메뉴 건너뛰기




Volumn 55, Issue 10, 2006, Pages 1247-1257

The immunologically active site of prothymosin α is located at the carboxy-terminus of the polypeptide. Evaluation of its in vitro effects in cancer patients

Author keywords

Anticancer activity; Cell proliferation; Cytotoxicity; Immune responses; Prothymosin fragmentation

Indexed keywords

CASPASE; CELL ADHESION MOLECULE; INTERLEUKIN 2 RECEPTOR ALPHA; PERFORIN; POLYPEPTIDE; PROTHYMOSIN ALPHA;

EID: 33745635719     PISSN: 03407004     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00262-005-0108-4     Document Type: Article
Times cited : (29)

References (48)
  • 2
    • 0023069056 scopus 로고
    • α-Thymosins: Relationships in structure, distribution, and function
    • Haritos AA (1987) α-Thymosins: relationships in structure, distribution, and function. Isozymes Curr Top Biol Med Res 14:123-152
    • (1987) Isozymes Curr Top Biol Med Res , vol.14 , pp. 123-152
    • Haritos, A.A.1
  • 3
    • 0022997102 scopus 로고
    • The human prothymosin α gene is polymorphic and induced upon growth stimulation: Evidence using a cloned cDNA
    • USA
    • Eschenfeldt WH, Berger SL (1986) The human prothymosin α gene is polymorphic and induced upon growth stimulation: evidence using a cloned cDNA. Proc Natl Acad Sci USA 83:9403-9407
    • (1986) Proc Natl Acad Sci , vol.83 , pp. 9403-9407
    • Eschenfeldt, W.H.1    Berger, S.L.2
  • 4
    • 0033783289 scopus 로고    scopus 로고
    • Fifteen years of prothymosin alpha: Contradictory past and new horizons
    • Pineiro A, Cordero OJ, Nogueira M (2000) Fifteen years of prothymosin alpha: contradictory past and new horizons. Peptides 21:1433-1446
    • (2000) Peptides , vol.21 , pp. 1433-1446
    • Pineiro, A.1    Cordero, O.J.2    Nogueira, M.3
  • 6
    • 0026099022 scopus 로고
    • The MYC protein activates transcription of the α-prothymosin gene
    • Eilers M, Schirm S, Bishop JM (1991) The MYC protein activates transcription of the α-prothymosin gene. EMBO J 10:133-141
    • (1991) EMBO J , vol.10 , pp. 133-141
    • Eilers, M.1    Schirm, S.2    Bishop, J.M.3
  • 7
    • 0038627113 scopus 로고    scopus 로고
    • A 180-kDa protein kinase seems to be responsible for the phosphorylation of prothymosin α observed in proliferating cells
    • Perez-Estevez A, Diaz-Jullien C, Covelo G, Salgueiro MT, Freire M (1997) A 180-kDa protein kinase seems to be responsible for the phosphorylation of prothymosin α observed in proliferating cells. J Biol Chem 272:10506-10513
    • (1997) J Biol Chem , vol.272 , pp. 10506-10513
    • Perez-Estevez, A.1    Diaz-Jullien, C.2    Covelo, G.3    Salgueiro, M.T.4    Freire, M.5
  • 9
    • 0030570995 scopus 로고    scopus 로고
    • Prothymosin α binds histones in vitro and shows activity in nucleosome assembly assay
    • Diaz-Jullien C, Perez-Estevez A, Covelo G, Freire M (1996) Prothymosin α binds histones in vitro and shows activity in nucleosome assembly assay. Biochim Biophys Acta 1296:219-227
    • (1996) Biochim Biophys Acta , vol.1296 , pp. 219-227
    • Diaz-Jullien, C.1    Perez-Estevez, A.2    Covelo, G.3    Freire, M.4
  • 10
    • 0036245548 scopus 로고    scopus 로고
    • Prothymosin α interacts with the CREB-binding protein and potentiates transcription
    • Karetsou Z, Kretsovali A, Murphy C, Tsolas O, Papamarcaki T (2002) Prothymosin α interacts with the CREB-binding protein and potentiates transcription. EMBO Rep 3:361-366
    • (2002) EMBO Rep , vol.3 , pp. 361-366
    • Karetsou, Z.1    Kretsovali, A.2    Murphy, C.3    Tsolas, O.4    Papamarcaki, T.5
  • 11
    • 0030704349 scopus 로고    scopus 로고
    • Prothymosin α in vivo contains phosphorylated glutamic acid residues
    • Trumbore MW, Wang RH, Enkemann SA, Berger SL (1997) Prothymosin α in vivo contains phosphorylated glutamic acid residues. J Biol Chem 272:26394-26404
    • (1997) J Biol Chem , vol.272 , pp. 26394-26404
    • Trumbore, M.W.1    Wang, R.H.2    Enkemann, S.A.3    Berger, S.L.4
  • 12
    • 0033942157 scopus 로고    scopus 로고
    • Modulation of histone acetyltransferase activity through interaction of Epstein-Barr nuclear antigen 3C with prothymosin alpha
    • Cotter MA, Robertson ES (2000) Modulation of histone acetyltransferase activity through interaction of Epstein-Barr nuclear antigen 3C with prothymosin alpha. Mol Cell Biol 20:5722-5735
    • (2000) Mol Cell Biol , vol.20 , pp. 5722-5735
    • Cotter, M.A.1    Robertson, E.S.2
  • 16
    • 0031442376 scopus 로고    scopus 로고
    • Prothymosin α1 effects, in vitro, on the antitumor activity and cytokine production of blood monocytes from colorectal tumor patients
    • Garbin F, Eckert K, Immenschuh P, Kreuser ED, Maurer HR (1997) Prothymosin α1 effects, in vitro, on the antitumor activity and cytokine production of blood monocytes from colorectal tumor patients. Int J Immunopharmacol 19:323-332
    • (1997) Int J Immunopharmacol , vol.19 , pp. 323-332
    • Garbin, F.1    Eckert, K.2    Immenschuh, P.3    Kreuser, E.D.4    Maurer, H.R.5
  • 20
    • 0031283476 scopus 로고    scopus 로고
    • Prothymosin α1 effects in vitro on chemotaxis, cytotoxicity and oxidative response of neutrophils from melanoma, colorectal and breast tumor patients
    • Heidecke H, Eckert K, Schulze-Forster K (1997) Prothymosin α1 effects in vitro on chemotaxis, cytotoxicity and oxidative response of neutrophils from melanoma, colorectal and breast tumor patients. Int J Immunopharmacol 19:413-420
    • (1997) Int J Immunopharmacol , vol.19 , pp. 413-420
    • Heidecke, H.1    Eckert, K.2    Schulze-Forster, K.3
  • 21
    • 0033964721 scopus 로고    scopus 로고
    • Functional discontinuities in prothymosin α caused by caspase cleavage in apoptotic cells
    • Enkemann SA, Wang RH, Trumbore MW, Berger SL (2000) Functional discontinuities in prothymosin α caused by caspase cleavage in apoptotic cells. J Cell Physiol 182:256-268
    • (2000) J Cell Physiol , vol.182 , pp. 256-268
    • Enkemann, S.A.1    Wang, R.H.2    Trumbore, M.W.3    Berger, S.L.4
  • 25
    • 0028039092 scopus 로고
    • Peripheral T-cell lymphomas. Immunoregulatory cytokine (interleukin-2, interleukin-4, and interferon-γ) abnormalities and autologous mixed lymphocyte reaction
    • Raziuddin S, Abu-Eshy S, Sheikka A (1994) Peripheral T-cell lymphomas. Immunoregulatory cytokine (interleukin-2, interleukin-4, and interferon-γ) abnormalities and autologous mixed lymphocyte reaction. Cancer 74:2843-2849
    • (1994) Cancer , vol.74 , pp. 2843-2849
    • Raziuddin, S.1    Abu-Eshy, S.2    Sheikka, A.3
  • 26
    • 1842734249 scopus 로고    scopus 로고
    • Thymosins: Chemistry and biological properties in health and disease
    • Goldstein AL, Badamchian M (2004) Thymosins: chemistry and biological properties in health and disease. Expert Opin Biol Ther 4:559-573
    • (2004) Expert Opin Biol Ther , vol.4 , pp. 559-573
    • Goldstein, A.L.1    Badamchian, M.2
  • 28
    • 0030831307 scopus 로고    scopus 로고
    • Interleukin-2-activated killer cell activity in colorectal tumor patients: Evaluation of in vitro effects by prothymosin α1
    • Eckert K, Gruenberg E, Immenschuh P, Gabrin F, Kreuser ED, Maurer HR (1997) Interleukin-2-activated killer cell activity in colorectal tumor patients: evaluation of in vitro effects by prothymosin α1. J Cancer Res Clin Oncol 123:420-428
    • (1997) J Cancer Res Clin Oncol , vol.123 , pp. 420-428
    • Eckert, K.1    Gruenberg, E.2    Immenschuh, P.3    Gabrin, F.4    Kreuser, E.D.5    Maurer, H.R.6
  • 29
    • 0028670530 scopus 로고
    • Thymosin α1 effects, in vitro, on lymphokine-activated killer cells from patients with primary immunodeficiencies: Preliminary results
    • Eckert K, Schmitt M, Gabrin F, Wahn U, Maurer HR (1994) Thymosin α1 effects, in vitro, on lymphokine-activated killer cells from patients with primary immunodeficiencies: preliminary results. Int J Immunopharmacol 16:1019-1025
    • (1994) Int J Immunopharmacol , vol.16 , pp. 1019-1025
    • Eckert, K.1    Schmitt, M.2    Gabrin, F.3    Wahn, U.4    Maurer, H.R.5
  • 30
    • 0028670928 scopus 로고
    • Prothymosin α augments deficient antitumor activity of monocytes from melanoma patients in vitro
    • Garbin F, Eckert K, Buttner P, Garbe C, Maurer HR (1994) Prothymosin α augments deficient antitumor activity of monocytes from melanoma patients in vitro. Anticancer Res 14:2405-2411
    • (1994) Anticancer Res , vol.14 , pp. 2405-2411
    • Garbin, F.1    Eckert, K.2    Buttner, P.3    Garbe, C.4    Maurer, H.R.5
  • 31
    • 0035496603 scopus 로고    scopus 로고
    • Natural killer cells, viruses and cancer
    • Cerwenka A, Lanier LL (2001) Natural killer cells, viruses and cancer. Nat Rev Immunol 1:41-49
    • (2001) Nat Rev Immunol , vol.1 , pp. 41-49
    • Cerwenka, A.1    Lanier, L.L.2
  • 32
    • 0023900714 scopus 로고
    • Enhancement of human T lymphocyte functions by prothymosin α. I. Augmentation of mixed lymphocyte culture reactions and soluble protein-induced proliferative responses
    • Baxevanis CN, Reclos GJ, Panneerselvam C, Papamichail M (1988) Enhancement of human T lymphocyte functions by prothymosin α. I. Augmentation of mixed lymphocyte culture reactions and soluble protein-induced proliferative responses. Immunopharmacology 15:73-84
    • (1988) Immunopharmacology , vol.15 , pp. 73-84
    • Baxevanis, C.N.1    Reclos, G.J.2    Panneerselvam, C.3    Papamichail, M.4
  • 33
    • 0027407824 scopus 로고
    • Prothymosin α restores depressed allogeneic cell-mediated lympholysis and natural-killer-cell activity in patients with cancer
    • Baxevanis CN, Reclos GJ, Papamichail M (1993) Prothymosin α restores depressed allogeneic cell-mediated lympholysis and natural-killer-cell activity in patients with cancer. Int J Cancer 53:264-268
    • (1993) Int J Cancer , vol.53 , pp. 264-268
    • Baxevanis, C.N.1    Reclos, G.J.2    Papamichail, M.3
  • 34
    • 0024598760 scopus 로고
    • Isolation and partial sequencing of the human prothymosin α gene family. Evidence against export of the gene products
    • Eschenfeldt WH, Manrow RE, Krug MS, Berger SL (1989) Isolation and partial sequencing of the human prothymosin α gene family. Evidence against export of the gene products. J Biol Chem 264:7546-7555
    • (1989) J Biol Chem , vol.264 , pp. 7546-7555
    • Eschenfeldt, W.H.1    Manrow, R.E.2    Krug, M.S.3    Berger, S.L.4
  • 36
    • 0028300257 scopus 로고
    • Prothymosin α receptors on peripheral blood mononuclear cells
    • Cordero OJ, Sarandeses C, Nogueira M (1994) Prothymosin α receptors on peripheral blood mononuclear cells. FEBS Lett 341:23-27
    • (1994) FEBS Lett , vol.341 , pp. 23-27
    • Cordero, O.J.1    Sarandeses, C.2    Nogueira, M.3
  • 39
    • 0024491478 scopus 로고
    • Synergy of human recombinant interleukin 1 with interleukin 2 in the generation of lymphokine-activated killer cells
    • Crump WL, Owen-Schaub LB, Grimm EA (1989) Synergy of human recombinant interleukin 1 with interleukin 2 in the generation of lymphokine-activated killer cells. Cancer Res 49:149-153
    • (1989) Cancer Res , vol.49 , pp. 149-153
    • Crump, W.L.1    Owen-Schaub, L.B.2    Grimm, E.A.3
  • 40
    • 0031416295 scopus 로고    scopus 로고
    • Prothymosin α1 enhances the interleukin-2 activated killer cell adhesion to and immunotoxicity against docetaxel-treated HT-29 colon carcinoma cells in vitro
    • Gruenberg E, Eckert K, Maurer R (1997) Prothymosin α1 enhances the interleukin-2 activated killer cell adhesion to and immunotoxicity against docetaxel-treated HT-29 colon carcinoma cells in vitro. Int J Thymol 5:415-423
    • (1997) Int J Thymol , vol.5 , pp. 415-423
    • Gruenberg, E.1    Eckert, K.2    Maurer, R.3
  • 41
    • 0027368830 scopus 로고
    • Role of natural killer cells in cancer
    • Pross HF, Lotzova E (1993) Role of natural killer cells in cancer. Nat Immun 12:279-292
    • (1993) Nat Immun , vol.12 , pp. 279-292
    • Pross, H.F.1    Lotzova, E.2
  • 42
    • 0042208329 scopus 로고    scopus 로고
    • Expression of functionally relevant cell surface markers in dibutyltin-exposed human natural killer cells
    • Odman-Ghazi SO, Hatcher F, Whalen MM (2003) Expression of functionally relevant cell surface markers in dibutyltin-exposed human natural killer cells. Chem Biol Interact 146:1-18
    • (2003) Chem Biol Interact , vol.146 , pp. 1-18
    • Odman-Ghazi, S.O.1    Hatcher, F.2    Whalen, M.M.3
  • 43
    • 0034651015 scopus 로고    scopus 로고
    • Soluble VCAM-1 binding to α4 integrins is cell-type specific and activation dependent and is disrupted during apoptosis in T cells
    • Rose DM, Cardarelli PM, Cobb RR, Ginsberg MH (2000) Soluble VCAM-1 binding to α4 integrins is cell-type specific and activation dependent and is disrupted during apoptosis in T cells. Blood 95:602-609
    • (2000) Blood , vol.95 , pp. 602-609
    • Rose, D.M.1    Cardarelli, P.M.2    Cobb, R.R.3    Ginsberg, M.H.4
  • 45
    • 0035176890 scopus 로고    scopus 로고
    • Retrovirus-mediated transfer of prothymosin gene inhibits tumor growth and prolongs survival in murine bladder cancer
    • Shiau AL, Lin PR, Chang MY, Wu CL (2001) Retrovirus-mediated transfer of prothymosin gene inhibits tumor growth and prolongs survival in murine bladder cancer. Gene Ther 8:1609-1617
    • (2001) Gene Ther , vol.8 , pp. 1609-1617
    • Shiau, A.L.1    Lin, P.R.2    Chang, M.Y.3    Wu, C.L.4
  • 48
    • 0037066427 scopus 로고    scopus 로고
    • The danger model: A renewed sense of self
    • Matzinger P (2002) The danger model: a renewed sense of self. Science 296:301-305
    • (2002) Science , vol.296 , pp. 301-305
    • Matzinger, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.