메뉴 건너뛰기




Volumn 30, Issue 12, 2009, Pages 2409-2417

In vitro binding and in vivo biodistribution studies of the neuroprotective peptide humanin using [125I]humanin derivatives

Author keywords

125I Radiolabeling; Humanin derivatives; In vitro cell binding; In vivo biodistribution; Metabolic stability; Neuroprotective peptides

Indexed keywords

HUMANIN; IODINE 125; QUINUCLIDINYL BENZILATE; TYROSINE; TYROSYLPROLYLALANYLGLYCYLALANYLSERYLARGINYLLEUCYLLEUCYLLEUCYLLEUCYLTHREONYLGLYCYLGLUTAMYLISOLEUCYLASPARTYLLEUCYLPROLINE; TYROSYLPROLYLALANYLGLYCYLALANYLSERYLARGINYLLEUCYLLEUCYLLEUCYLTHREONYLGLYCYLGLUTAMYLISOLEUCYLASPARTYLLEUCYLPROLINE; TYROSYLSERYLALANYLLEUCYLLEUCYLARGINYLSERYLISOLEUCYLPROLYLALANYLPROLYLALANYLGLYCYLALANYLSERYLARGINYLLEUCYLLEUCYLLEUCYLLEUCYLTHREONYLGLYCYLGLUTAMYLISOLEUCYLASPARTYLLEUCYLPROLINE; TYROSYLSERYLALANYLLEUCYLLEUCYLARGINYLSERYLISOLEUCYLPROLYLALANYLPROLYLALANYLGLYCYLALANYLSERYLARGINYLLEUCYLLEUCYLLEUCYLTHREONYLGLYCYLGLUTAMYLISOLEUCYLASPARTYLLEUCYLPROLINE; UNCLASSIFIED DRUG;

EID: 70450223711     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.peptides.2009.07.028     Document Type: Article
Times cited : (4)

References (38)
  • 2
    • 0028248322 scopus 로고
    • Labeling of peptides and proteins by radioiodination
    • Bailey G.S. Labeling of peptides and proteins by radioiodination. Methods Mol Biol 32 (1994) 441-448
    • (1994) Methods Mol Biol , vol.32 , pp. 441-448
    • Bailey, G.S.1
  • 3
    • 0025867084 scopus 로고
    • In vivo use of a radioiodinated somatostatin analogue: dynamics, metabolism, and binding to somatostatin receptor-positive tumors in man
    • Bakker W.H., Krenning E.P., Breeman W.A., Kooij P.P., Reubi J.-C., Koper J.W., et al. In vivo use of a radioiodinated somatostatin analogue: dynamics, metabolism, and binding to somatostatin receptor-positive tumors in man. J Nucl Med 32 (1991) 1184-1189
    • (1991) J Nucl Med , vol.32 , pp. 1184-1189
    • Bakker, W.H.1    Krenning, E.P.2    Breeman, W.A.3    Kooij, P.P.4    Reubi, J.-C.5    Koper, J.W.6
  • 4
    • 0031809440 scopus 로고    scopus 로고
    • Activity-dependent neurotrophic factor: structure-activity relationships of femtomolar-acting peptides
    • Brenneman D.E., Hauser J., Neale E., Rubinraut S., Fridkin M., Davidson A., et al. Activity-dependent neurotrophic factor: structure-activity relationships of femtomolar-acting peptides. J Pharmacol Exp Ther 285 (1998) 619-627
    • (1998) J Pharmacol Exp Ther , vol.285 , pp. 619-627
    • Brenneman, D.E.1    Hauser, J.2    Neale, E.3    Rubinraut, S.4    Fridkin, M.5    Davidson, A.6
  • 6
    • 27744563035 scopus 로고    scopus 로고
    • Development of a femtomolar-acting humanin derivative named colivelin by attaching activity-dependent neurotrophic factor to its N terminus: characterization of colivelin-mediated neuroprotection against Alzheimer's disease-relevant insults in vitro and in vivo
    • Chiba T., Yamada M., Hashimoto Y., Sato M., Sasabe J., Kita Y., et al. Development of a femtomolar-acting humanin derivative named colivelin by attaching activity-dependent neurotrophic factor to its N terminus: characterization of colivelin-mediated neuroprotection against Alzheimer's disease-relevant insults in vitro and in vivo. J Neurosci 25 (2005) 10252-10261
    • (2005) J Neurosci , vol.25 , pp. 10252-10261
    • Chiba, T.1    Yamada, M.2    Hashimoto, Y.3    Sato, M.4    Sasabe, J.5    Kita, Y.6
  • 8
    • 6944241283 scopus 로고    scopus 로고
    • High-yield, solid-phase synthesis of humanin, an Alzheimer's disease associated, novel 24-mer peptide which contains a difficult sequence
    • Evangelou A., Zikos C., Livaniou E., and Evangelatos G. High-yield, solid-phase synthesis of humanin, an Alzheimer's disease associated, novel 24-mer peptide which contains a difficult sequence. J Pept Sci 10 (2004) 631-635
    • (2004) J Pept Sci , vol.10 , pp. 631-635
    • Evangelou, A.1    Zikos, C.2    Livaniou, E.3    Evangelatos, G.4
  • 9
    • 66249146075 scopus 로고    scopus 로고
    • Spacer site modifications for the improvement of the in vitro and in vivo binding properties of (99m)Tc-N(3)S-X-bombesin[2-14] derivatives
    • Fragogeorgi E.A., Zikos C., Gourni E., Bouziotis P., Paravatou-Petsotas M., Loudos G., et al. Spacer site modifications for the improvement of the in vitro and in vivo binding properties of (99m)Tc-N(3)S-X-bombesin[2-14] derivatives. Bioconj Chem 20 (2009) 856-867
    • (2009) Bioconj Chem , vol.20 , pp. 856-867
    • Fragogeorgi, E.A.1    Zikos, C.2    Gourni, E.3    Bouziotis, P.4    Paravatou-Petsotas, M.5    Loudos, G.6
  • 10
    • 0017874586 scopus 로고
    • Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoruril
    • Fraker P.J., and Speck Jr. J.C. Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphrenylglycoruril. Biochem Biophys Res Commun 80 (1978) 849-857
    • (1978) Biochem Biophys Res Commun , vol.80 , pp. 849-857
    • Fraker, P.J.1    Speck Jr., J.C.2
  • 11
    • 0021679888 scopus 로고
    • Insulin receptors: binding kinetics and structure-function relationship of insulin
    • Gammeltoft S. Insulin receptors: binding kinetics and structure-function relationship of insulin. Physiol Rev 64 (1984) 1321-1378
    • (1984) Physiol Rev , vol.64 , pp. 1321-1378
    • Gammeltoft, S.1
  • 12
    • 0038485614 scopus 로고    scopus 로고
    • Humanin peptide suppresses apoptosis by interfering with Bax activation
    • Guo B., Zhai D., Cabezas E., Welsh K., Nouraini S., Satterthwait A.C., et al. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature 423 (2003) 456-461
    • (2003) Nature , vol.423 , pp. 456-461
    • Guo, B.1    Zhai, D.2    Cabezas, E.3    Welsh, K.4    Nouraini, S.5    Satterthwait, A.C.6
  • 13
    • 4243333514 scopus 로고    scopus 로고
    • A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Aβ
    • Hashimoto Y., Niikura T., Tajima H., Yasukawa T., Sudo H., Ito Y., et al. A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Aβ. Proc Natl Acad Sci USA 98 (2001) 6336-6341
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6336-6341
    • Hashimoto, Y.1    Niikura, T.2    Tajima, H.3    Yasukawa, T.4    Sudo, H.5    Ito, Y.6
  • 14
    • 0034805623 scopus 로고    scopus 로고
    • Mechanisms of neuroprotection by a novel rescue factor humanin from Swedish mutant amyloid precursor protein
    • Hashimoto Y., Ito Y., Niikura T., Shao Z., Hata M., Oyama F., et al. Mechanisms of neuroprotection by a novel rescue factor humanin from Swedish mutant amyloid precursor protein. Biochem Biophys Res Commun 283 (2001) 460-468
    • (2001) Biochem Biophys Res Commun , vol.283 , pp. 460-468
    • Hashimoto, Y.1    Ito, Y.2    Niikura, T.3    Shao, Z.4    Hata, M.5    Oyama, F.6
  • 15
    • 20244361899 scopus 로고    scopus 로고
    • Involvement of c-Jun N-terminal kinase in amyloid precursor protein-mediated neuronal cell death
    • Hashimoto Y., Tsuji O., Niikura T., Yamagishi Y., Ishizaka M., Kawasumi M., et al. Involvement of c-Jun N-terminal kinase in amyloid precursor protein-mediated neuronal cell death. J Neurochem 84 (2003) 864-877
    • (2003) J Neurochem , vol.84 , pp. 864-877
    • Hashimoto, Y.1    Tsuji, O.2    Niikura, T.3    Yamagishi, Y.4    Ishizaka, M.5    Kawasumi, M.6
  • 16
    • 26444463390 scopus 로고    scopus 로고
    • Involvement of tyrosine kinases and STAT3 in humanin-mediated neuroprotection
    • Hashimoto Y., Suzuki H., Aiso S., Niikura T., Nishimoto I., and Matsuoka M. Involvement of tyrosine kinases and STAT3 in humanin-mediated neuroprotection. Life Sci 77 (2005) 3092-3104
    • (2005) Life Sci , vol.77 , pp. 3092-3104
    • Hashimoto, Y.1    Suzuki, H.2    Aiso, S.3    Niikura, T.4    Nishimoto, I.5    Matsuoka, M.6
  • 18
    • 33644687190 scopus 로고    scopus 로고
    • Sodium-iodide symporter mediates iodide secretion in rat gastric mucosa in vitro
    • Josefsson M., Evilevitch L., Weström B., Grunditz T., and Ekblad E. Sodium-iodide symporter mediates iodide secretion in rat gastric mucosa in vitro. Exp Biol Med 231 (2006) 277-281
    • (2006) Exp Biol Med , vol.231 , pp. 277-281
    • Josefsson, M.1    Evilevitch, L.2    Weström, B.3    Grunditz, T.4    Ekblad, E.5
  • 19
    • 0037262465 scopus 로고    scopus 로고
    • Humanin rescues human cerebrovascular smooth muscle cells from Aβ-induced toxicity
    • Jung S.S., and Van Nostrand W.E. Humanin rescues human cerebrovascular smooth muscle cells from Aβ-induced toxicity. J Neurochem 84 (2003) 266-272
    • (2003) J Neurochem , vol.84 , pp. 266-272
    • Jung, S.S.1    Van Nostrand, W.E.2
  • 21
    • 0344034355 scopus 로고    scopus 로고
    • Humanin improves impaired metabolic activity and prolongs survival of serum deprived human lymphocytes
    • Kariya S., Takahashi N., Hirano M., and Ueno S. Humanin improves impaired metabolic activity and prolongs survival of serum deprived human lymphocytes. Mol Cell Biochem 254 (2003) 83-89
    • (2003) Mol Cell Biochem , vol.254 , pp. 83-89
    • Kariya, S.1    Takahashi, N.2    Hirano, M.3    Ueno, S.4
  • 22
    • 0036987994 scopus 로고    scopus 로고
    • Effects of atropine and the oxime HI-6 on low-level sarin-induced alteration of performance of rats in a T-maze
    • Krejčová G., Kassa J., and Vachek J. Effects of atropine and the oxime HI-6 on low-level sarin-induced alteration of performance of rats in a T-maze. Acta Med (Hradec Králové) 45 (2002) 107-110
    • (2002) Acta Med (Hradec Králové) , vol.45 , pp. 107-110
    • Krejčová, G.1    Kassa, J.2    Vachek, J.3
  • 23
    • 6944252056 scopus 로고    scopus 로고
    • Effect of humanin analogues on experimentally induced impairment of spatial memory in rats
    • Krejčová G., Patočka J., and Slaninová J. Effect of humanin analogues on experimentally induced impairment of spatial memory in rats. J Pept Sci 10 (2004) 636-639
    • (2004) J Pept Sci , vol.10 , pp. 636-639
    • Krejčová, G.1    Patočka, J.2    Slaninová, J.3
  • 24
    • 54149087626 scopus 로고    scopus 로고
    • The multiple T-maze in vivo testing of the neuroprotective effect of humanin analogues
    • Kunešová G., Hlaváček J., Patočka J., Evangelou A., Zikos C., Benaki D., et al. The multiple T-maze in vivo testing of the neuroprotective effect of humanin analogues. Peptides 29 (2008) 1982-1987
    • (2008) Peptides , vol.29 , pp. 1982-1987
    • Kunešová, G.1    Hlaváček, J.2    Patočka, J.3    Evangelou, A.4    Zikos, C.5    Benaki, D.6
  • 25
    • 18144427811 scopus 로고    scopus 로고
    • Cytoprotective peptide humanin binds and inhibits pro-apoptotic Bcl-2/Bax-family protein BimEL
    • Luciano F., Zhai D., Zhu X., Bailly-Maitre B., Ricci J.-E., Satterthwait A.C., et al. Cytoprotective peptide humanin binds and inhibits pro-apoptotic Bcl-2/Bax-family protein BimEL. J Biol Chem 280 (2005) 15825-15835
    • (2005) J Biol Chem , vol.280 , pp. 15825-15835
    • Luciano, F.1    Zhai, D.2    Zhu, X.3    Bailly-Maitre, B.4    Ricci, J.-E.5    Satterthwait, A.C.6
  • 26
    • 0035678839 scopus 로고    scopus 로고
    • 14]-Humanin improved the learning and memory impairment induced by scopolamine in vivo
    • 14]-Humanin improved the learning and memory impairment induced by scopolamine in vivo. Br J Pharmacol 134 (2001) 1597-1599
    • (2001) Br J Pharmacol , vol.134 , pp. 1597-1599
    • Mamiya, T.1    Ukai, M.2
  • 27
    • 33748049127 scopus 로고    scopus 로고
    • Humanin and colivelin: neuronal-death-suppressing peptides for Alzheimer's disease and amyotrophic lateral sclerosis
    • Matsuoka M., Hashimoto Y., Aiso S., and Nishimoto I. Humanin and colivelin: neuronal-death-suppressing peptides for Alzheimer's disease and amyotrophic lateral sclerosis. CNS Drug Rev 12 (2006) 113-122
    • (2006) CNS Drug Rev , vol.12 , pp. 113-122
    • Matsuoka, M.1    Hashimoto, Y.2    Aiso, S.3    Nishimoto, I.4
  • 29
    • 0015484902 scopus 로고
    • Blood-brain barrier: penetration of morphine, codeine, heroin, and methadone after carotid injection
    • Oldendorf W.H., Hyman S., Braun L., and Oldendorf S.Z. Blood-brain barrier: penetration of morphine, codeine, heroin, and methadone after carotid injection. Science 178 (1972) 984-986
    • (1972) Science , vol.178 , pp. 984-986
    • Oldendorf, W.H.1    Hyman, S.2    Braun, L.3    Oldendorf, S.Z.4
  • 30
    • 69949084373 scopus 로고    scopus 로고
    • Assays for determination of protein concentration
    • [Chapter 3, Unit 3.4]
    • Olson B.J., and Markwell J. Assays for determination of protein concentration. Curr Protoc Protein Sci (2007) [Chapter 3, Unit 3.4]
    • (2007) Curr Protoc Protein Sci
    • Olson, B.J.1    Markwell J2
  • 32
    • 0029075980 scopus 로고
    • Radiolabeled peptides: now and the future
    • Thakur M.L. Radiolabeled peptides: now and the future. Nucl Med Commun 16 (1995) 724-732
    • (1995) Nucl Med Commun , vol.16 , pp. 724-732
    • Thakur, M.L.1
  • 33
    • 0032913063 scopus 로고    scopus 로고
    • Iodide, thyroid and stomach carcinogenesis: evolutionary story of a primitive antioxidant?
    • Venturi S., and Venturi M. Iodide, thyroid and stomach carcinogenesis: evolutionary story of a primitive antioxidant?. Eur J Endocrinol 140 (1999) 371-372
    • (1999) Eur J Endocrinol , vol.140 , pp. 371-372
    • Venturi, S.1    Venturi, M.2
  • 34
    • 24644445576 scopus 로고    scopus 로고
    • Humanin delays apoptosis in K562 cells by downregulation of P38 MAP kinase
    • Wang D., Li H., Yuan H., Zheng M., Bai C., Chen L., et al. Humanin delays apoptosis in K562 cells by downregulation of P38 MAP kinase. Apoptosis 10 (2005) 963-971
    • (2005) Apoptosis , vol.10 , pp. 963-971
    • Wang, D.1    Li, H.2    Yuan, H.3    Zheng, M.4    Bai, C.5    Chen, L.6
  • 35
  • 36
    • 0013056674 scopus 로고    scopus 로고
    • Identification of essential amino acids in humanin, a neuroprotective factor against Alzheimer's disease-relevant insults
    • Yamagishi Y., Hashimoto Y., Niikura T., and Nishimoto I. Identification of essential amino acids in humanin, a neuroprotective factor against Alzheimer's disease-relevant insults. Peptides 24 (2003) 585-595
    • (2003) Peptides , vol.24 , pp. 585-595
    • Yamagishi, Y.1    Hashimoto, Y.2    Niikura, T.3    Nishimoto, I.4
  • 37
    • 2442705358 scopus 로고    scopus 로고
    • Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor
    • Ying G., Iribarren P., Zhou Y., Gong W., Zhang N., Yu Z.-X., et al. Humanin, a newly identified neuroprotective factor, uses the G protein-coupled formylpeptide receptor-like-1 as a functional receptor. J Immunol 172 (2004) 7078-7085
    • (2004) J Immunol , vol.172 , pp. 7078-7085
    • Ying, G.1    Iribarren, P.2    Zhou, Y.3    Gong, W.4    Zhang, N.5    Yu, Z.-X.6
  • 38
    • 18144399957 scopus 로고    scopus 로고
    • Humanin binds and nullifies Bid activity by blocking its activation of Bax and Bak
    • Zhai D., Luciano F., Zhu X., Guo B., Satterthwait A.C., and Reed J.C. Humanin binds and nullifies Bid activity by blocking its activation of Bax and Bak. J Biol Chem 280 (2005) 15815-15824
    • (2005) J Biol Chem , vol.280 , pp. 15815-15824
    • Zhai, D.1    Luciano, F.2    Zhu, X.3    Guo, B.4    Satterthwait, A.C.5    Reed, J.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.