Myeloid cell function in MRP-14 (S100A9) null mice

Molecular and Cellular Biology

Volumn 23, Issue 7, 2003, Pages 2564-2576

  Hobbs, Josie A R ^a   May, Richard ^a,b   Tanousis, Kiki ^a   McNeill, Eileen ^a   Mathies, Margaret ^a,c   Gebhardt, Christoffer ^a,d   Henderson, Robert ^a   Robinson, Matthew J ^a,e   Hogg, Nancy ^a  

^a IMPERIAL CANCER RESEARCH FUND   (United Kingdom)

^b MEDIMMUNE LTD   (United Kingdom)

^c KECK GRADUATE INSTITUTE   (United States)

^d GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

^e NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; CALCIUM ION; CALGRANULIN; CHEMOKINE; MESSENGER RNA; SUPEROXIDE;

ANIMAL CELL; ANIMAL MODEL; ANIMAL TISSUE; APOPTOSIS; ARTICLE; BONE MARROW CELL; CALCIUM TRANSPORT; CELL FUNCTION; CONTROLLED STUDY; FLOW CYTOMETRY; GENE; GENOTYPE; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; IN SITU HYBRIDIZATION; ISOELECTRIC FOCUSING; MONOCYTE; MOUSE; NEUTROPHIL; NONHUMAN; PERITONITIS; PHAGOCYTOSIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ANIMALS; CALCIUM; CALGRANULIN A; CALGRANULIN B; CELL COUNT; CELLS, CULTURED; CHEMOKINES; DOSE-RESPONSE RELATIONSHIP, DRUG; FLUORESCENT DYES; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENE TARGETING; MICE; MICE, KNOCKOUT; MONOCYTES; MYELOID CELLS; NEUTROPHILS; PERITONITIS; PHENOTYPE; RNA, MESSENGER;

ANIMALIA;

EID: 0037377737     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.7.2564-2576.2003     Document Type: Article

References (55)

1. Baudier, J., C. Delphin, D. Grunwald, S. Khochbin, and J. J. Lawrence. 1992. Characterization of the tumor suppressor protein p53 as a protein kinase C substrate and a S100b-binding protein. Proc. Natl. Acad. Sci. USA 89:11627-11631.
2. 2+ binding on S100b protein. J. Biol. Chem. 261:8192-8203.
3. Berridge, M. J., P. Lipp, and M. D. Bootman. 2000. The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell. Biol. 1:11-21.
4. 2+-free states. Biochemistry 38:1695-1704.
5. Donato, R. 2001. S100: a multigenic family of calcium-modulated proteins of the EF-hand type with intracellular and extracellular functional roles. Int. J. Biochem. Cell. Biol. 33:637-668.
6. Drohat, A. C., D. M. Baldisseri, R. R. Rustandi, and D. J. Weber. 1998. Solution structure of calcium-bound rat S100B(ββ) as determined by nuclear magnetic resonance spectroscopy. Biochemistry 37:2729-2740.
7. Du, X. J., T. J. Cole, N. Tenis, X. M. Gao, F. Kontgen, B. E. Kemp, and J. Heierhorst. 2002. Impaired cardiac contractility response to hemodynamic stress in S100A1-deficient mice. Mol. Cell. Biol. 22:2821-2829.
8. Duda, T., K. W. Koch, V. Venkataraman, C. Lange, M. Beyermann, and R. K. Sharma. 2002. Ca(2+) sensor S100β-modulated sites of membrane guanylate cyclase in the photoreceptor-bipolar synapse. EMBO J. 21:2547-2556.
9. Edgeworth, J., M. Gorman, R. Bennett, P. Freemont, and N. Hogg. 1991. Identification of p8,14 as a highly abundant heterodimeric calcium binding protein complex of myeloid cells. J. Biol. Chem. 266:7706-7713.
10. Freemont, P., N. Hogg, and J. Edgeworth. 1989. Sequence identity. Nature 339:516.
11. Gabrielsen, T. O., I. Dale, P. Brandtzaeg, P. S. Hoel, M. K. Fagerhol, T. E. Larsen, and P. O. Thune. 1986. Epidermal and dermal distribution of a myelomonocytic antigen (LI) shared by epithelial cells in various inflammatory skin diseases. J. Am. Acad. Dermatol. 15:173-179.
12. Gebhardt, C., U. Breitenbach, J. P. Tuckermann, K. H. Richter, and P. Angel. 2002. Calgranulins S100A8 and S100A9 are negatively regulated by glucocorticoid in a c-Fos-dependent manner and overexpressed throughout skin carcinogenesis. Oncogene 21:4266-4276.
13. Goebeler, M., J. Roth, U. Henseleit, C. Sunderkotter, and C. Sorg. 1993. Expression and complex assembly of calcium-binding proteins MRP8 and MRP14 during differentiation of murine myelomonocytic cells. J. Leukoc. Biol. 53:11-18.
14. Gribenko, A. V., J. E. Hopper, and G. I. Makhatadze. 2001. Molecular characterization and tissue distribution of a novel member of the S100 family of EF-hand proteins. Biochemistry 40:15538-15548.
15. Grigorian, M., E. Tulchinsky, O. Burrone, S. Tarabykina, G. Georgiev, and E. Lukanidin. 1994. Modulation of mts1 expression in mouse and human normal and tumor cells. Electrophoresis 15:463-468.
16. 2+/S100 regulation of giant protein kinases. Nature 380:636-639.
17. 2+-binding protein family. Biometals 11:383-397.
18. Henderson, R. B., L. H. Lim, P. A. Tessier, F. N. Gavins, M. Mathies, M. Perretti, and N. Hogg. 2001. The use of lymphocyte function-associated antigen (LFA)-1-deficient mice to determine the role of LFA-1, Mac-1, and a4 integrin in the inflammatory response of neutrophils. J. Exp. Med. 194: 219-226.
19. 2+-binding proteins of neutrophils and monocytes. J. Leukoc. Biol. 53:197-204.
20. Hofmann, M. A., S. Drury, C. Fu, W. Qu, A. Taguchi, Y. Lu, C. Avila, N. Kambham, A. Bierhaus, P. Nawroth, M. F. Neurath, T. Slattery, D. Beach, J. McClary, M. Nagashima, J. Morser, D. Stern, and A. M. Schmidt. 1999. RAGE mediates a novel proinflammatory axis: a central cell surface receptor for S100/calgranulin polypeptides. Cell 97:889-901.
21. Hogg, N., C. Allen, and J. Edgeworth. 1989. Monoclonal antibody 5.5 reacts with p8,14, a myeloid molecule associated with some vascular endothelium. Eur. J. Immunol. 19:1053-1061.
22. Howell, M., and C. S. Hill. 1997. XSmad2 directly activates the activin-inducible, dorsal mesoderm gene XFKH1 in Xenopus embryos. EMBO J. 16:7411-7421.
23. Hubl, W., J. Iturraspe, G. A. Martinez, C. E. Hutcheson, C. G. Roberts, D. D. Fisk, M. W. Sugrue, J. R. Wingard, and R. C. Braylan. 1998. Measurement of absolute concentration and viability of CD34+ cells in cord blood and cord blood products with fluorescent beads and cyanine nucleic acid dyes. Cytometry 34:121-127.
24. Hunter, M. J., and W. J. Chazin. 1998. High level expression and dimer characterization of the S100 EF-hand proteins, migration inhibitory factor-related proteins 8 and 14. J. Biol. Chem. 273:12427-12435.
25. Jinquan, T., H. Vorum, C. G. Larsen, P. Madsen, H. H. Rasmussen, B. Gesser, M. Etzerodt, B. Honore, J. E. Celis, and K. Thestrup-Pedersen. 1996. Psoriasin: a novel chemotactic protein. J. Investig. Dermatol. 107:5-10.
26. Kerkhoff, C., C. Sorg, N. N. Tandon, and W. Nacken. 2001. Interaction of S100A8/S100A9-arachidonic acid complexes with the scavenger receptor CD36 may facilitate fatty acid uptake by endothelial cells. Biochemistry 40:241-248.
27. Komada, T., R. Araki, K. Nakatani, I. Yada, M. Naka, and T. Tanaka. 1996. Novel specific chemotactic receptor for S100L protein on guinea pig eosinophils. Biochem. Biophys. Res. Commun. 220:871-874.
28. Lackmann, M., C. J. Cornish, R. J. Simpson, R. L. Moritz, and C. L. Geczy. 1992. Purification and structural analysis of a murine chemotactic cytokine (CP-10) with sequence homology to S100 proteins. J. Biol. Chem. 267:7499-7504.
29. Lackmann, M., P. Rajasekariah, S. E. Iismaa, G. Jones, C. J. Cornish, S. Hu, R. J. Simpson, R. L. Moritz, and C. L. Geczy. 1993. Identification of a chemotactic domain of the pro-inflammatory S100 protein CP-10. J. Immunol. 150:2981-2991.
30. Lagasse, E., and R. G. Clerc. 1988. Cloning and expression of two human genes encoding calcium-binding proteins that are regulated during myeloid differentiation. Mol. Cell. Biol. 8:2402-2410.
31. Lagasse, E., and I. L. Weissman. 1992. Mouse MRP8 and MRP14, two intracellular calcium-binding proteins associated with the development of the myeloid lineage. Blood 79:1907-1915.
32. McColl, S. R., and P. H. Naccache. 1997. Calcium mobilization assays. Methods Enzymol. 288:301-309.
33. Millward, T. A., C. W. Heizmann, B. W. Schafer, and B. A. Hemmings. 1998. Calcium regulation of Ndr protein kinase mediated by S100 calcium-binding proteins. EMBO J. 17:5913-5922.
34. Nacken, W., C. Sopalla, C. Propper, C. Sorg, and C. Kerkhoff. 2000. Biochemical characterization of the murine S100A9 (MRP14) protein suggests that it is functionally equivalent to its human counterpart despite its low degree of sequence homology. Eur. J. Biochem. 267:560-565.
35. Nishiyama, H., T. Knopfel, S. Endo, and S. Itohara. 2002. Glial protein S100B modulates long-term neuronal synaptic plasticity. Proc. Natl. Acad. Sci. USA 99:4037-4042.
36. Odink, K., N. Cerletti, J. Bruggen, R. G. Clerc, L. Tarcsay, G. Zwadlo, G. Gerhards, R. Schlegel, and C. Sorg. 1987. Two calcium-binding proteins in infiltrate macrophages of rheumatoid arthritis. Nature 330:80-82.
37. 2+-bound states. The calcium sensor mechanism of S100 proteins revealed at atomic resolution. Structure (Cambridge) 10:557-567.
38. Passey, R. J., E. Williams, A. M. Lichanska, C. Wells, S. Hu, C. L. Geczy, M. H. Little, and D. A. Hume. 1999. A null mutation in the inflammation-associated S100 protein S100A8 causes early resorption of the mouse embryo. J. Immunol. 163:2209-2216.
39. Pettit, E. J., E. V. Davies, and M. B. Hallett. 1997. The microanatomy of calcium stores in human neutrophils: relationship of structure to function. Histol. Histopathol. 12:479-490.
40. Raftery, M. J., C. A. Harrison, P. Alewood, A. Jones, and C. L. Geczy. 1996. Isolation of the murine S100 protein MRP14 (14 kDa migration-inhibitory-factor-related protein) from activated spleen cells: characterization of posttranslational modifications and zinc binding. Biochem. J. 316:285-293.
41. Rammes, A., J. Roth, M. Goebeler, M. Klempt, M. Hartmann, and C. Sorg. 1997. Myeloid-related protein (MRP) 8 and MRP14, calcium-binding proteins of the S100 family, are secreted by activated monocytes via a novel, tubulin-dependent pathway. J. Biol. Chem. 272:9496-9502.
42. Ridinger, K., E. C. Ilg, F. K. Niggli, C. W. Heizmann, and B. W. Schafer. 1998. Clustered organization of S100 genes in human and mouse. Biochim. Biophys. Acta 1448:254-263.
43. Robinson, M. J., and N. Hogg. 2000. A comparison of human S100A12 with MRP-14 (S100A9). Biochem. Biophys. Res. Commun. 275:865-870.
44. Robinson, M. J., P. Tessier, R. Poulsom, and N. Hogg. 2002. The S100 family heterodimer, MRP-8 and MRP-14, binds with high affinity to heparin and heparan sulfate glycosaminoglycans on endothelial cells. J. Biol. Chem. 277: 3658-3665.
45. Schafer, B. W., and C. W. Heizmann. 1996. The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biochem. Sci. 21:134-140.
46. Schmidt, M., R. Gillitzer, A. Toksoy, E. B. Brocker, U. R. Rapp, R. Paus, J. Roth, S. Ludwig, and M. Goebeler. 2001. Selective expression of calcium. binding proteins S100a8 and S100a9 at distinct sites of hair follicles. J. Investig. Dermatol. 117:748-750.
47. Senior, P. V., D. R. Critchley, F. Beck, R. A. Walker, and J. M. Varley. 1988. The localization of laminin mRNA and protein in the postimplantation embryo and placenta of the mouse: an in situ hybridization and immunocytochemical study. Development 104:431-446.
48. Smelt, S. C., S. E. Cotterell, C. R. Engwerda, and P. M. Kaye. 2000. B cell-deficient mice are highly resistant to Leishmania donovani infection, but develop neutrophil-mediated tissue pathology. J. Immunol. 164:3681-3688.
49. Smith, J. A., and M. J. Weidemann. 1993. Further characterization of the neutrophil oxidative burst by flow cytometry. J. Immunol. Methods 162:261-268.
50. Srikrishna, G., K. Panneerselvam, V. Westphal, V. Abraham, A. Varki, and H. H. Freeze. 2001. Two proteins modulating transendothelial migration of leukocytes recognize novel carboxylated glycans on endothelial cells. J. Immunol. 166:4678-4688.
51. Teigelkamp, S., R. S. Bhardwaj, J. Roth, G. Meinardus-Hager, M. Karas, and C. Sorg. 1991. Calcium-dependent complex assembly of the myeloic differentiation proteins MRP-8 and MRP-14. J. Biol. Chem. 266:13462-13467.
52. 2+-binding proteins S100A8 and S100A9 are encoded by novel injury-regulated genes. J. Biol. Chem. 276:35818-35825.
53. Vogl, T., C. Propper, M. Hartmann, A. Strey, K. Strupat, C. van den Bos, C. Sorg, and J. Roth. 1999. S100A12 is expressed exclusively by granulocytes and acts independently from MRP8 and MRP14. J. Biol. Chem. 274:25291-25296.
54. Wan, C. P., C. S. Park, and B. H. Lau. 1993. A rapid and simple microfluorometric phagocytosis assay. J. Immunol. Methods 162:1-7.
55. Witko-Sarsat, V., P. Rieu, B. Descamps-Latscha, P. Lesavre, and L. Halbwachs-Mecarelli. 2000. Neutrophils: molecules, functions and pathophysiological aspects. Lab. Investig. 80:617-653.