ά4Β1 integrin and 190-kDa CD44v constitute a cell surface docking complex for gelatinase B/MMP-9 in chronic leukemic but not in normal B cells

Blood

Volumn 112, Issue 1, 2008, Pages 169-178

  Redondo Muñoz, Javier ^a   Ugarte Berzal, Estefanía ^a   García Marco, José A ^b   Del Cerro, Mercedes Hernández ^a   Van Den Steen, Philippe E ^c   Opdenakker, Ghislain ^c   Terol, María José ^d   García Pardo, Angeles ^a  

^a CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^b HOSPITAL UNIVERSITARIO PUERTA DE HIERRO   (Spain)

^c REGA INSTITUTE FOR MEDICAL RESEARCH   (Belgium)

^d HOSPITAL CLÍNICO UNIVERSITARIO   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

BETA1 INTEGRIN; CD44V ANTIGEN; GELATINASE B; HEMOPEXIN; VERY LATE ACTIVATION ANTIGEN 4; CD44 PROTEIN, HUMAN; ENZYME PRECURSOR; HERMES ANTIGEN; ISOPROTEIN; MULTIPROTEIN COMPLEX; PRO MATRIX METALLOPROTEINASE 9; PRO-MATRIX METALLOPROTEINASE 9; SMALL INTERFERING RNA;

ADULT; AGED; ARTICLE; B LYMPHOCYTE; CELL CYCLE ARREST; CELL INVASION; CELL MIGRATION; CELL SURFACE; CHRONIC LEUKEMIA; CLINICAL ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME RELEASE; FEMALE; HUMAN; HUMAN CELL; IMMUNOFLUORESCENCE; IMMUNOPRECIPITATION; MALE; MOLECULAR WEIGHT; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN SECRETION; B CELL LEUKEMIA; CANCER INVASION; CELL ADHESION; CELL MEMBRANE; CELL MOTION; CHEMISTRY; DRUG ANTAGONISM; ENZYMOLOGY; GENE SILENCING; GENETIC VARIABILITY; GENETICS; IMMUNOLOGY; METABOLISM; MIDDLE AGED; PATHOLOGY;

AGED; AGED, 80 AND OVER; ANTIGENS, CD44; B-LYMPHOCYTES; CELL ADHESION; CELL MEMBRANE; CELL MOVEMENT; ENZYME PRECURSORS; FEMALE; GENE SILENCING; HUMANS; INTEGRIN ALPHA4BETA1; LEUKEMIA, LYMPHOCYTIC, CHRONIC, B-CELL; MALE; MATRIX METALLOPROTEINASE 9; MIDDLE AGED; MOLECULAR WEIGHT; MULTIPROTEIN COMPLEXES; NEOPLASM INVASIVENESS; PROTEIN ISOFORMS; RNA, SMALL INTERFERING; VARIATION (GENETICS);

EID: 47249093296     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2007-08-109249     Document Type: Article

References (49)

1. Zent CS, Kay NE. Advances in the understanding of biology and prognosis in chronic lymphocytic leukemia. Curr Oncol Rep. 2004;6:348-354.
2. Rai KR. Pathophysiologic mechanisms of chronic lymphocytic leukemia and their application to therapy. Exp Hematol. 2007;35:134-136.
3. Till KJ, Lin K, Zuzel M, Cawley JC. The chemokine receptor CCR7 and α4 integrin are important for migration of chronic lymphocytic leukemia cells into lymph nodes. Blood. 2002;99:2977-2984.
4. López-Giral S, Quintana NE, Cabrerizo M, et al. Chemokine receptors that mediate B cell homing to secondary lymphoid tissues are highly expressed in B cell chronic lymphocytic leukemia and non-Hodgkin lymphomas with widespread nodular dissemination. J Leuk Biol. 2004;76:462-471.
5. Till KJ, Spiller DG, Harris RJ, et al. CLL, but not normal, B cells are dependent on autocrine VEGF and alpha;4beta;1 integrin for chemokine-induced motility on and through endothelium. Blood. 2005; 105:4813-4819.
6. Redondo-Muñoz J, Escobar-Díaz E, Samaniego R, et al. MMP-9 in B-cell chronic lymphocytic leukemia is up-regulated by alpha;4beta;1 integrin or CXCR4 engagement via distinct signaling pathways, localizes to podosomes, and is involved in cell invasion and migration. Blood. 2006;108:3143-3151.
7. Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nature Rev Cancer. 2002;2:161-176.
8. Stamenkovic I. Extracellular matrix remodelling: the role of matrix metalloproteinases. J Pathol. 2003;200:448-464.
9. Deryugina EI, Quigley JP. Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev. 2006;25:9-34.
10. Bauvois B, Dumont J, Mathiot C, Kolb JP. Production of matrix metalloproteinase-9 in early stage B-CLL: suppression by interferons. Leukemia. 2002;16:791-798.
11. Kamiguti AS, Lee ES, Till KJ, et al. The role of matrix metalloproteinase-9 in the patogenesis of chronic lymphocytic leukemia. Br J Haematol. 2004;125:128-140.
12. Redondo-Muñoz J, Terol MJ, García-Marco JA, García-Pardo A. Matrix metalloproteinase-9 is up-regulated by CCL21/CCR7 interaction via extracellular signal-regulated kinase-1/2 signaling and is involved in CCL21-driven B-cell chronic lymphocytic leukemia cell invasion and migration. Blood. 2008;111:383-386.
13. Fridman R, Toth M, Chvyrkova I, et al. Cell surface association of matrix metalloproteinase-9 (gelatinase B). Cancer Metastasis Rev. 2003;22:153-166.
14. 3,8-10 is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells. J Cell Physiol. 1998;176:206-215.
15. Yu Q, Stamenkovic I. Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev. 1999;13:35-48.
16. Stefanidakis M, Ruohtula T, Borregaard N, et al. Intracellular and cell surface localization of a complex between αMβ2 integrin and promatrix metalloproteinase-9 progelatinase in neutrophils. J Immunol. 2004;172:7060-7068.
17. Olson MW, Toth M, Gervasi DC, et al. High affinity binding of latent matrix metalloproteinase-9 to the alpha2(IV) chain of collagen IV. J Biol Chem. 1998;273:10672-10681.
18. Monferran S, Paupert J, Dauvillier S, et al. The membrane form of the DNA repair protein Ku interacts at the cell surface with metalloproteinase 9. EMBO J. 2004;23:3758-3768.
19. Yu Q, Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-β and promotes tumor invasion and angiogenesis. Genes Dev. 2000;14:163-176.
20. Oh J, Takahashi R, Kondo S, et al. The membrane-anchored MMP inhibitor RECK is a key regulador of extracellular matrix integrity and angiogenesis. Cell. 2001;107:789-800.
21. Hahn-Dantona E, Ruiz JF, Bornstein P, Strickland DK. The low density lipoprotein receptor-related protein modulates levels of matrix metalloproteinase 9 (MMP-9) by mediating its cellular catabolism. J Biol Chem. 2001;276:15498-15503.
22. Binet JL, Auqier A, Dighiero G, el al. A new prognostic classification of chronic lymphocytic leukemia derived from a multivariate analysis. Cancer. 1981;48:198-206.
23. Rai KR, Sawitsky A, Cronkite EP, et al. Clinical staging of chronic lymphocytic leukemia. Blood. 1975;46:219-234.
24. Hus I, Podhorecka M, Bojarska-Junak A, et al. The clinical significance of ZAP-70 and CD38 expression in B-cell chronic lymphocytic leukaemia. Ann Oncol. 2006;17:683-690.
25. Deaglio S, Vaisitti T, Aydin S, et al. CD38 and ZAP-70 are functionally linked and mark CLL cells with high migratory potential. Blood. 2007; 110:4012-4021.
26. Pulido R, Elices MJ, Campanero MR, et al. Functional evidence for three distinct and independently inhibitable adhesion activities mediated by the human integrin VLA-4: correlation with distinct α4 epitopes. J Biol Chem. 1991;266:10241-10245.
27. Humphries MJ, Komoriya A, Akiyama SK, et al. Identification of two distinct regions of the type III connecting segment of human plasma fibronectin that promote cell type specific adhesion. J Biol Chem. 1987;262:6886-6892.
28. Garcia-Pardo A, Wayner EA, Carter WG, Ferreira OC Jr. Human B lymphocytes define an alternative mechanism of adhesion to fibronectin. The interaction of the α4β1 integrin with the LHGPEILDVPST sequence of the type III connecting segment is sufficient to promote cell attachment. J Immunol. 1990;144:3361-3366.
29. Vincent AM, Cawley JC, Burthem J. Integrin function in chronic lymphocytic leukemia. Blood. 1996;87:4780-4788.
30. De la Fuente MT, Casanova B, García-Gila M, et al. Fibronectin interaction with α4β1 integrin prevents apoptosis in B cell chronic lymphocytic leukemia: correlation with Bcl-2 and Bax. Leukemia. 1999;13:266-274.
31. Van den Steen PE, Van Aelst I, Hvidberg V, et al. The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors. J Biol Chem. 2006;281:18626-18637.
32. Irving JA, Cain G, Howard M, et al. The role of alternative splicing of the adhesion molecule, CD44, in lymphoid malignancy. J Clin Pathol. 2007;51:776-780.
33. Stefanidakis M, Koivunen E. Cell-surface association between matrix metalloproteinases and integrins: role of the complexes in leukocyte migration and cancer progression. Blood. 2006;108:1441-1450.
34. Björklund M, Koivunen E. Gelatinase-mediated migration and invasion of cancer cells. Biochim Biophys Acta. 2005;1755:37-69.
35. Pittner BT, Shanafelt TD, Kay NE, Jelinek DF. CD38 expression levels in chronic lymphocytic leukemia B cells are associated with activation marker expression and differential responses to interferon stimulation. Leukemia. 2005;19:2264-2272.
36. Zucchetto A, Bomben R, Dal Bo M, et al. CD49d in B-cell chronic lymphocytic leukemia: correlated expression with CD38 and prognostic relevance. Leukemia. 2006;20:523-525.
37. Naor D, Vogt Sionov R, Ish-Shalom D. CD44: structure, function, and association with the malignant process. Adv Cancer Res. 1997;71:241-319.
38. Ponta H, Sherman L, Herrlich PA. CD44: from adhesion molecules to signalling regulators. Nature Rev Mol Cell Biol. 2003;4:33-45.
39. Zarcone D, De Rossi G, Tenca C, et al. Functional and clinical relevance of CD44 variant isoform expression on B-cell chronic lymphocytic leukemia cells. Haematologica. 1998;83:1088-1098.
40. De Rossi G, Marroni P, Paganuzzi M, et al. Increased serum levels of soluble CD44 standard, but not of variants isoforms v5 and v6, in B cell chronic lymphocytic leukemia. Leukemia. 1997; 11:134-141.
41. Eisterer W, Bechter O, Soderberg O, et al. Elevated levels of soluble CD44 are associated with advanced disease and in vitro proliferation of neoplastic lymphocytes in B-cell chronic lymphocytic leukemia. Leukemia Res. 2004;28:1043-1051.
42. Karadag A, Fedarko NS, Fisher LW. Dentin matrix protein 1 enhances invasion potentiaal of colon cancer cells by bridging matrix metalloproteinase-9 to integrins and CD44. Cancer Res. 2005;65:11545-11552.
43. Desai B, Rogers MJ, Chellaiah MA. Mechanisms of osteopontin and CD44 as metastatic principles in prostate cancer cells. Mol Cancer. 2007;6:1-16.
44. Cauwe B, Van den Steen PE, Opdenakker G. The biochemical, biological, and pathological kaleidoscope of cell surface substrates processed by matrix metalloproteinases. Crit Rev Biochem Mol Biol. 2007;42:113-185.
45. Deryugina EI, Zijlstra A, Partidge JJ, et al. Unexpected effect of matrix metalloproteinase downregulation on vascular intravasation and metastasis of human fibrosarcoma cells selected in vivo for high rates of dissemination. Cancer Res. 2005;65:10959-10969.
46. Pozzi A, Moberg PE, Miles LA, et al. Elevated matrix metalloprotease and angiostatin levels in integrin α1 knockout mice cause reduced tumor vascularization. Proc Natl Acad Sci U S A. 2000; 97:2202-2207.
47. Pozzi A, LeVine WF, Gadner HA. Low plasma levels of matrix metalloproteinase 9 permit increased tumor angiogenesis. Oncogene. 2002; 21:272-281.
48. Mira E, Lacalle RA, Buesa JM, et al. Secreted MMP9 promotes angiogenesis more efficiently than constitutively active MMP9 bound to the tumor cell surface. J Cell Science. 2004;117:1847-1856.
49. McQuibban GA, Butler GS, Gong J-H, et al. Matrix metalloproteinase activity inactivates the CXC chemokine stromal cell-derived factor-1. J Biol Chem. 2001;276:43503-43508.