994. The monocytic receptor for lactoferrin and its involvement in lactoferrin-mediated iron transport. Adv. Exp. Med. Biol. 357: 99-109. 10.1007/978-1-4615-2548-6-10 7762450
11. Birgens H.S. Kristensen L.O. 1990. Impaired receptor binding and decrease in isoelectric point of lactoferrin after interaction with human monocytes. Eur. J. Haematol. 45 (1): 31-35. 10.1111/j.1600-0609.1990.tb00411.x 2165916
12. Britigan B.E. Serody J.S. Hayek M.B. Charniga L.M. Cohen M.S. 1991. Uptake of lactoferrin by mononuclear phagocytes inhibits their ability to form hydroxyl radical and protects them from membrane autoperoxidation. J. Immunol. 147 (12): 4271-4277. 1661314
13. Brock J.H. Mulero V. 2000. Cellular and molecular aspects of iron and immune function. Proc. Nutr. Soc. 59 (4): 537-540. 10.1017/S002966510000077X 11115788
14. Cleves A.E. Cooper D.N. Barondes S.H. Kelly R.B. 1996. A new pathway for protein export in Saccharomyces cerevisiae. J. Cell Biol. 133 (5): 1017-1026. 10.1083/jcb.133.5.1017 8655575
15. Conneely O.M. 2001. Antiinflammatory activities of lactoferrin. J. Am. Coll. Nutr. 20 (5 Suppl.): 389S-395S, discussion 396S-397S. 11603648
16. Grey A. Banovic T. Zhu Q. Watson M. Callon K. Palmano K. et al. 2004. The low-density lipoprotein receptor-related protein 1 is a mitogenic receptor for lactoferrin in osteoblastic cells. Mol. Endocrinol. 18 (9): 2268-2278. 10.1210/me.2003-0456 15178744
17. He J. Furmanski P. 1995. Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature, 373 (6516): 721-724. 10.1038/373721a0 7854459
18. Hudson, L., and Hay, F.C. 1989. Practical Immunology. 3rd ed. Blackwell Scientific Publications, Oxford London, Edinburgh Boston Melbourne.
19. Iancu T.C. 2011. Ultrastructural aspects of iron storage, transport and metabolism. J. Neural Transm. 118 (3): 329-335. 10.1007/s00702-011-0588-7 21318635
20. Ismail M. Brock J.H. 1993. Binding of lactoferrin and transferrin to the human promonocytic cell line U937. Effect on iron uptake and release. J. Biol. Chem. 268 (29): 21618-21625. 8408013
21. Kawakami H. Lönnerdal B. 1991. Isolation and function of a receptor for human lactoferrin in human fetal intestinal brush-border membranes. Am. J. Physiol. 261 (5): G841-G846. 1659221
22. Kenworthy A.K. 2001. Imaging Protein-Protein interactions Using fluorescence resonance energy transfer microscopy. Methods, 24 (3): 289-296. 10.1006/meth.2001.1189 11403577
23. Lönnerdal B. Iyer S. 1995. Lactoferrin: molecular structure and biological function. Annu. Rev. Nutr. 15 (1): 93-110. 10.1146/annurev.nu.15. 070195.000521 8527233
24. McGraw T.E. Greenfield L. Maxfield F.R. 1987. Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor. J. Cell Biol. 105 (1): 207-214. 10.1083/jcb.105.1.207 3611186
25. Modun B. Williams P. 1999. The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. Infect. Immun. 67 (3): 1086-1092. 10024547
26. Mulero V. Brock J.H. 1999. Regulation of iron metabolism in murine J774 macrophages: role of nitric oxide-dependent and-independent pathways following activation with gamma interferon and lipopolysaccharide. Blood, 94 (7): 2383-2389. 10498610
27. Nombela C. Gil C. Chaffin W.L. 2006. Non-conventional protein secretion in yeast. Trends Microbiol. 14 (1): 15-21. 10.1016/j.tim.2005.11.009 16356720
28. Raje C.I. Kumar S. Harle A. Nanda J.S. Raje M. 2007. The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor. J. Biol. Chem. 282 (5): 3252-3261. 10.1074/jbc.M608328200 17121833
29. Roiron D. Amouric M. Marvaldi J. Figarella C. 1989. Lactoferrin-binding sites at the surface of HT29-D4 cells. Comparison with transferrin. Eur. J. Biochem. 186 (1-2): 367-373. 10.1111/j.1432-1033.1989.tb15218.x 2557211
30. Shimazaki, K.I., Kushida, T., and Takase, M. 2007. Lactoferrin binding protein detected in bifidobacteria is GAPDH: A hypothesis of growth promotion of bifidobacteria by lactoferrin using the text mining approach. In Proceedings of the Xth International Conference on Lactoferrin: Structure, Function and Applications, 8-12 May 2011.
31. Suzuki Y.A. Shin K. Lönnerdal B. 2001. Molecular cloning and functional expression of a human intestinal lactoferrin receptor. Biochemistry, 40 (51): 15771-15779. 10.1021/bi0155899 11747454
32. Takayama Y. Takahashi H. Mizumachi K. Takezawa T. 2003. Low density lipoprotein receptor-related protein (LRP) is required for lactoferrin-enhanced collagen gel contractile activity of human fibroblasts. J. Biol. Chem. 278 (24): 22112-22118. 10.1074/jbc.M300894200 12672816
33. Tanaka T. Abe Y. Kim W.S. Xuan X. Nagasawa H. Igarashi I. et al. 2003. The detection of bovine lactoferrin binding protein on Toxoplasma gondii. J. Vet. Med. Sci. 65 (12): 1377-1380. 10.1292/jvms.65.1377 14709832
34. Tanaka T. Abe Y. Inoue N. Kim W.S. Kumura H. Nagasawa H. et al. 2004 a. The detection of bovine lactoferrin binding protein on Trypanosoma brucei. J. Vet. Med. Sci. 66 (6): 619-625. 10.1292/jvms.66.619 15240935
35. Tanaka T. Morita H. Yoo Y.C. Kim W.S. Kumura H. Shimazaki K. 2004 b. Detection of bovine lactoferrin binding protein on Jurkat human lymphoblastic T cell line. J. Vet. Med. Sci. 66 (7): 865-869. 10.1292/jvms.66.865 15297761
36. Tisdale E.J. Kelly C. Artalejo C.R. 2004. Glyceraldehyde-3-phosphate dehydrogenase interacts with Rab2 and plays an essential role in endoplasmic reticulum to Golgi transport exclusive of its glycolytic activity. J. Biol. Chem. 279 (52): 54046-54052. 10.1074/jbc.M409472200 15485821
37. Tristan C. Shahani N. Sedlak T.W. Sawa A. 2011. The diverse functions of GAPDH: views from different subcellular compartments. Cell. Signal. 23 (2): 317-323. 10.1016/j.cellsig.2010.08.003 20727968
38. Van Snick J.L. Masson P.L. 1976. The binding of human lactoferrin to mouse peritoneal cells. J. Exp. Med. 144 (6): 1568-1580. 10.1084/jem.144.6.1568 1003104
39. Wally J. Buchanan S.K. 2007. A structural comparison of human serum transferrin and human lactoferrin. Biometals, 20 (3-4): 249-262. 10.1007/s10534-006-9062-7 17216400
40. Ward P.P. Conneely O.M. 2004. Lactoferrin: role in iron homeostasis and host defense against microbial infection. Biometals, 17 (3): 203-208. 10.1023/B:BIOM.0000027693.60932.26 15222466
41. Yamaji R. Chatani E. Harada N. Sugimoto K. Inui H. Nakano Y. 2005. Glyceraldehyde-3-phosphate dehydrogenase in the extracellular space inhibits cell spreading. Biochim. Biophys. Acta, 1726 (3): 261-271.
42. Ziere G.J. van Dijk M.C. Bijsterbosch M.K. van Berkel T.J. 1992. Lactoferrin uptake by the rat liver. Characterization of the recognition site and effect of selective modification of arginine residues. J. Biol. Chem. 267 (16): 11229-11235. 1597458