Stanniocalcin 1 binds hemin through a partially conserved heme regulatory motif

Biochemical and Biophysical Research Communications

Volumn 409, Issue 2, 2011, Pages 266-269

  Westberg, Johan A ^a   Jiang, Ji ^a   Andersson, Leif C ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Iron; Mitochondria; Oxidative stress; Porphyrin; Redox; STC1

Indexed keywords

CYSTEINE DERIVATIVE; HEME; HEMIN; HEMOPROTEIN; HYDROGEN PEROXIDE; HYPOCALCIN; IRON; PROTOPORPHYRIN; STANNIOCALCIN 1; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; ATOM; CATALYSIS; CONTROLLED STUDY; ELECTRON TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION;

AMINO ACID MOTIFS; ANIMALS; CERCOPITHECUS AETHIOPS; CONSERVED SEQUENCE; COS CELLS; GLYCOPROTEINS; HEMIN; HUMANS; MICE; POINT MUTATION; PROTEIN BINDING; RATS; RECOMBINANT PROTEINS;

EID: 79957924832     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.05.002     Document Type: Article

References (28)

1. Wagner G.F., Hampong M., Park C.M., Copp D.H. Purification, characterization, and bioassay of teleocalcin, a glycoprotein from salmon corpuscles of stannius. Gen. Comp. Endocrinol. 1986, 63:481-491.
2. Ellard J.P., McCudden C.R., Tanega C., James K.A., Ratkovic S., Staples J.F., Wagner G.F. The respiratory effects of stanniocalcin-1 (STC-1) on intact mitochondria and cells: STC-1 uncouples oxidative phosphorylation and its actions are modulated by nucleotide triphosphates. Mol. Cell. Endocrinol. 2007, 264:90-101.
3. dos Santos M.T., Trindade D.M., Goncalves Kde A., Bressan G.C., Anastassopoulos F., Yunes J.A., Kobarg J. Human stanniocalcin-1 interacts with nuclear and cytoplasmic proteins and acts as a SUMO E3 ligase. Mol. Biosyst. 2011, 7:180-193.
4. Serlachius M., Andersson L.C. Upregulated expression of stanniocalcin-1 during adipogenesis. Exp. Cell Res. 2004, 296:256-264.
5. Hasilo C.P., McCudden C.R., Gillespie J.R., James K.A., Hirvi E.R., Zaidi D., Wagner G.F. Nuclear targeting of stanniocalcin to mammary gland alveolar cells during pregnancy and lactation. Am. J. Physiol. Endocrinol. Metab. 2005, 289:E634-E642.
6. Westberg J.A., Serlachius M., Lankila P., Andersson L.C. Hypoxic preconditioning induces elevated expression of stanniocalcin-1 in the heart. Am. J. Physiol. Heart Circ. Physiol. 2007, 293:H1766-H1771.
7. McCudden C.R., James K.A., Hasilo C., Wagner G.F. Characterization of mammalian stanniocalcin receptors: mitochondrial targeting of ligand and receptor for regulation of cellular metabolism. J. Biol. Chem. 2002, 277:45249-45258.
8. Westberg J.A., Serlachius M., Lankila P., Penkowa M., Hidalgo J., Andersson L.C. Hypoxic preconditioning induces neuroprotective stanniocalcin-1 in brain via IL-6 signaling. Stroke 2007, 38:1025-1030.
9. Nguyen A., Chang A.C., Reddel R.R. Stanniocalcin-1 acts in a negative feedback loop in the prosurvival ERK1/2 signaling pathway during oxidative stress. Oncogene 2009, 28:1982-1992.
10. Wang Y., Huang L., Abdelrahim M., Cai Q., Truong A., Bick R., Poindexter B., Sheikh-Hamad D. Stanniocalcin-1 suppresses superoxide generation in macrophages through induction of mitochondrial UCP2. J. Leukoc. Biol. 2009, 86:981-988.
11. Ascenzi P., Bocedi A., Visca P., Altruda F., Tolosano E., Beringhelli T., Fasano M. Hemoglobin and heme scavenging. IUBMB Life 2005, 57:749-759.
12. Hou S., Reynolds M.F., Horrigan F.T., Heinemann S.H., Hoshi T. Reversible binding of heme to proteins in cellular signal transduction. Acc. Chem. Res. 2006, 39:918-924.
13. Jentzen W., Song X.-, Shelnutt J.A. Structural characterization of synthetic and protein-bound porphyrins in terms of the lowest-frequency normal coordinates of the macrocycle. J. Phys. Chem. B 1997, 101:1684-1699.
14. Zhou Z., Cao C., Liu Q., Jiang R. Hybrid orbital deformation (HOD) effect and spectral red-shift property of nonplanar porphyrin. Org. Lett. 2010, 12:1780-1783.
15. Lathrop J.T., Timko M.P. Regulation by heme of mitochondrial protein transport through a conserved amino acid motif. Science 1993, 259:522-525.
16. Zhang L., Guarente L. Heme binds to a short sequence that serves a regulatory function in diverse proteins. EMBO J. 1995, 14:313-320.
17. Morrison G.R. Fluorometric microdetermination of heme protein. Anal. Chem. 1965, 37:1124-1126.
18. Brown S.B., Dean T.C., Jones P. Aggregation of ferrihaems: dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solution. Biochem. J. 1970, 117:733-739.
19. Huang T.J., McCoubrey W.K., Maines M.D. Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs. Antioxid. Redox Signal. 2001, 3:685-696.
20. Yang F., Xia X., Lei H.Y., Wang E.D. Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity. J. Biol. Chem. 2010, 285:39437-39446.
21. Igarashi J., Murase M., Iizuka A., Pichierri F., Martinkova M., Shimizu T. Elucidation of the heme binding site of heme-regulated eukaryotic initiation factor 2alpha kinase and the role of the regulatory motif in heme sensing by spectroscopic and catalytic studies of mutant proteins. J. Biol. Chem. 2008, 283:18782-18791.
22. Hunter G.A., Ferreira G.C. 5-Aminolevulinate synthase: catalysis of the first step of heme biosynthesis. Cell. Mol. Biol. (Noisy-Le-Grand) 2009, 55:102-110.
23. Gray C.H. The Bile Pigments 1953, Methuen and Co., London.
24. Grinberg L.N., O'Brien P.J., Hrkal Z. The effects of heme-binding proteins on the peroxidative and catalatic activities of hemin. Free Radic. Biol. Med. 1999, 27:214-219.
25. Ogawa K., Sun J., Taketani S., Nakajima O., Nishitani C., Sassa S., Hayashi N., Yamamoto M., Shibahara S., Fujita H., Igarashi K. Heme mediates derepression of maf recognition element through direct binding to transcription repressor Bach1. EMBO J. 2001, 20:2835-2843.
26. McCoubrey W.K., Huang T.J., Maines M.D. Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis. J. Biol. Chem. 1997, 272:12568-12574.
27. Rouault T.A., Haile D.J., Downey W.E., Philpott C.C., Tang C., Samaniego F., Chin J., Paul I., Orloff D., Harford J.B. An iron-sulfur cluster plays a novel regulatory role in the iron-responsive element binding protein. Biometals 1992, 5:131-140.
28. Yang J., Kim K.D., Lucas A., Drahos K.E., Santos C.S., Mury S.P., Capelluto D.G., Finkielstein C.V. A novel heme-regulatory motif mediates heme-dependent degradation of the circadian factor period 2. Mol. Cell. Biol. 2008, 28:4697-4711.