Phagocyte-specific S100 proteins: A novel group of proinflammatory molecules

Trends in Immunology

Volumn 24, Issue 4, 2003, Pages 155-158

  Roth, Johannes ^a   Vogl, Thomas ^a   Sorg, Clemens ^a   Sunderkötter, Cord ^a,b  

^a UNIVERSITY OF MÜNSTER   (Germany)

^b UNIVERSITY OF ULM   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; PROTEIN S 100; PROTEIN S 100A12; PROTEIN S 100A8; PROTEIN S 100A9; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

CALCIUM BINDING; ENDOTHELIUM CELL; GENE OVEREXPRESSION; GLYCATION; HUMAN; IN VITRO STUDY; INFLAMMATION; LEUKOCYTE; LYMPHOCYTE; PHAGOCYTE; PROTEIN EXPRESSION; PROTEIN FAMILY; PROTEIN INTERACTION; REVIEW;

EID: 0037383648     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1471-4906(03)00062-0     Document Type: Review

References (27)

1. Heizmann C.W. The multifunctional S100 protein family. Methods Mol. Biol. 172:2002;69-80.
2. Odink K., et al. Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis. Nature. 330:1987;80-82.
3. Roth J., et al. MRP8 and MRP14, S-100-like proteins associated with myeloid differentiation, are translocated to plasma membrane and intermediate filaments in a calcium-dependent manner. Blood. 82:1993;1875-1883.
4. Passey R.J., et al. A null mutation in the inflammation-associated S100 protein S100A8 causes early resorption of the mouse embryo. J. Immunol. 163:1999;2209-2216.
5. Manitz M.P., et al. Loss of S100A9 (MRP14) results in a reduced IL-8 induced CD11b surface expression, a polarized microfilament system and a diminished responsiveness upon chemoattractants in vitro. Mol. Cell. Biol. 23:2003;1034-1043.
6. Berntzen H.B., Fagerhol M.K. L1, a major granulocyte protein; isolation of high quantities of its subunits. Scand. J. Clin. Lab. Invest. 50:1990;769-774.
7. Kerkhoff C., et al. Novel insights into structure and function of MRP8 (S100A8) and MRP14 (S100A9). Biochim. Biophys. Acta. 1448:1998;200-211.
8. Hunter M.J., Chazin W.J. High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14. J. Biol. Chem. 273:1998;12427-12435.
9. Vogl T., et al. Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 detected by ultraviolet matrix-assisted laser desorption/ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 10:1999;1124-1130.
10. Frosch M., et al. Myeloid-related proteins 8 and 14 are specifically secreted during interaction of phagocytes and activated endothelium and are useful markers for monitoring disease activity in pauciarticular-onset juvenile rheumatoid arthritis. Arthritis Rheum. 43:2000;628-637.
11. Robinson M.J., et al. The S100 family heterodimer, MRP-8/14, binds with high affinity to heparin and heparan sulphate glycosaminoglycans on endothelial cells. J. Biol. Chem. 277:2002;3658-3665.
12. Srikrishna G., et al. Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells. J. Immunol. 166:2001;4678-4688.
13. Newton R.A., Hogg N. The human S100 protein MRP-14 is a novel activator of the β2 integrin Mac-1 on neutrophils. J. Immunol. 160:1998;1427-1435.
14. Geczy C. Regulation and proinflammatory properties of the chemotactic protein, Cp 10. Biochim. Biophys. Acta. 1313:1996;246-252.
15. 2+-binding proteins S100A8 and S100A9 are encoded by novel injury-regulated genes. J. Biol. Chem. 276:2001;35818-35825.
16. Kerkhoff C., et al. Interaction of S100A8-S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells. Biochemistry. 40:2001;241-248.
17. Sampson B., et al. Hyperzincaemia with hypercalprotectinaemia: a new disorder of zinc metabolism. Identification of calprotectin (S100A8/S100A9) as the zinc binding protein in patients with hyperzincaemia. Lancet. 360:2002;1742-1745.
18. Yui S., et al. Growth inhibitory and apoptosis inducing activities of calprotectin derived from inflammatory exudate cells on normal fibroblasts: regulation by metal ions. J. Leukoc. Biol. 61:1997;50-57.
19. Vogl T., et al. S100A12 is expressed exclusively by granulocytes and acts independently from MRP8 and MRP14. J. Biol. Chem. 274:1999;25291-25296.
20. Boussac M., Garin J. Calcium-dependent secretion in human neutrophils: a proteomic approach. Electrophoresis. 21:2000;665-672.
21. Hofmann M.A., et al. RAGE mediates a novel proinflammatory-axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell. 97:1999;889-901.
22. Schmidt A.M., et al. The multiligand receptor RAGE as a progression factor amplifying immune and inflammatory responses. J. Clin. Invest. 108:2001;949-955.
23. Yan S.D., et al. Receptor-dependent cell stress and amyloid accumulation in systemic amyloidosis. Nat. Med. 6:2000;643-651.
24. Taguchi A., et al. Blockade of RAGE-amphoterin signalling suppresses tumour growth and metastases. Nature. 405:2000;354-360.
25. Foell, D. et al. Neutrophil derived human S100A12 (EN-RAGE) is strongly expressed during chronic active inflammatory bowel disease. Gut (in press).
26. Foell, D. et al. S100A12 (EN-RAGE): A novel serum marker in the monitoring of Kawasaki disease. Lancet (in press).
27. Huttunen H.J., et al. Receptor for advanced glycation end products-binding COOH-terminal motif of amphoterin inhibits invasive migration and metastasis. Cancer Res. 62:2002;4805-4811.