CD11c Integrin Gene Promoter Activity During Myeloid Differentiation

References

• Hynes R. O. Integrins: versatility, modulation and signalling in cell adhesion. Cell 1992; 69: 11–25
   PubMed Web of Science ®Google Scholar
• van der Vieren M., Trong H. L., Wood C. L., Moore P. F., Staunton D. E., St John T., Gallatin W. M. A novel leukointegrin, αdβ2, binds preferentially to ICAM‐3. Immunity 1995; 3: 683–690
   PubMed Web of Science ®Google Scholar
• Bilsland C. A., Diamond M. S., Springer T. A. The leukocyte integrin p150, 95 (CD11c/CD18) as a receptor for iC3b. Activation by a heterologous beta subunit and localization of a ligand recognition site to the I domain. J. Immunol. 1994; 152: 4582–4589
   PubMed Web of Science ®Google Scholar
• Loike J. D., Sodeik B., Cao L., Leucona S., Wettz J. I., Detmers P. A., Silverstein S. C. CD11c/CD18 on neutrophils recognizes a domain at the Nterminus of the A alpha chain of fibrinogen. Proc. Natl. Acad. Sci. USA 1991; 88: 1044–1048
   PubMed Web of Science ®Google Scholar
• Postigo A. A., Corbi A. L., Sanchez‐Madrid F., De Landazuri M. O. Regulated expression and function of CD11c/CD18 integrin on human B lymphocytes. Relation between attachment to fibrinogen and triggering of proliferation through CD11c/CD18. J. Exp. Med. 1991; 174: 1313–1322
   PubMed Web of Science ®Google Scholar
• Diamond M. S., Alon R., Parkos C. A., Quinn M. T., Springer T. A. Heparin is an adhesive ligand for the leukocyte integrin Mac‐1 (CD11b/CD18). J. Cell. Biol. 1995; 130: 1473–1482
   PubMed Web of Science ®Google Scholar
• Ingalls R. R., Golenbock D. T. CD11c/CD18, a transmembrane signaling receptor for lipopolysaccharide. J. Exp. Med. 1995; 181: 1473–1479
   PubMed Web of Science ®Google Scholar
• Keizer G. D., te Velde A. A., Schwarting R., Figdor C. G., de Vries J. Role of p150, 95 in adhesion, migration, chemotaxis and phagocytosis of human monocytes. Eur. J. Immunol. 1987; 17: 1317–1322
   PubMed Web of Science ®Google Scholar
• Keizer G. D., Borst J., Visser W., Schwarting R., de Vries J., Figdor C. G. Membrane glycoprotein p150, 95 of human cytotoxic T cell clones is involved in conjugate formation with target cells. J. Immunol. 1987; 138: 3130–3136
   PubMed Web of Science ®Google Scholar
• Stacker S. A., Springer T. A. Leukocyte integrin p150, 95 (CD11c/CD18) functions as an adhesion molecule binding to a counter‐receptor on stimulated endothelium. J. Immunol. 1991; 146: 648–655
   PubMed Web of Science ®Google Scholar
• Krieger M., Herz J. Structures and functions of multiligand lipoprotein receptors: macrophage scavenger receptors and LDL receptor‐related protein (LRP). Annu. Rev. Biochem. 1994; 63: 601–637
   PubMed Web of Science ®Google Scholar
• Davis G. E. The Mac‐1 and p150.95 beta 2 integrins bind denatured proteins to mediate leukocyte cell‐substrate adhesion. Exp. Cell. Res. 1992; 200: 242–252
   PubMed Web of Science ®Google Scholar
• Anderson D. C., Miller L. J., Schmalstieg F. C., Rothlein R., Springer T. A. Contributions of the Mac‐1 glycoprotein family to adherence‐dependent granulocyte functions: structure‐function assessments employing subunit‐specific monoclonal antibodies. J. Immunol. 1986; 137: 15–27
   PubMed Web of Science ®Google Scholar
• Nueda A., López‐Rodríguez C., Rubio M., Sotillos M., Postigo A., del Pozo M. A., Vega M., Corbí A. L. Hematopoietic cell type‐dependent regulation of leukocyte integrins functional activity. CD11b and CD11c expression inhibit LFA‐1‐dependent aggregation of differentiated U937 cells. Cell. Immunol. 1995; 164: 163–169
   PubMed Web of Science ®Google Scholar
• Hogg N., Takacs L., Palmer D. G., Selvendran Y., Allen C. The p150, 95 molecule is a marker of human mononuclear phagocytes: comparison with expression of class II molecules. Eur. J. Immunol. 1986; 16: 240–248
   PubMed Web of Science ®Google Scholar
• Chadburn A., Inghirami G., Knowles D. M. Hairy cell leukemia‐associated antigen LeuM5 (CD11c) is preferentially expressed by benign activated and neoplastic CD8 T cells. Am. J. Pathol. 1990; 136: 29–37
   PubMed Web of Science ®Google Scholar
• Huleatt J. W., Lefrancois L. Antigen‐driven induction of CDllc on intestinal intraepithelial lymphocytes and CD8+ T cells in vivo. J. Immunol. 1995; 154: 5684–5693
   PubMed Web of Science ®Google Scholar
• McFarland H. I., Nahill S. R., Maciaszek J. W., Welsh R. M. CD11b (Mac‐1): a marker for CD8+ cytotoxic T cell activation and memory in virus infection. J. Immunol. 1992; 149: 1326–1333
   PubMed Web of Science ®Google Scholar
• Hanson C. A., Gribbin T. E., Schnitzer B., Schlegelmilch J. A., Mitchell B. S., Stoolman L. M. CD11c (Leu‐M5) expression characterizes a B‐cell chronic lymphoproliferative disorder with features of both chronic lymphocytic leukemia and hairy cell leukemia. Blood 1990; 76: 2360–2367
   PubMed Web of Science ®Google Scholar
• Schwarting R., Stein H., Wang C. Y. The monoclonal antibodies ami S‐HCL 1 (anti Leu 14) and anti S‐HCL 3 (anti Leu M5) allow the diagnosis of hairy cell leukemia. Blood 1985; 65: 974–983
   PubMed Web of Science ®Google Scholar
• Macon W. R., Williams M. E., Greer J. P., Hammer R. D., Glick A. D., Collins R. D., Cousar J. B. Natural killer T‐cell lymphomas: aggressive lymphomas of T‐large granular lymphocytes. Blood 1996; 87: 1474–1483
   PubMed Web of Science ®Google Scholar
• Bellón T., López‐Rodríguez C., Vara A., Jochems G., Bernabeu C., Corbí A. L. Transcriptionally regulated expression of the p150, 95 and VLA‐4 integrins during myeloid cell differentiation. Eur. J. Immunol. 1994; 24: 41–47
   PubMed Web of Science ®Google Scholar
• Noti J. D., Reinemann B. C. The leukocyte integrin gene CD11c is transcriptionaily regulated during monocyte differentiation. Mol. Immunol. 1995; 32: 361–369
   PubMed Web of Science ®Google Scholar
• Kansas G. S., Muirhead M. J., Dailey M. O. Expression of the CD11/CD18, leukocyte adhesion molecule 1, and CD44 adhesion molecules during normal myeloid and eryhroid differentiation in humans. Blood 1990; 76: 2483–2492
   PubMed Web of Science ®Google Scholar
• Miller L. J., Schwarting R., Springer T. A. Regulated expression of the Mac‐1, LFA‐1, p 150, 95 glycoprotein family during leukocyte differentiation. J. Immunol. 1987; 137: 2891–2900
   Web of Science ®Google Scholar
• Dudley D., Baker D. M., Hickey M. J., Hickstein D. D. Expression of surface antigen and mRNA for the CD11c (αX, p150) subunit of the human leukocyte adherence receptor family in hematopoietic cells. Biochem. Biophys. Res. Commun. 1989; 160: 346–353
   PubMed Web of Science ®Google Scholar
• Cheng T., Erikcson‐Miller C. L., Li C., Cardier J., Wang Y., Dempsey J., Mogle M., Barbera E., Murphy M. J., Jr, Dai W. HIMeg‐1, a cell line derived from a CML patient, is capable of monocytic and megakaryocytic differentiation. Leukemia 1995; 9: 1257–1263
   PubMed Web of Science ®Google Scholar
• Öberg F., Botling J., Nilsson K. Functional antagonism between vitamin D3 and retinoic acid in the regulation of CD 14 and CD23 expression during monocytic differentiation of U‐937 cells. J. Immunol. 1993; 150: 3487–3495
   PubMed Web of Science ®Google Scholar
• Ehinger M., Bergh G., Olofsson T., Baldertorp B., Olsson Y., Gullberg U. Expression of the p53 tumor suppressor gene induces differentiation and promotes induction of differentiation by 1, 25‐dihydroxycholecalciferol in leukemic U‐937 cells. Blood 1996; 87: 1064–1074
   PubMed Web of Science ®Google Scholar
• Testa U., Masciulli R., Tritarelli E., Pustorino R., Mariani G., Martucci R., Barberi T., Camagna A., Valtieri M., Peschle C. Transforming growth factor‐β potentiates vitamin D3‐induced terminal monocytic differentiation of human leukemic cell lines. J. Immunol. 1993; 150: 2418–2430
   PubMed Web of Science ®Google Scholar
• Hewison M., Dabrowski M., Faulkner L., Hughson E., Vadher S., Rut A., Brickell P. M., O'Riordan J. L. H., Katz D. R. Transfection of vitamin D3 receptor cDNA into the monoblastoid cell line U937. J. Immunol. 1994; 153: 5709–5719
   PubMed Web of Science ®Google Scholar
• Lübbert M., Herrmann F., Koeffler H. P. Expression and regulation of myeloid‐specific genes in normal and leukemic myeloid cells. Blood 1991; 77: 909–924
   PubMed Web of Science ®Google Scholar
• Sundström C., Nilsson K. Establishment and characterization of a human histiocytic lymphoma cell line (U‐937). Int. J. Cancer 1976; 17: 565–577
   PubMed Web of Science ®Google Scholar
• Larsson L. G., Ivhed I., Gidlund M., Patterson U., Vennström B., Nilsson K. Phorbol ester‐induced terminal differentiation is inhibited in human U‐937 monoblastic cells expressing a v‐myc oncogene. Proc. Natl. Acad. Sci. USA 1988; 85: 2638–2642
   PubMed Web of Science ®Google Scholar
• Holt J. T., Redner R. L., Nienhuis A. W. An oligomer complementary to c‐myc mRNA inhibits proliferation of HL‐60 promyelocytic cells and induces differentiation. Mol. Cell. Biol 1988; 8: 963–973
   PubMed Web of Science ®Google Scholar
• Prieto J., Eklund A., Patarroyo M. Regulated expression of integrins and other adhesion molecules during differentiation of monocytes into macrophages. Cell. Immunol 1994; 156: 191–211
   PubMed Web of Science ®Google Scholar
• Huh H. Y., Pearce S. F., Yesner L. M., Schindler J. L., Silverstein R. L. Regulated expression of CD36 during monocyte‐to‐macrophage differentiation: potential role of CD36 in foam cell formation. Blood 1996; 87: 2020–2028
   PubMed Web of Science ®Google Scholar
• Corbí A. L., Garcia‐Aguilar J., Springer T. A. Genomic structure of an integrin alpha subunit, the leukocyte p150, 95 molecule. J. Biol. Chem. 1990; 265: 2782–2788
   PubMed Web of Science ®Google Scholar
• López‐Cabrera M., Nueda A., Vara A., Garcia‐Aguilar J., Tugores A., Corbi A. L. Characterization of the p150, 95 leukocyte integrin alpha subunit (CD11c) gene promoter. Identification of cis‐acting elements. J. Biol. Chem. 1993; 268: 1187–1193
   PubMed Web of Science ®Google Scholar
• Noti J. D., Reinemann B. C., Petrus M. N. Regulation of the leukocyte integrin gene CD11c is mediated by API and Ets transcription factors. Mol. Immunol 1996; 33: 115–127
   PubMed Web of Science ®Google Scholar
• López‐Rodríguez C., Chen H., Tenen D. G., Corbí A. L. Identification of Spl‐binding sites in the CD11c (p150, 95α) and CD11a (LFA‐1α) integrin subunit promoters and their involvement in the tissue‐specific expression of CD11c. Eur. J. Immunol 1995; 25: 3496–3503
   PubMed Web of Science ®Google Scholar
• López‐Rodríguez C., Kluin‐Nelemans H. C., Corbí A. L. The AP‐1 transcription factor regulates the basal and differentiation‐inducible transcription of the CD11c integrin gene. J. Immunol 1996; 156: 3780–3787
   PubMed Web of Science ®Google Scholar
• Smale S. T., Baltimore D. The “initiator” as a transcription control element. Cell 1989; 57: 103–113
   PubMed Web of Science ®Google Scholar
• Chen H. M., Pahl H. L., Scheibe R. J., Zhang D. E., Tenen D. G. The Spl transcription factor binds the CD11b promoter specifically in myeloid cells in vivo and is essential for myeloid‐specific promoter activity. J. Biol. Chem. 1993; 268: 8230–8239
   PubMed Web of Science ®Google Scholar
• Zhang D. ‐E., Hetherington C. J., Tan S., Dziennis S. E., Gonzalez D. A., Chen H. M., Tenen D. G. Spl is a critical factor for the monocyte specific expression of human CD14. J. Biol. Chem. 1994; 269: 11425–11434
   PubMed Web of Science ®Google Scholar
• Jane S. M., Gumucio D. L., Ney P. A., Cunningham J. M., Nienhuis A. W. Methylation‐enhanced binding of Sp1 to the stage selector element of the human γ‐globin gene promoter may regulate development specificity of expression. Mol. Cell. Biol. 1993; 13: 3272–3281
   PubMed Web of Science ®Google Scholar
• Spanopoulou E., Giguere V., Grosveld F. The functional domains of the murine Thy‐1 gene promoter. Mol. Cell. Biol 1991; 11: 2216–2228
   PubMed Web of Science ®Google Scholar
• Jackson S. P., Tjian R. O‐Glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation. Cell 1988; 55: 125–133
   PubMed Web of Science ®Google Scholar
• Bessereau J., Mendelzon D., LePoupon C., Fiszman M., Changeux J., Piette J. Muscle‐specific expression of the acetylcholine receptor a‐subunit gene requires both positive and negative interactions between myogenic factors, Sp1 and GBF factors. EMBO J. 1993; 12: 443–449
   PubMed Web of Science ®Google Scholar
• Chen J. L., Attardi L. D., Verrijzer C. P., Yokomori K., Tjian R. Assembly of recombinant TFIID reveales differential coactivator requirements for dictinct transcriptional activators. Cell 1994; 79: 93–105
   PubMed Web of Science ®Google Scholar
• Chiang C. ‐M., Roeder R. G. Cloning of an intrinsic human TFIID subunit that interacts with multiple transcriptional activators. Science 1995; 267: 531–536
   PubMed Web of Science ®Google Scholar
• Udvadia A. J., Templeton D. J., Horowitz J. M. Functional interactions between the retinoblastoma (Rb) protein and Sp‐family members: superactivation by Rb requires amino acids necessary for growth suppression. Proc. Natl Acad. Sci. USA 1995; 92: 3953–3957
   PubMed Web of Science ®Google Scholar
• Chen L. I., Nishinaka T., Kwan K., Kitabayashi Y., Yokoyama K., Fu Y. ‐H. F., Griinwald S., Chiu R. The retinoblastoma gene product RB stimulates Spl‐mediated transcription by liberating Spl from a negatuive regulator. Mol, Cell. Biol 1994; 14: 4380–4389
   PubMed Web of Science ®Google Scholar
• Udvadia A. J., Rogers K. T., Higgins P. D. R., Murata Y., Martin K. H., Humphrey P. A., Horowitz J. M. Sp‐1 binds promoter elements regulated by the RB protein and Sp‐1‐mediated transcription is stimulated by RB coexpression. Proc. Natl. Acad. Sci. USA 1993; 90: 3265–3269
   PubMed Web of Science ®Google Scholar
• Wang J. Y. J., Knudsen E. S., Welch P. J. The retinoblastoma tumor suppressor protein. Adv. Cancer Res. 1994; 64: 25–85
   PubMed Web of Science ®Google Scholar
• Liu M., Lee M. ‐H., Cohen M., Bommakanti M., Freedman L. P. Transcriptional activation of the Cdk inhibitor p21 by vitamin D3 leads to the induced differentiation of the myelomonocytic cell line U937. Genes Dew. 1996; 10: 142–153
   PubMed Web of Science ®Google Scholar
• Harper J. W., Elledge S. J. Cdk inhibitors in development and cancer. Curr. Opin. Genetics Dev. 1996; 6: 56–64
   PubMed Web of Science ®Google Scholar
• Zhang D. ‐E., Hetherington C. J., Gonzalez D. A., Chen H. ‐M., Tenen D. G. Regulation of CD14 expression during monocytic differentiation induced with 1α, 25‐dihy‐droxyvitamin D3. J. Immunol. 1994; 153: 3276–3284
   PubMed Web of Science ®Google Scholar
• Rubio M. A., López‐Rodríguez C., Nueda A., Aller P., Armesilla A. L., Vega M. A., Corbí A. L. Granulocyte/macrophage colony‐stimulating factor, phorbol ester, and sodium butyrate induce the CD11c integrin gene promoter activity during myeloid differentiation. Blood 1995; 86: 3715–3724
   PubMed Web of Science ®Google Scholar
• Colotta F., Wang J. M., Polentarutti N., Mantovani A. Expression of c‐fos protooncogene in normal human peripheral blood granulocytes. J. Exp. Med. 1987; 165: 1224–1229
   PubMed Web of Science ®Google Scholar
• Sariban E., Mitchell T., Rambaldi A., Kufe D. W. c‐sis but not c‐Fos gene expression is lineage‐specific in human myeloid cells. Blood 1988; 71: 488–493
   PubMed Web of Science ®Google Scholar
• Mavilio F., Testa U., Sposi N. M., Petrini M., Pelosi E., Bordignon C., Amadori C., Mandeli F., Peschle C. Selective expression of c‐fos protooncogene in human acute myelomonocytic and monocytic leukemias: a molecular marker of terminal differentiation. Blood 1987; 69: 160–164
   PubMed Web of Science ®Google Scholar
• Pinto A., Colletta G., del Vecchio L., Rosati R., Attadia V., Cimino R., Colombatti A. c‐fos oncogene expression in human hematopoietic malignancies is restricted to acute leukemias with monocytic phenotype and to subsets of B cell leukemias. Blood 1987; 70: 1450–1457
   PubMed Web of Science ®Google Scholar
• Angel P., Karin M. The role of Jun, Fos, and the AP‐I complex in cell proliferation and transformation. Biochim. Biophys. Acta. 1991; 1072: 129–157
   PubMed Web of Science ®Google Scholar
• Pahl H. L., Burn T. C., Tenen D. G. Optimization of transient transfection into human myeloid cell lines using a luciferase reporter gene. Exp. Hematol. 1991; 19: 1038–1041
   PubMed Web of Science ®Google Scholar
• Sato N., Sakamaki K., Terada N., Arai K. ‐I., Miyajima A. Signal transduction by the high‐affinity GM‐CSF receptor: two distinct cytoplasmic regions of the common β subunit responsible for different signaling. EMBO J. 1993; 12: 4181–4189
   PubMed Web of Science ®Google Scholar
• Roskelley C. D., Srebrow A., Bissell M. J. A hierarchy of ECM‐mediated signalling regulates tissue‐specific gene expression. Curr. Opin. Cell. Biol. 1995; 7: 736–747
   PubMed Web of Science ®Google Scholar