A transcriptionally permissive epigenetic landscape at the vasoactive intestinal peptide receptor-1 promoter suggests a euchromatin nuclear position in murine CD4 T cells

Regulatory Peptides

Volumn 158, Issue 1-3, 2009, Pages 68-76

  Benton, K D ^a   Hermann, R J ^a   Vomhof DeKrey, E E ^a   Haring, J S ^a   Van der Steen, T ^a   Smith, J ^a   Dovat, S ^b   Dorsam, G P ^a  

^a NORTH DAKOTA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

Euchromatin; Histone acetylation; Histone methylation; Neuropeptides; TCR signaling; VPAC1

Indexed keywords

CD3 ANTIGEN; COMPLEMENTARY DNA; DNA POLYMERASE; HISTONE; VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR 1;

ACETYLATION; ANIMAL CELL; ARTICLE; B LYMPHOCYTE; CD4+ T LYMPHOCYTE; CELL ISOLATION; CHROMATIN IMMUNOPRECIPITATION; CONTROLLED STUDY; DOWN REGULATION; EPIGENETICS; EUCHROMATIN; METHYLATION; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN MODIFICATION; STAINING;

ACETYLATION; ANIMALS; BASE SEQUENCE; CD4-POSITIVE T-LYMPHOCYTES; CELL NUCLEUS; CHROMATIN IMMUNOPRECIPITATION; DNA PRIMERS; DOWN-REGULATION; EPIGENESIS, GENETIC; EUCHROMATIN; METHYLATION; MICE; POLYMERASE CHAIN REACTION; RECEPTORS, VASOACTIVE INTESTINAL POLYPEPTIDE, TYPE I; RNA, MESSENGER; SIGNAL TRANSDUCTION; TRANSCRIPTION, GENETIC;

MURINAE;

EID: 70349731913     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.regpep.2009.08.010     Document Type: Article

References (46)

1. Delgado M., Pozo D., and Ganea D. The significance of vasoactive intestinal peptide in immunomodulation. Pharmacol Rev 56 (2004) 249-290
2. Dorsam G., Voice J., Kong Y., and Goetzl E.J. Vasoactive intestinal peptide mediation of development and functions of T lymphocytes. Ann N Y Acad Sci 921 (2000) 79-91
3. Nussdorfer G.G., and Malendowicz L.K. Role of VIP, PACAP, and related peptides in the regulation of the hypothalamo-pituitary-adrenal axis. Peptides 19 (1998) 1443-1467
4. Bellinger D.L., Lorton D., Brouxhon S., Felten S., and Felten D.L. The significance of vasoactive intestinal polypeptide (VIP) in immunomodulation. Adv Neuroimmunol 6 (1996) 5-27
5. Delgado M., Munoz-Elias E.J., Gomariz R.P., and Ganea D. VIP and PACAP inhibit IL-12 production in LPS-stimulated macrophages. Subsequent effect on IFNgamma synthesis by T cells. J Neuroimmunol 96 (1999) 167-181
6. Ganea D., and Delgado M. The neuropeptides VIP/PACAP and T cells: inhibitors or activators?. Curr Pharm Des 9 (2003) 997-1004
7. Wang H.Y., Jiang X.M., and Ganea D. The neuropeptides VIP and PACAP inhibit IL-2 transcription by decreasing c-Jun and increasing JunB expression in T cells. J Neuroimmunol 104 (2000) 68-78
8. Vomhof-DeKrey E.E., and Dorsam G.P. Stimulatory and suppressive signal transduction regulates vasoactive intestinal peptide receptor-1 (VPAC-1) in primary mouse CD4 T cells. Brain Behav Immun 22 (2008) 1024-1031
9. Delgado M., Martinez C., Johnson M.C., Gomariz R.P., and Ganea D. Differential expression of vasoactive intestinal peptide receptors 1 and 2 (VIP-R1 and VIP-R2) mRNA in murine lymphocytes. J Neuroimmunol 68 (1996) 27-38
10. Johnson M.C., McCormack R.J., Delgado M., Martinez C., and Ganea D. Murine T-lymphocytes express vasoactive intestinal peptide receptor 1 (VIP-R1) mRNA. J Neuroimmunol 68 (1996) 109-119
11. Vomhof-DeKrey E.E., Hermann R.J., Palmer M.F., Benton K.D., Sandy A.R., Dorsam S.T., and Dorsam G.P. TCR signaling and environment affect vasoactive intestinal peptide receptor-1 (VPAC-1) expression in primary mouse CD4 T cells. Brain Behav Immun 22 (2008) 1032-1040
12. Lara-Marquez M., O Dorisio M., O Dorisio T., Shah M., and Karacay B. Selective gene expression and activation-dependent regulation of vasoactive intestinal peptide receptor type 1 and type 2 in human T cells. J Immunol 166 (2001) 2522-2530
13. Quina A.S., Buschbeck M., and Di Croce L. Chromatin structure and epigenetics. Biochem Pharmacol 72 (2006) 1563-1569
14. Wyrick J.J., and Parra M.A. The role of histone H2A and H2B post-translational modifications in transcription: a genomic perspective. Biochim Biophys Acta 1789 (2009) 37-44
15. Luger K., Mader A.W., Richmond R.K., Sargent D.F., and Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389 (1997) 251-260
16. Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074-1080
17. Turner B.M. Histone acetylation and control of gene expression. J Cell Sci 99 Pt 1 (1991) 13-20
18. Zeng L., and Zhou M.M. Bromodomain: an acetyl-lysine binding domain. FEBS Lett 513 (2002) 124-128
19. Schneider R., Bannister A.J., Myers F.A., Thorne A.W., Crane-Robinson C., and Kouzarides T. Histone H3 lysine 4 methylation patterns in higher eukaryotic genes. Nat Cell Biol 6 (2004) 73-77
20. Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A., and Reinberg D. Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. Cell 125 (2006) 703-717
21. Park P.H., Lim R.W., and Shukla S.D. Involvement of histone acetyltransferase (HAT) in ethanol-induced acetylation of histone H3 in hepatocytes: potential mechanism for gene expression. Am J Physiol Gastrointest Liver Physiol 289 (2005) G1124-1136
22. Lee K.Y., Ito K., Hayashi R., Jazrawi E.P., Barnes P.J., and Adcock I.M. NF-kappaB and activator protein 1 response elements and the role of histone modifications in IL-1beta-induced TGF-beta1 gene transcription. J Immunol 176 (2006) 603-615
23. Vomhof-Dekrey E.E., and Dorsam G.P. Stimulatory and suppressive signal transduction regulates vasoactive intestinal peptide receptor-1 (VPAC-1) in primary mouse CD4 T cells. Brain Behav Immun (2008)
24. Rosenstein Y., Santana A., and Pedraza-Alva G. CD43, a molecule with multiple functions. Immunol Res 20 (1999) 89-99
25. Duan B., and Morel L. Role of B-1a cells in autoimmunity. Autoimmun Rev 5 (2006) 403-408
26. Kimata H., and Fujimoto M. Induction of IgA1 and IgA2 production in immature human fetal B cells and pre-B cells by vasoactive intestinal peptide. Blood 85 (1995) 2098-2104
27. Bartova E., Krejci J., Harnicarova A., Galiova G., and Kozubek S. Histone modifications and nuclear architecture: a review. J Histochem Cytochem 56 (2008) 711-721
28. Bernstein B.E., Kamal M., Lindblad-Toh K., Bekiranov S., Bailey D.K., Huebert D.J., McMahon S., Karlsson E.K., Kulbokas E.J., Gingeras T.R., Schreiber S.L., and Lander E.S. Genomic maps and comparative analysis of histone modifications in human and mouse. Cell 120 (2005) 169-181
29. Fujieda S., Waschek J.A., Zhang K., and Saxon A. Vasoactive intestinal peptide induces S(alpha)/S(mu) switch circular DNA in human B cells. J Clin Invest 98 (1996) 1527-1532
30. Kimata H., and Fujimoto M. Vasoactive intestinal peptide specifically induces human IgA1 and IgA2 production. Eur J Immunol 24 (1994) 2262-2265
31. Schubeler D., MacAlpine D.M., Scalzo D., Wirbelauer C., Kooperberg C., van Leeuwen F., Gottschling D.E., O Neill L.P., Turner B.M., Delrow J., Bell S.P., and Groudine M. The histone modification pattern of active genes revealed through genome-wide chromatin analysis of a higher eukaryote. Genes Dev 18 (2004) 1263-1271
32. Bannister A.J., Zegerman P., Partridge J.F., Miska E.A., Thomas J.O., Allshire R.C., and Kouzarides T. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410 (2001) 120-124
33. Dorsam G., and Goetzl E.J. Vasoactive intestinal peptide receptor-1 (VPAC-1) is a novel gene target of the hemolymphopoietic transcription factor Ikaros. J Biol Chem 277 (2002) 13488-13493
34. Ronni T., Payne K.J., Ho S., Bradley M.N., Dorsam G., and Dovat S. Human Ikaros function in activated T cells is regulated by coordinated expression of its largest isoforms. J Biol Chem 282 (2007) 2538-2547
35. Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R., and Georgopoulos K. Ikaros DNA-binding proteins direct formation of chromatin remodeling complexes in lymphocytes. Immunity 10 (1999) 345-355
36. Koipally J., Kim J., Jones B., Jackson A., Avitahl N., Winandy S., Trevisan M., Nichogiannopoulou A., Kelley C., and Georgopoulos K. Ikaros chromatin remodeling complexes in the control of differentiation of the hemo-lymphoid system. Cold Spring Harb Symp Quant Biol 64 (1999) 79-86
37. Koipally J., Renold A., Kim J., and Georgopoulos K. Repression by Ikaros and Aiolos is mediated through histone deacetylase complexes. EMBO J 18 (1999) 3090-3100
38. Koipally J., and Georgopoulos K. Ikaros-CtIP interactions do not require C-terminal binding protein and participate in a deacetylase-independent mode of repression. J Biol Chem 277 (2002) 23143-23149
39. Koipally J., and Georgopoulos K. Ikaros interactions with CtBP reveal a repression mechanism that is independent of histone deacetylase activity. J Biol Chem 275 (2000) 19594-19602
40. Denslow S.A., and Wade P.A. The human Mi-2/NuRD complex and gene regulation. Oncogene 26 (2007) 5433-5438
41. Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H., Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P., Bannister A.J., and Kouzarides T. Histone deimination antagonizes arginine methylation. Cell 118 (2004) 545-553
42. Li B., Carey M., and Workman J.L. The role of chromatin during transcription. Cell 128 (2007) 707-719
43. Sims R.J., Millhouse S., Chen C.F., Lewis B.A., Erdjument-Bromage H., Tempst P., Manley J.L., and Reinberg D. Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. Mol Cell 28 (2007) 665-676
44. Kleinmann E., Geimer Le Lay A.S., Sellars M., Kastner P., and Chan S. Ikaros represses the transcriptional response to notch signaling in T-cell development. Mol Cell Biol 28 (2008) 7465-7475
45. Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
46. Ceraudo E., Tan Y.V., Nicole P., Couvineau A., and Laburthe M. The N-terminal parts of VIP and antagonist PG97-269 physically interact with different regions of the human VPAC1 receptor. J Mol Neurosci 36 (2008) 245-248