Hemopexin: The primary specific carrier of plasma heme

Biochemistry and Molecular Biology Education

Volumn 30, Issue 5, 2002, Pages 332-335

  Mattu, Marco ^a   Fasano, Mauro ^b   Spallarossa, Andrea ^c   Bolognesi, Martino ^c   Ascenzi, Paolo ^a  

^a ROMA TRE UNIVERSITY   (Italy)

^b UNIVERSITY OF INSUBRIA   (Italy)

^c UNIVERSITY OF GENOA   (Italy)

Author keywords

Heme hemopexin complex; Heme iron geometry; Hemopexin

Indexed keywords

ARGININE; CARRIER PROTEIN; CATALASE; CLATHRIN; CYTOCHROME; DISULFIDE; HEME; HEMOGLOBIN; HEMOPEXIN; HIGH DENSITY LIPOPROTEIN CHOLESTEROL; HISTIDINE; INTEGRIN; IRON; LIGAND; LOW DENSITY LIPOPROTEIN CHOLESTEROL; MATRIX METALLOPROTEINASE; MYELOPEROXIDASE; MYOGLOBIN; PEROXIDASE; PHENYLALANINE; SERUM ALBUMIN; TRYPTOPHAN; TYROSINE;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; BLOOD FLOW; CARBOXY TERMINAL SEQUENCE; ERYTHROCYTE; GEOMETRY; LIVER; METABOLIC CLEARANCE RATE; NEUTROPHIL; NONHUMAN; PROTEIN DOMAIN; PROTEIN STRUCTURE; TISSUE INJURY; TRANSPORT KINETICS;

EID: 8644292749     PISSN: 14708175     EISSN: None     Source Type: Journal    
DOI: 10.1002/bmb.2002.494030050123     Document Type: Article

References (24)

1. M. E. Conrad, J. N. Umbreit, E. G. Moore (1999) Iron absorption and transport, Am. J. Med. Sci. 318, 213-229.
2. Y. I. Miller, N. Shaklai (1999) Kinetics of hemin distribution in plasma reveals its role in lipoprotein oxidation, Biochim. Biophys. Acta 1454, 153-164.
3. J. R. Delanghe, M. R. Langlois (2001) Hemopexin: a review of biological aspects and the role in laboratory medicine, Clin. Chim. Acta 312, 13-23.
4. H. R. Faber, C. R. Groom, H. M. Baker, W. T. Morgan, A. Smith, E. N. Baker (1995) 1.8 Å crystal structure of the C-terminal domain of rabbit serum haemopexin. Structure 3, 551-559.
5. M. Paoli, B. F. Anderson, H. M. Baker, W. T. Morgan, A. Smith, E. N. Baker (1999) Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains. Nat. Struct. Biol. 6, 926-931.
6. U. Gohlke, F. X. Gomis-Ruth, T. Crabbe, G. Murphy, A. J. Docherty, W. Bode (1996) The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function. FEBS Lett. 378, 126-130.
7. I. Massova, L. P. Kotra, R. Fridman, S. Mobashery (1998) Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 12, 1075-1095.
8. W. Bode, C. Fernandez-Catalan, H. Tschesche, F. Grams, H. Nagase, K. Maskos (1999) Structural properties of matrix metalloproteinases. Cell. Mol. Life. Sci. 55, 639-652.
9. C. M. Overall (2001) Matrix metalloproteinase substrate binding domains, modules and exosites: overview and experimental strategies. Methods Mol. Biol. 151, 79-120.
10. M. Gioia, G. F. Fasciglione, S. Marini, S. D'Alessio, G. De Sanctis, O. Diekmann, M. Pieper, V. Politi, H. Tschesche, M. Coletta (2002) Modulation of the catalytic activity of neutrophil collagenase MMP-8 on bovine collagen: I. role of the activation cleavage and of the hemopexin-like domain, J. Biol. Chem. 277, 23123-23130.
11. D. G. Lambright, J. Sondek, A. Bohm, N. P. Skiba, H. E. Hamm, P. B. Sigler (1996) The 2.0 ̊ crystal structure of a heterotrimeric G protein, Nature 379, 311-319.
12. E. Ter Haar, A. Musacchio, S. C. Harrison, T. Kirchhausen (1998) Atomic structure of clathrin: a β-propeller terminal domain joins an α-zigzag linker, Cell 95, 563-573.
13. T. A. Springer (1997) Folding of the N-terminal, ligand-binding region of integrin α-subunits into a β-propeller domain, Proc. Natl. Acad. Sci. U. S. A. 94, 65-72.
14. T. F. Smith, C. Gaitatzes, K. Saxena, E. J. Neer (1999) The WD repeat: a common architecture for diverse functions, Trends Biochem. Sci. 24, 181-185.
15. M. F. Perutz (1979) Regulation of oxygen affinity of hemoglobin: influence of structure of the globin on the heme iron, Annu. Rev. Biochem. 48, 327-386.
16. M. Bolognesi, D. Bordo, M. Rizzi, C. Tarricone, P. Ascenzi (1997) Nonvertebrate hemoglobins: structural bases for reactivity, Prog. Biophys. Mol. Biol. 68, 29-68.
17. W. E. Royer, Jr., J. E. Knapp, K. Strand, H. A. Heaslet (2001) Cooperative hemoglobins: conserved fold, diverse quaternary assemblies and allosteric mechanisms, Trends Biochem. Sci. 26, 297-304.
18. A. Pesce, M. Nardini, S. Dewilde, E. Geuens, K. Yamauchi, P. Ascenzi, A. F. Riggs, L. Moens, M. Bolognesi (2002) The 109 residue nerve tissue minihemoglobin from Cerebratulus lacteus highlights striking structural plasticity of the α-helical globin fold, Structure 10, 725-735.
19. J. B. Wittenberg, M. Bolognesi, B. A. Wittenberg, M. Guertin (2002) Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants, J. Biol. Chem. 277, 871-874.
20. W. T. Morgan, A. Smith (1984) Domain structure of rabbit hemopexin: isolation and characterization of a heme-binding glycopeptide, J. Biol. Chem. 259, 12001-12006.
21. P. Ascenzi, M. Nardini, M. Bolognesi, W. R. Montfort (2002) Nitrophorins: Lipocalin-based heme proteins transporting nitric oxide, Biochem. Mol. Biol. Biol. 30, 68-71.
22. P. J. Kraulis (1991) MOLSCRIPT a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 34, 946-950.
23. G. S. Kachalova, A. N. Popov, H. D. Bartunik (1999) A steric mechanism for inhibition of CO binding to heme proteins, Science 284, 473-476.
24. T. Takano (1977) Structure of myoglobin refined at 2.0 Å resolution: I. Crystallographic refinement of metamyoglobin from sperm whale, J. Mol. Biol. 110, 537-568.