메뉴 건너뛰기




Volumn 20, Issue 6, 2003, Pages 889-896

Targeted proapoptotic LHRH-BH3 peptide

Author keywords

Apoptosis; BH3 peptide; Cancer; LHRH peptide

Indexed keywords

GLUTAMINYLHISTIDYLTRYPTOPHYLSERYLTYROSYLGLYCYLLEUCYLARGINYLPROLYLGLYCINE; GLUTAMINYLHISTIDYLTRYPTOPHYLSERYLTYROSYLGLYCYLLEUCYLARGINYLPROLYLGLYCYLG LYC YLMETHIONYLVALYLGLUTAMINYLGLYCYLGLUTAMINYLARGINYLLEUCYLISOLEUCYLALANYLISOLEUCYLA SPARTYLGLYCYLISOLEUCYLARGINYLASPARTYLASPARAGINYLTYROSYLARGININE; GLUTAMINYLHISTIDYLTRYPTOPHYLSERYLTYROSYLGLYCYLLEUCYLARGINYLPROLYLGLYCYLM ETH IONYLGLYCYLGLUTAMINYLVALYLGLYCYLARGINYLGLUTAMINYLLEUCYLALANYLISOLEUCYLISOLEUCYLG LYCYLASPARTYLASPARTYLISOLEUCYLASPARAGINYLARGINYLARGINYLTYROSINE; GONADORELIN; GONADORELIN RECEPTOR; HISTIDYLGLUTAMINYLSERYLTRYPTOPHYLGLYCYLTYROSYLARGINYLLEUCYLGLYCYLPROLYLM ETH IONYLGLYCYLGLUTAMINYLVALYLGLYCYLARGINYLGLUTAMINYLLEUCYLALANYLISOLEUCYLISOLEUCYLG LYCYLASPARTYLASPARTYLISOLEUCYLASPARAGINYLARGINYLARGINYLTYROSINE; METHIONYLGLYCYLGLUTAMINYLVALYLGLYCYLARGINYLGLUTAMINYLLEUCYLALANYLISOLEUC YLI SOLEUCYLGLYCYLASPARTYLASPARTYLISOLEUCYLASPARAGINYLARGINYLARGINYLTYROSINE; PEPTIDE DERIVATIVE; PROTEIN BCL 2; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

EID: 0038015452     PISSN: 07248741     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023839319950     Document Type: Article
Times cited : (73)

References (29)
  • 1
    • 0037092949 scopus 로고    scopus 로고
    • Constitutive nuclear factor-kappaB activity preserves homeostasis of quiescent mature lymphocytes and granulocytes by controlling the expression of distinct Bcl-2 family proteins
    • F. Bureau, A. Vanderplasschen, F. Jaspar, F. Minner, P. P. Pastoret, M. P. Merville, V. Bours, and P. Lekeux. Constitutive nuclear factor-kappaB activity preserves homeostasis of quiescent mature lymphocytes and granulocytes by controlling the expression of distinct Bcl-2 family proteins. Blood 99:3683-3691 (2002).
    • (2002) Blood , vol.99 , pp. 3683-3691
    • Bureau, F.1    Vanderplasschen, A.2    Jaspar, F.3    Minner, F.4    Pastoret, P.P.5    Merville, M.P.6    Bours, V.7    Lekeux, P.8
  • 2
    • 0034057320 scopus 로고    scopus 로고
    • Apoptosis in cancer
    • S. W. Lowe and A. W. Lin. Apoptosis in cancer. Carcinogenesis 21:485-495 (2000).
    • (2000) Carcinogenesis , vol.21 , pp. 485-495
    • Lowe, S.W.1    Lin, A.W.2
  • 3
    • 0032877668 scopus 로고    scopus 로고
    • Dysregulation of apoptosis in cancer
    • J. Reed. Dysregulation of apoptosis in cancer. J. Clin. Oncol. 17:2941-2953 (1999).
    • (1999) J. Clin. Oncol. , vol.17 , pp. 2941-2953
    • Reed, J.1
  • 4
    • 0033786057 scopus 로고    scopus 로고
    • Selective light-induced modulation of bcl-XL and bax expressions in indocyanine green-loaded U937 cells: Effects of continuous or intermittent photo-sensitization with low IR-light using a 805-nm diode laser
    • L. Varriale, E. Crescenzi, V. Paba, B. M. di Celso, and G. Palumbo. Selective light-induced modulation of bcl-XL and bax expressions in indocyanine green-loaded U937 cells: effects of continuous or intermittent photo-sensitization with low IR-light using a 805-nm diode laser. J. Photochem. Photobiol. B 57:66-75 (2000).
    • (2000) J. Photochem. Photobiol. B , vol.57 , pp. 66-75
    • Varriale, L.1    Crescenzi, E.2    Paba, V.3    Di Celso, B.M.4    Palumbo, G.5
  • 5
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • A. Gross, J. M. McDonnell, and S. Korsmeyer. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13:1899-1911 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.3
  • 6
    • 0033965412 scopus 로고    scopus 로고
    • Role of the BH3 (BCL-2 homology 3) domain in the regulation of apoptosis and BCL-2-related proteins
    • R. J. Lutz. Role of the BH3 (BCL-2 homology 3) domain in the regulation of apoptosis and BCL-2-related proteins. Biochem. Sci. Trans. 28:51-56 (2000).
    • (2000) Biochem. Sci. Trans. , vol.28 , pp. 51-56
    • Lutz, R.J.1
  • 7
    • 0037336279 scopus 로고    scopus 로고
    • Simultaneous modulation of multidrug resistance and antiapoptotic cellular defense by MDR1 and BCL-2 targeted antisense oligonucleotides enhances the anticancer efficacy of doxorubicin
    • R. I. Pakunlu, T. J. Cook, and T. Minko. Simultaneous modulation of multidrug resistance and antiapoptotic cellular defense by MDR1 and BCL-2 targeted antisense oligonucleotides enhances the anticancer efficacy of doxorubicin. Pharm. Res. 20:351-359 (2003).
    • (2003) Pharm. Res. , vol.20 , pp. 351-359
    • Pakunlu, R.I.1    Cook, T.J.2    Minko, T.3
  • 8
    • 0038377441 scopus 로고    scopus 로고
    • Enhancing the efficacy of chemotherapeutic drugs by the suppression of anti-apoptotic cellular defense
    • in press
    • T. Minko, S. S. Dharap, and A. T. Fabbricatore. Enhancing the efficacy of chemotherapeutic drugs by the suppression of anti-apoptotic cellular defense. Cancer Detect. Prev. in press
    • Cancer Detect. Prev.
    • Minko, T.1    Dharap, S.S.2    Fabbricatore, A.T.3
  • 9
    • 0033531926 scopus 로고    scopus 로고
    • Bak BH3 peptides antagonize BCL-XL functions and induce apoptosis through cytochrome c-independent activation of caspases
    • E. Holinger, T. Chittenden, and R. J. Lutz. Bak BH3 peptides antagonize BCL-XL functions and induce apoptosis through cytochrome c-independent activation of caspases. J. Biol. Chem. 274:13298-13304 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 13298-13304
    • Holinger, E.1    Chittenden, T.2    Lutz, R.J.3
  • 12
    • 0036965115 scopus 로고    scopus 로고
    • Expression of gonadotropin-releasing hormone II (GnRH-II) receptor in human endometrial and ovarian cancer cells and effects of GnRH-II on tumor cell proliferation
    • C. Grundker, A. R. Gunthert, R. P. Millar, and G. Emons. Expression of gonadotropin-releasing hormone II (GnRH-II) receptor in human endometrial and ovarian cancer cells and effects of GnRH-II on tumor cell proliferation. J. Clin. Endocrinol. Metab. 87:1427-1430 (2002).
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 1427-1430
    • Grundker, C.1    Gunthert, A.R.2    Millar, R.P.3    Emons, G.4
  • 13
    • 0036182849 scopus 로고    scopus 로고
    • Expression of receptors for luteinizing hormone-releasing hormone in human ovarian and endometrial cancers: Frequency, autoregulation, and correlation with direct antiproliferative activity of luteinizing hormone-releasing hormone analogues
    • P. Volker, C. Grundker, O. Schmidt, K. D. Schulz, and G. Emons. Expression of receptors for luteinizing hormone-releasing hormone in human ovarian and endometrial cancers: frequency, autoregulation, and correlation with direct antiproliferative activity of luteinizing hormone-releasing hormone analogues. Am. J. Obstet. Gynecol. 186:171-179 (2002).
    • (2002) Am. J. Obstet. Gynecol. , vol.186 , pp. 171-179
    • Volker, P.1    Grundker, C.2    Schmidt, O.3    Schulz, K.D.4    Emons, G.5
  • 14
    • 0345367901 scopus 로고    scopus 로고
    • HPMA copolymer bound adriamycin overcomes MDR 1 gene encoded resistance in a human ovarian carcinoma cell line
    • T. Minko, P. Kopeckova, V. Pozharov, and J. Kopecek. HPMA copolymer bound adriamycin overcomes MDR1 gene encoded resistance in a human ovarian carcinoma cell line. J. Control. Release 54:223-233 (1998).
    • (1998) J. Control. Release , vol.54 , pp. 223-233
    • Minko, T.1    Kopeckova, P.2    Pozharov, V.3    Kopecek, J.4
  • 15
    • 0032766043 scopus 로고    scopus 로고
    • Comparison of the anticancer effect of free and HPMA copolymer-bound adriamycin in human ovarian carcinoma cells
    • T. Minko, P. Kopeckova, and J. Kopecek. Comparison of the anticancer effect of free and HPMA copolymer-bound adriamycin in human ovarian carcinoma cells. Pharm. Res. 16:986-996 (1999).
    • (1999) Pharm. Res. , vol.16 , pp. 986-996
    • Minko, T.1    Kopeckova, P.2    Kopecek, J.3
  • 16
    • 0035962380 scopus 로고    scopus 로고
    • Preliminary evaluation of caspase-dependent apoptosis signaling pathways of free and HPMA copolymer-bound doxorubicin in human ovarian carcinoma cells
    • T. Minko, P. Kopeckova, and J. Kopecek. Preliminary evaluation of caspase-dependent apoptosis signaling pathways of free and HPMA copolymer-bound doxorubicin in human ovarian carcinoma cells. J. Control. Release 71:227-237 (2001).
    • (2001) J. Control. Release , vol.71 , pp. 227-237
    • Minko, T.1    Kopeckova, P.2    Kopecek, J.3
  • 17
    • 0036354863 scopus 로고    scopus 로고
    • Enhancing the anticancer efficacy of camptothecin using biotinylated poly(ethyleneglycol) conjugates in sensitive and multidrug-resistant human ovarian carcinoma cells
    • T. Minko, P. V. Paranjpe, B. Qiu, A. Lallo, R. Won, S. Stein, and P. J. Sinko. Enhancing the anticancer efficacy of camptothecin using biotinylated poly(ethyleneglycol) conjugates in sensitive and multidrug-resistant human ovarian carcinoma cells. Cancer Chemother. Pharmacol. 50:143-150 (2002).
    • (2002) Cancer Chemother. Pharmacol. , vol.50 , pp. 143-150
    • Minko, T.1    Paranjpe, P.V.2    Qiu, B.3    Lallo, A.4    Won, R.5    Stein, S.6    Sinko, P.J.7
  • 19
    • 0036565880 scopus 로고    scopus 로고
    • Erythrocyte survival is promoted by plasma and suppressed by a Bak-derived BH3 peptide that interacts with membrane-associated Bcl-X(L)
    • M. Walsh, R. J. Lutz, T. G. Cotter, and R. O'Connor. Erythrocyte survival is promoted by plasma and suppressed by a Bak-derived BH3 peptide that interacts with membrane-associated Bcl-X(L). Blood 99:3439-3448 (2002).
    • (2002) Blood , vol.99 , pp. 3439-3448
    • Walsh, M.1    Lutz, R.J.2    Cotter, T.G.3    O'Connor, R.4
  • 20
    • 0034049291 scopus 로고    scopus 로고
    • Efficacy of the chemotherapeutic action of HPMA copolymer-bound doxorubicin in a solid tumor model of ovarian carcinoma
    • T. Minko, P. Kopeckova, and J. Kopecek. Efficacy of the chemotherapeutic action of HPMA copolymer-bound doxorubicin in a solid tumor model of ovarian carcinoma. Int. J. Cancer 86:108-117 (2000).
    • (2000) Int. J. Cancer , vol.86 , pp. 108-117
    • Minko, T.1    Kopeckova, P.2    Kopecek, J.3
  • 21
    • 0037193473 scopus 로고    scopus 로고
    • Intrinsic and extrinsic pathway signaling during neuronal apoptosis: Lessons from the analysis of mutant mice
    • G. V. Putcha, C. A. Harris, K. L. Moulder, R. M. Easton, C. B. Thompson, and E. M. Johnson Jr. Intrinsic and extrinsic pathway signaling during neuronal apoptosis: lessons from the analysis of mutant mice. J. Cell Biol. 157:441-453 (2002).
    • (2002) J. Cell Biol. , vol.157 , pp. 441-453
    • Putcha, G.V.1    Harris, C.A.2    Moulder, K.L.3    Easton, R.M.4    Thompson, C.B.5    Johnson E.M., Jr.6
  • 22
    • 0034637606 scopus 로고    scopus 로고
    • Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH 3 domain on Ser155
    • X. M. Zhou, Y. Liu, G. Payne, R. J. Lutz, and T. Chittenden. Growth factors inactivate the cell death promoter BAD by phosphorylation of its BH3 domain on Ser155. J. Biol. Chem. 275: 25046-25051 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 25046-25051
    • Zhou, X.M.1    Liu, Y.2    Payne, G.3    Lutz, R.J.4    Chittenden, T.5
  • 24
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • J. Chai, C. Du, J. W. Wu, S. Kyin, X. Wang, and Y. Shi. Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 406:855-862 (2000).
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3    Kyin, S.4    Wang, X.5    Shi, Y.6
  • 25
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • C. Du, M. Fang, Y. Li, L. Li, and X. Wang. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102:33-42 (2000).
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 26
    • 0035525594 scopus 로고    scopus 로고
    • A vision for the future?
    • M. Baum. A vision for the future? Br. J. Cancer 85(Suppl 2):15-18 (2001).
    • (2001) Br. J. Cancer , vol.85 , Issue.SUPPL. 2 , pp. 15-18
    • Baum, M.1
  • 27
    • 0036131189 scopus 로고    scopus 로고
    • The influence of luteinizing hormone-releasing hormone analog on serum leptin and body composition in women with solitary uterine myoma
    • M. Nowicki, G. Adamkiewicz, W. Bryc, and F. Kokot. The influence of luteinizing hormone-releasing hormone analog on serum leptin and body composition in women with solitary uterine myoma. Am. J. Obstet. Gynecol. 186:340-344 (2002).
    • (2002) Am. J. Obstet. Gynecol. , vol.186 , pp. 340-344
    • Nowicki, M.1    Adamkiewicz, G.2    Bryc, W.3    Kokot, F.4
  • 28
    • 0036204393 scopus 로고    scopus 로고
    • Down-regulation of proliferation and up-regulation of apoptosis by gonadotropin-releasing hormone agonist in cultured uterine leiomyoma cells
    • Y. Wang, H. Matsuo, O. Kurachi, and T. Maruo. Down-regulation of proliferation and up-regulation of apoptosis by gonadotropin-releasing hormone agonist in cultured uterine leiomyoma cells. Eur. J. Endocrinol. 146:447-456 (2002).
    • (2002) Eur. J. Endocrinol. , vol.146 , pp. 447-456
    • Wang, Y.1    Matsuo, H.2    Kurachi, O.3    Maruo, T.4
  • 29
    • 0036554706 scopus 로고    scopus 로고
    • Luteinizing hormone-releasing hormone agonist limits DU-145 prostate cancer growth by attenuating epidermal growth factor receptor signaling
    • A. Wells, J. C. Souto, J. Solava, J. Kassis, K. J. Bailey, and T. Turner. Luteinizing hormone-releasing hormone agonist limits DU-145 prostate cancer growth by attenuating epidermal growth factor receptor signaling. Clin. Cancer Res. 8:1251-1257 (2002).
    • (2002) Clin. Cancer Res. , vol.8 , pp. 1251-1257
    • Wells, A.1    Souto, J.C.2    Solava, J.3    Kassis, J.4    Bailey, K.J.5    Turner, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.