A1M/α1-microglobulin is proteolytically activated by myeloperoxidase, binds its heme group and inhibits low density lipoprotein oxidation

Frontiers in Physiology

Volumn 6, Issue FEB, 2015, Pages

  Cederlund, Martin ^a   Deronic, Adnan ^b   Pallon, Jan ^a   Sørensen, Ole E ^a   Åkerström, Bo ^a  

^a LUND UNIVERSITY   (Sweden)

^b LUND UNIVERSITY   (Sweden)

Author keywords

C terminal proteolysis; Heme binding; Low density lipoprotein; Myeloperoxidase; Neutrophils; 1 microglobulin

Indexed keywords

ALPHA 1 MICROGLOBULIN; HEME; LOW DENSITY LIPOPROTEIN; MYELOPEROXIDASE;

ARTICLE; BINDING AFFINITY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME REGULATION; HUMAN; HUMAN CELL; NONHUMAN; NORMAL HUMAN; PH; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN FUNCTION; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION; TIME;

EID: 84926453297     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2015.00011     Document Type: Article

References (43)

1. Åkerström, B., and Gram, M. (2014). A1M, an extravascular tissue cleaning and housekeeping protein. Free Radic. Biol. Med . 74, 274-282. doi: 10.1016/j.freeradbiomed.2014.06.025
2. 1-microglobulin has radical-scavenger activity. J. Biol. Chem . 282, 31493-31503. doi: 10.1074/jbc.M702624200
3. 1-microglobulin by hemoglobin induces heme-binding and heme-degradation properties. Blood 99, 1894-1901. doi: 10.1182/blood.V99.6.1894
4. 1-microglobulin: reduction of cytochrome c , hemoglobin, and free iron. Free Radic. Biol. Med . 38, 557-567. doi: 10.1016/j.freeradbiomed.2004.12.013
5. 1-microglobulin in chronic ulcers. J. Invest. Dermatol . 121, 640-646. doi: 10.1046/j.1523-1747.2003.12409.x
6. 2-globulin occurring in human biological fluids. J. Biol. Chem . 243, 4095-4103.
7. 1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound. Protein. Sci . 8, 2611-2620. doi: 10.1110/ps.8.12.2611
8. 1-microglobulin in human plasma. Eur. J. Biochem . 245, 676-683. doi: 10.1111/j.1432-1033.1997.00676.x
9. 2-microglobulin and alloantigens coded for by the major histocompatibility complexes of the rabbit and the guinea pig. Scand. J. Immunol . 6, 1063-1069. doi: 10.1111/j.1365-3083.1977.tb00342.x
10. Calero, M., Escribano, J., Soriano, F., Grubb, A., Brew, K., and Mendez, E. (1996). Spectroscopic characterization by photodiode array detection of human urinary and amniotic protein HC subpopulations fractionated by anion-exchange and size-exclusion high performance liquid chromatography. J. Chromatogr. A 719, 149-157. doi: 10.1016/0021-9673(95)00100-X
11. Daugherty, A., Dunn, J. L., Rateri, D. L., and Heinecke, J. W. (1994). Myeloperoxidase, a catalyst for lipoprotein oxidation, is expressed in human atherosclerotic lesions. J. Clin. Invest . 94, 437-444. doi: 10.1172/JCI117342
12. 1-microglobulin by a combined immunoenzyme/immunoradiometric assay technique. Clin. Chem . 35, 766-772.
13. Ekström, B., Peterson, P. A., and Berggård, I. (1975). A urinary and plasma α1-glycoprotein of low molecular weight: isolation and some properties. Biochem. Biophys. Res. Commun . 65, 1427-1433. doi: 10.1016/S0006-291X(75)80388-3
14. Elfman, M., Kristiansson, P., Malmqvist, K., Pallon, J., Sjöland, A., Utui, R., et al. (1997). New CAMAC based data acquisition and beam control system for Lund nuclear microprobe. Nucl. Instr. Methods B 130, 123-126. doi: 10.1016/S0168-583X(97)00271-1
15. Farschou, M., and Borregaard, N. (2003). Neutrophil granules and secretory vesicles in inflammation. Microbes Infect . 5, 1317-1327. doi: 10.1016/j.micinf.2003.09.008
16. Fiedler, T. J., Davey, C. A., and Fenna, R. E. (2000). X-ray Crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 Å resolution. J. Biol. Chem . 275, 11964-11971. doi: 10.1074/jbc.275.16.11964
17. Flower, D. R. (1996). The lipocalin protein family: structure and function. Biochem. J . 318(Pt 1), 1-14.
18. Girotti, A. W., and Thomas, J. P. (1984). Damaging effects of oxygen radicals on resealed erythrocyte ghosts. J. Biol. Chem . 259, 1744-1752.
19. 131I-labelled human growth hormone. Biochem. J . 89, 114-123.
20. Gutteridge, J. M. (1977). The measurement of malondialdehyde in peroxidised ox-brain phospholipid liposomes. Anal. Biochem . 82, 76-82. doi: 10.1016/0003-2697(77)90136-1
21. Johansson, S. A. E., and Campbell, J. L. (1988). PIXE: A Novel Technique for Elemental Analysis . New York, NY: Wiley.
22. Karnaukhova, E., Rutardottir, S., Rajabi, M., Wester Rosenlöf, L., Alayash, A. I., and Åkerström, B. (2014). Characterization of heme binding to α1-microglobulin. Front. Physiol . 5:465. doi: 10.3389/fphys.2014.00465
23. Klebanoff, S. J. (2005). Myeloperoxidase: friend and foe. J. Leukoc. Biol . 77, 598-625. doi: 10.1189/jlb.1204697
24. Kumar, S., and Bandyopadhyay, U. (2005). Free heme toxicity and its detoxification systems in human. Toxicol. Lett . 157, 175-188. doi: 10.1016/j.toxlet.2005.03.004
25. 1-microglobulin and mutant forms involved in chromophore formation. Protein. Expr. Purif . 53, 145-152. doi: 10.1016/j.pep.2006.10.023
26. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685. doi: 10.1038/227680a0
27. 1-microglobulin binds heme in different species. Arch. Biochem. Biophys . 432, 196-204. doi: 10.1016/j.abb.2004.09.021
28. Lopez, C., Grubb, A., and Mendez, E. (1982). Human protein HC displays variability in its carboxyterminal amino acid sequence. FEBS Lett . 144, 349-353. doi: 10.1016/0014-5793(82)80670-4
29. Malle, E., Furtmüller, P. G., Sattler, W., and Obinger, C. (2007). Myeloperoxidase: a target for new drug development? Brit. J. Pharmacol . 152, 838-854. doi: 10.1038/sj.bjp.0707358
30. Malmqvist, K. G., Hyltén, G., Hult, M., Håkansson, K., Knox, J. M., Larsson, N. P.-O., et al. (1993). Dedicated accelerator and microprobe line. Nucl. Instr. Methods B 77, 3-7. doi: 10.1016/0168-583X(93)95514-6
31. Matsudaira, P. (1987). Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem . 262, 10035-10038.
32. 1-microglobulin. Placenta 32, 323-332. doi: 10.1016/j.placenta.2011.01.017
33. 1-microglobulin reveals a potential haem-binding site. Biochem. J . 445, 175-182. doi: 10.1042/BJ20120448
34. Nauseef, W. M., and Malech, H. L. (1986). Analysis of the peptide subunits of the human neutrophil myeloperoxidase. Blood 67, 1504-1507.
35. 1-microglobulin. Antioxid. Redox Signal . 17, 813-846. doi: 10.1089/ars.2011.4282
36. 1-microglobulin in skin by heme and reactive oxygen species gives protection from oxidative damage. PLoS ONE 6:e27505. doi: 10.1371/journal.pone.0027505
37. 1-microglobulin protects erythroid K562 cells against oxidative damage induced by heme and reactive oxygen species. Free Radic. Res . 42, 725-736. doi: 10.1080/10715760802337265
38. 1-microglobulin protects from heme-induced placental and renal damage in a pregnant sheep model of preeclampsia. PLoS ONE 9:e86353. doi: 10.1371/journal.pone.0086353
39. 1-microglobulin is essential for protection of irradiated cell cultures and reduction of carbonyl groups. Free Radic. Res . 47, 541-550. doi: 10.3109/10715762.2013.801555
40. 1-microglobulin is covalently bound to kynurenine-derived chromophores. J. Biol. Chem . 279, 51033-51041. doi: 10.1074/jbc.M408242200
41. 3complex. Chembiochem 13, 879-887. doi: 10.1002/cbic.201100808
42. 1-microglobulin (A1M) and Tempol. Am. J. Physiol. Renal Physiol . 306, F442-F448. doi: 10.1152/ajprenal.00502.2013
43. Winrow, V. R., Winyard, P. G., Morris, C. J., and Blake, D. R. (1993). Free radicals in inflammation: second messengers and mediators of tissue destruction. Br. Med. Bull . 49, 506-522.