Disruption of the meprin α and β genes in mice alters homeostasis of monocytes and natural killer cells

Experimental Hematology

Volumn 37, Issue 3, 2009, Pages 346-356

  Sun, Qi ^a   Jin, Hong Jian ^a   Bond, Judith S ^b  

^a PENN STATE CHILDREN S HOSPITAL   (United States)

^b PENN STATE COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MEPRIN; MEPRIN ALPHA; MEPRIN BETA; METALLOPROTEINASE; THIOGLYCOLIC ACID; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; B LYMPHOCYTE; BONE MARROW; CONTROLLED STUDY; GENE; GENE DISRUPTION; HOMEOSTASIS; INFLAMMATION; LEUKOCYTE; MEPRIN ALPHA GENE; MEPRIN BETA GENE; MONOCYTE; MOUSE; NATURAL KILLER CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; T LYMPHOCYTE; WILD TYPE;

ANIMALS; BLOOD CELL COUNT; BODY TEMPERATURE; BONE MARROW CELLS; HOMEOSTASIS; IMMUNE SYSTEM; INFLAMMATION; KILLER CELLS, NATURAL; METALLOENDOPEPTIDASES; MICE; MONOCYTES;

MUS;

EID: 59749090413     PISSN: 0301472X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exphem.2008.10.016     Document Type: Article

References (39)

1. Beynon R.J., Shannon J.D., and Bond J.S. Purification and characterization of a metallo-endoproteinase from mouse kidney. Biochem J 199 (1981) 591-598
2. Sterchi E.E., Naim H.Y., Lentze M.J., Hauri H.P., and Fransen J.A. N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase: a metalloendopeptidase of the human intestinal microvillus membrane which degrades biologically active peptides. Arch.Biochem.Biophys 265 (1988) 105-118
3. Bond J.S., Matters G.L., Banerjee S., and Dusheck R.E. Meprin metalloprotease expression and regulation in kidney, intestine, urinary tract infections and cancer. FEBS Lett 579 (2005) 3317-3322
4. Lottaz D., Hahn D., Muller S., Muller C., and Sterchi E.E. Secretion of human meprin from intestinal epithelial cells depends on differential expression of the alpha and beta subunits. Eur J Biochem 259 (1999) 496-504
5. Crisman J.M., Zhang B., Norman L.P., and Bond J.S. Deletion of the mouse meprin β metalloprotease gene diminishes the ability of leukocytes to disseminate through extracellular matrix. J Immunol 172 (2004) 4510-4519
6. Stocker W., and Zwilling R. Astacin. Methods Enzymol 248 (1995) 305-325
7. Bertenshaw G.P., Norcum M.T., and Bond J.S. Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers. J Biol Chem 278 (2003) 2522-2532
8. Marchand P., Tang J., and Bond J.S. Membrane association and oligomeric organization of the alpha and beta subunits of mouse meprin A. J Biol Chem 269 (1994) 15388-15393
9. Hahn D., Pischitzis A., Roesmann S., et al. Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinbeta metalloprotease. J Biol Chem 278 (2003) 42829-42839
10. Kumar J.M., and Bond J.S. Developmental expression of meprin metalloprotease subunits in ICR and C3H/He mouse kidney and intestine in the embryo, postnatally and after weaning. Biochim Biophys Acta 1518 (2001) 106-114
11. Becker-Pauly C., Howel M., Walker T., et al. The alpha and beta subunits of the metalloprotease meprin are expressed in separate layers of human epidermis, revealing different functions in keratinocyte proliferation and differentiation. J Invest Dermatol 127 (2007) 1115-1125
12. Bertenshaw G.P., Turk B.E., Hubbard S.J., et al. Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity. J Biol Chem 276 (2001) 13248-13255
13. Kruse M.N., Becker C., Lottaz D., et al. Human meprin alpha and beta homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors. Biochem J 378 (2004) 383-389
14. Bylander J.E., Bertenshaw G.P., Matters G.L., Hubbard S.J., and Bond J.S. Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities. Biol Chem 388 (2007) 1163-1172
15. Kaushal G.P., Walker P.D., and Shah S.V. An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin. J Cell Biol 126 (1994) 1319-1327
16. Herzog C., Kaushal G.P., and Haun R.S. Generation of biologically active interleukin-1beta by meprin B. Cytokine 31 (2005) 394-403
17. Norman L.P., Jiang W., Han X., Saunders T.L., and Bond J.S. Targeted disruption of the meprin β gene in mice leads to underrepresentation of knockout mice and changes in renal gene expression profiles. Mol Cell Biol 23 (2003) 1221-1230
18. Banerjee S. Meprin metalloproteases modulate the intestinal host response. Doctoral thesis. Pennsylvania State University; 2008. (http://etda.libraries.psu.edu/theses/approved/WorldWideIndex/ETD-2541/index.html).
19. Sun Q., Burton R.L., Dai L.J., and Lucas K.G. B-lymphoblastoid cell lines expressing CMV pp65 elicited ex vivo polyclonal expansion of CD8+cytotoxic T-lymphocytes against Epstein-Barr virus and cytomegalovirus. Blood 94 (1999) 556A
20. Sun Q., Brewer N., Dunham K., et al. Interferon-gamma expressing EBV LMP2A-specific T cells for cellular immunotherapy. Cell Immunol 246 (2007) 81-91
21. Lagasse E., and Weissman I.L. Flow cytometric identification of murine neutrophils and monocytes. J Immunol Methods 197 (1996) 139-150
22. Geissmann F., Jung S., and Littman D.R. Blood monocytes consist of two principal subsets with distinct migratory properties. Immunity 19 (2003) 71-82
23. Benamar K., McMenamin M., Geller E.B., Chung Y.G., Pintar J.E., and Adler M.W. Unresponsiveness of mu-opioid receptor knockout mice to lipopolysaccharide-induced fever. Br J Pharmacol 144 (2005) 1029-1031
24. Hanson D.F. Fever, temperature, and the immune response. Ann N Y Acad Sci 813 (1997) 453-464
25. Sunderkotter C., Nikolic T., Dillon M.J., et al. Subpopulations of mouse blood monocytes differ in maturation stage and inflammatory response. J Immunol 172 (2004) 4410-4417
26. Varol C., Landsman L., Fogg D.K., et al. Monocytes give rise to mucosal, but not splenic, conventional dendritic cells. J Exp Med 204 (2007) 171-180
27. Leon B., Martinez del Hoyo G., Parrillas V., et al. Dendritic cell differentiation potential of mouse monocytes: monocytes represent immediate precursors of CD8- and CD8+ splenic dendritic cells. Blood 103 (2004) 2668-2676
28. Passlick B., and Flieger D. Ziegler-Heitbrock HW. Identification and characterization of a novel monocyte subpopulation in human peripheral blood. Blood 74 (1989) 2527-2534
29. Akashi S., Saitoh S.I., Wakabayashi Y., et al. Lipopolysaccharide interaction with cell surface toll-like receptor 4-MD-2: higher affinity than that with MD-2 or CD14. J Exp Med 198 (2003) 1035-1042
30. Gordon S., and Taylor P.R. Monocyte and macrophage heterogeneity. Nat Rev Immunol 5 (2005) 953-964
31. Tsou C.L., Peters W., Si Y., et al. Critical roles for CCR2 and MCP-3 in monocyte mobilization from bone marrow and recruitment to inflammatory sites. J Clin Invest 117 (2007) 902-909
32. Yokoyama W.M., Kim S., and French A.R. The dynamic life of natural killer cells. Annu Rev Immunol 22 (2004) 405-429
33. Jameson SC. Maintaining the norm. T-cell homeostasis. Nat Rev Immunol 2 (2002) 547-556
34. Mackay F., Schneider P., Rennert P., and Browning J. BAFF AND APRIL: a tutorial on B cell survival. Annu Rev Immunol 21 (2003) 231-264
35. Banchereau J., and Steinman R.M. Dendritic cells and the control of immunity. Nature 392 (1998) 245-252
36. Ostberg J.R., and Repasky E.A. Emerging evidence indicates that physiologically relevant thermal stress regulates dendritic cell function. Cancer Immunol Immunother 55 (2006) 292-298
37. Ostberg J.R., Dayanc B.E., Yuan M., Oflazoglu E., and Repasky E.A. Enhancement of natural killer (NK) cell cytotoxicity by fever-range thermal stress is dependent on NKG2D function and is associated with plasma membrane NKG2D clustering and increased expression of MICA on target cells. J Leukoc Biol 82 (2007) 1322-1331
38. Hatzfeld-Charbonnier A.S., Lasek A., Castera L., et al. Influence of heat stress on human monocyte-derived dendritic cell functions with immunotherapeutic potential for antitumor vaccines. J Leukoc Biol 81 (2007) 1179-1187
39. Ebnet K., and Vestweber D. Molecular mechanisms that control leukocyte extravasation: the selectins and the chemokines. Histochem Cell Biol 112 (1999) 123