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Volumn 164, Issue 2-3, 2010, Pages 83-89

Addition of a cysteine to glucagon-like peptide-1 (GLP-1) conjugates GLP-1 to albumin in serum and prolongs GLP-1 action in vivo

Author keywords

Albumin conjugation; Diabetic treatment; Glucagon like peptide 1; Protease degradation

Indexed keywords

ANTIDIABETIC AGENT; CYCLIC AMP; CYSTEINE; GLUCAGON LIKE PEPTIDE 1; GLUCOSE; INSULIN; PROTEINASE; RECOMBINANT GLUCAGON LIKE PEPTIDE 1; SERUM ALBUMIN; UNCLASSIFIED DRUG;

EID: 77955846737     PISSN: 01670115     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.regpep.2010.05.003     Document Type: Article
Times cited : (12)

References (28)
  • 1
    • 1842855402 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 regulates proliferation and apoptosis via activation of protein kinase B in pancreatic INS-1 beta cells
    • Wang Q., Li L., Xu E., Wong V., Rhodes C., Brubaker P.L. Glucagon-like peptide-1 regulates proliferation and apoptosis via activation of protein kinase B in pancreatic INS-1 beta cells. Diabetologia 2004, 47:478-487.
    • (2004) Diabetologia , vol.47 , pp. 478-487
    • Wang, Q.1    Li, L.2    Xu, E.3    Wong, V.4    Rhodes, C.5    Brubaker, P.L.6
  • 2
    • 33644618433 scopus 로고    scopus 로고
    • The biology of incretin hormones
    • Drucker D.J. The biology of incretin hormones. Cell Metab 2006, 3:153-165.
    • (2006) Cell Metab , vol.3 , pp. 153-165
    • Drucker, D.J.1
  • 3
    • 15244363744 scopus 로고    scopus 로고
    • Synthesis, characterization, and pharmacokinetic studies of PEGylated glucagon-like peptide-1
    • Lee S.H., Lee S., Youn Y.S., Na D.H., Chae S.Y., Byun Y., Lee K.C. Synthesis, characterization, and pharmacokinetic studies of PEGylated glucagon-like peptide-1. Bioconjug Chem 2005, 16:377-382.
    • (2005) Bioconjug Chem , vol.16 , pp. 377-382
    • Lee, S.H.1    Lee, S.2    Youn, Y.S.3    Na, D.H.4    Chae, S.Y.5    Byun, Y.6    Lee, K.C.7
  • 4
    • 0036182251 scopus 로고    scopus 로고
    • A novel neurotrophic property of glucagon-like peptide 1: a promoter of nerve growth factor-mediated differentiation in PC12 cells
    • Perry T., Lahiri D.K., Chen D., Zhou J., Shaw K.T., Egan J.M., Greig N.H. A novel neurotrophic property of glucagon-like peptide 1: a promoter of nerve growth factor-mediated differentiation in PC12 cells. J Pharmacol Exp Ther 2002, 300:958-966.
    • (2002) J Pharmacol Exp Ther , vol.300 , pp. 958-966
    • Perry, T.1    Lahiri, D.K.2    Chen, D.3    Zhou, J.4    Shaw, K.T.5    Egan, J.M.6    Greig, N.H.7
  • 5
    • 52249112474 scopus 로고    scopus 로고
    • Mutated recombinant human glucagon-like peptide-1 protects SH-SY5Y cells from apoptosis induced by amyloid-beta peptide (1-42)
    • Qin Z., Sun Z., Huang J., Hu Y., Wu Z., Mei B. Mutated recombinant human glucagon-like peptide-1 protects SH-SY5Y cells from apoptosis induced by amyloid-beta peptide (1-42). Neurosci Lett 2008, 444:217-221.
    • (2008) Neurosci Lett , vol.444 , pp. 217-221
    • Qin, Z.1    Sun, Z.2    Huang, J.3    Hu, Y.4    Wu, Z.5    Mei, B.6
  • 6
    • 12144260853 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 can directly protect the heart against ischemia/reperfusion injury
    • Bose A.K., Mocanu M.M., Carr R.D., Brand C.L., Yellon D.M. Glucagon-like peptide 1 can directly protect the heart against ischemia/reperfusion injury. Diabetes 2005, 54:146-151.
    • (2005) Diabetes , vol.54 , pp. 146-151
    • Bose, A.K.1    Mocanu, M.M.2    Carr, R.D.3    Brand, C.L.4    Yellon, D.M.5
  • 7
    • 33845207048 scopus 로고    scopus 로고
    • Evaluation of therapeutic potentials of site-specific PEGylated glucagon-like peptide-1 isomers as a type 2 anti-diabetic treatment: insulinotropic activity, glucose-stabilizing capability, and proteolytic stability
    • Youn Y.S., Chae S.Y., Lee S., Jeon J.E., Shin H.G., Lee K.C. Evaluation of therapeutic potentials of site-specific PEGylated glucagon-like peptide-1 isomers as a type 2 anti-diabetic treatment: insulinotropic activity, glucose-stabilizing capability, and proteolytic stability. Biochem Pharmacol 2007, 73:84-93.
    • (2007) Biochem Pharmacol , vol.73 , pp. 84-93
    • Youn, Y.S.1    Chae, S.Y.2    Lee, S.3    Jeon, J.E.4    Shin, H.G.5    Lee, K.C.6
  • 8
    • 0038519125 scopus 로고    scopus 로고
    • Pharmacology of exenatide (synthetic exendin-4) for the treatment of type 2 diabetes
    • Nielsen L.L., Baron A.D. Pharmacology of exenatide (synthetic exendin-4) for the treatment of type 2 diabetes. Curr Opin Investig Drugs 2003, 4:401-405.
    • (2003) Curr Opin Investig Drugs , vol.4 , pp. 401-405
    • Nielsen, L.L.1    Baron, A.D.2
  • 9
    • 33745937115 scopus 로고    scopus 로고
    • Novel glucagon-like peptide-1 (GLP-1) analog (Val8)GLP-1 results in significant improvements of glucose tolerance and pancreatic beta-cell function after 3-week daily administration in obese diabetic (ob/ob) mice
    • Green B.D., Lavery K.S., Irwin N., O'Harte F.P., Harriott P., Greer B., Bailey C.J., Flatt P.R. Novel glucagon-like peptide-1 (GLP-1) analog (Val8)GLP-1 results in significant improvements of glucose tolerance and pancreatic beta-cell function after 3-week daily administration in obese diabetic (ob/ob) mice. J Pharmacol Exp Ther 2006, 318:914-921.
    • (2006) J Pharmacol Exp Ther , vol.318 , pp. 914-921
    • Green, B.D.1    Lavery, K.S.2    Irwin, N.3    O'Harte, F.P.4    Harriott, P.5    Greer, B.6    Bailey, C.J.7    Flatt, P.R.8
  • 11
    • 0037339649 scopus 로고    scopus 로고
    • Development and characterization of a glucagon-like peptide 1-albumin conjugate: the ability to activate the glucagon-like peptide 1 receptor in vivo
    • Kim J.G., Baggio L.L., Bridon D.P., Castaigne J.P., Robitaille M.F., Jette L., Benquet C., Drucker D.J. Development and characterization of a glucagon-like peptide 1-albumin conjugate: the ability to activate the glucagon-like peptide 1 receptor in vivo. Diabetes 2003, 52:751-759.
    • (2003) Diabetes , vol.52 , pp. 751-759
    • Kim, J.G.1    Baggio, L.L.2    Bridon, D.P.3    Castaigne, J.P.4    Robitaille, M.F.5    Jette, L.6    Benquet, C.7    Drucker, D.J.8
  • 12
    • 0033974696 scopus 로고    scopus 로고
    • N-terminally modified glucagon-like peptide-1(7-36) amide exhibits resistance to enzymatic degradation while maintaining its antihyperglycaemic activity in vivo
    • O'Harte F.P., Mooney M.H., Lawlor A., Flatt P.R. N-terminally modified glucagon-like peptide-1(7-36) amide exhibits resistance to enzymatic degradation while maintaining its antihyperglycaemic activity in vivo. Biochim Biophys Acta 2000, 1474:13-22.
    • (2000) Biochim Biophys Acta , vol.1474 , pp. 13-22
    • O'Harte, F.P.1    Mooney, M.H.2    Lawlor, A.3    Flatt, P.R.4
  • 13
    • 1842530457 scopus 로고    scopus 로고
    • N-terminal His(7)-modification of glucagon-like peptide-1(7-36) amide generates dipeptidyl peptidase IV-stable analogues with potent antihyperglycaemic activity
    • Green B.D., Mooney M.H., Gault V.A., Irwin N., Bailey C.J., Harriott P., Greer B., O'Harte F.P., Flatt P.R. N-terminal His(7)-modification of glucagon-like peptide-1(7-36) amide generates dipeptidyl peptidase IV-stable analogues with potent antihyperglycaemic activity. J Endocrinol 2004, 180:379-388.
    • (2004) J Endocrinol , vol.180 , pp. 379-388
    • Green, B.D.1    Mooney, M.H.2    Gault, V.A.3    Irwin, N.4    Bailey, C.J.5    Harriott, P.6    Greer, B.7    O'Harte, F.P.8    Flatt, P.R.9
  • 14
    • 37549030476 scopus 로고    scopus 로고
    • Decreased dipeptidyl peptidase-IV activity and glucagon-like peptide-1(7-36)amide degradation in type 2 diabetic subjects
    • McKillop A.M., Duffy N.A., Lindsay J.R., O'Harte F.P., Bell P.M., Flatt P.R. Decreased dipeptidyl peptidase-IV activity and glucagon-like peptide-1(7-36)amide degradation in type 2 diabetic subjects. Diab Res Clin Pract 2008, 79:79-85.
    • (2008) Diab Res Clin Pract , vol.79 , pp. 79-85
    • McKillop, A.M.1    Duffy, N.A.2    Lindsay, J.R.3    O'Harte, F.P.4    Bell, P.M.5    Flatt, P.R.6
  • 16
    • 0344357096 scopus 로고
    • Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line
    • Drucker D.J., Philippe J., Mojsov S., Chick W.L., Habener J.F. Glucagon-like peptide I stimulates insulin gene expression and increases cyclic AMP levels in a rat islet cell line. Proc Natl Acad Sci U S A 1987, 84:3434-3438.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 3434-3438
    • Drucker, D.J.1    Philippe, J.2    Mojsov, S.3    Chick, W.L.4    Habener, J.F.5
  • 17
    • 0029118049 scopus 로고
    • Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV
    • Kieffer T.J., McIntosh C.H., Pederson R.A. Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology 1995, 136:3585-3596.
    • (1995) Endocrinology , vol.136 , pp. 3585-3596
    • Kieffer, T.J.1    McIntosh, C.H.2    Pederson, R.A.3
  • 18
    • 33644902945 scopus 로고    scopus 로고
    • GLP-1 based therapy for type 2 diabetes
    • Arulmozhi D.K., Portha B. GLP-1 based therapy for type 2 diabetes. Eur J Pharm Sci 2006, 28:96-108.
    • (2006) Eur J Pharm Sci , vol.28 , pp. 96-108
    • Arulmozhi, D.K.1    Portha, B.2
  • 20
    • 0342314489 scopus 로고    scopus 로고
    • A novel macromolecular prodrug concept exploiting endogenous serum albumin as a drug carrier for cancer chemotherapy
    • Kratz F., Muller-Driver R., Hofmann I., Drevs J., Unger C. A novel macromolecular prodrug concept exploiting endogenous serum albumin as a drug carrier for cancer chemotherapy. J Med Chem 2000, 43:1253-1256.
    • (2000) J Med Chem , vol.43 , pp. 1253-1256
    • Kratz, F.1    Muller-Driver, R.2    Hofmann, I.3    Drevs, J.4    Unger, C.5
  • 21
    • 0036189831 scopus 로고    scopus 로고
    • The pharmacokinetics, pharmacodynamics, safety and tolerability of NN2211, a new long-acting GLP-1 derivative, in healthy men
    • Agerso H., Jensen L.B., Elbrond B., Rolan P., Zdravkovic M. The pharmacokinetics, pharmacodynamics, safety and tolerability of NN2211, a new long-acting GLP-1 derivative, in healthy men. Diabetologia 2002, 45:195-202.
    • (2002) Diabetologia , vol.45 , pp. 195-202
    • Agerso, H.1    Jensen, L.B.2    Elbrond, B.3    Rolan, P.4    Zdravkovic, M.5
  • 22
    • 0022429584 scopus 로고
    • High-performance liquid chromatographic studies on non-mercapt in equilibrium with mercapt conversion of human serum albumin. II
    • Sogami M., Era S., Nagaoka S., Kuwata K., Kida K., Shigemi J., Miura K., Suzuki E., Muto Y., Tomita E., et al. High-performance liquid chromatographic studies on non-mercapt in equilibrium with mercapt conversion of human serum albumin. II. J Chromatogr 1985, 332:19-27.
    • (1985) J Chromatogr , vol.332 , pp. 19-27
    • Sogami, M.1    Era, S.2    Nagaoka, S.3    Kuwata, K.4    Kida, K.5    Shigemi, J.6    Miura, K.7    Suzuki, E.8    Muto, Y.9    Tomita, E.10
  • 23
    • 0026716122 scopus 로고
    • Rapid analysis of human serum albumin by high-performance liquid chromatography
    • Etoh T., Miyazaki M., Harada K., Nakayama M., Sugii A. Rapid analysis of human serum albumin by high-performance liquid chromatography. J Chromatogr 1992, 578:292-296.
    • (1992) J Chromatogr , vol.578 , pp. 292-296
    • Etoh, T.1    Miyazaki, M.2    Harada, K.3    Nakayama, M.4    Sugii, A.5
  • 24
    • 0023881390 scopus 로고
    • Further studies on the resolution of human mercapt- and nonmercaptalbumin and on human serum albumin in the elderly by high-performance liquid chromatography
    • Era S., Hamaguchi T., Sogami M., Kuwata K., Suzuki E., Miura K., Kawai K., Kitazawa Y., Okabe H., Noma A., et al. Further studies on the resolution of human mercapt- and nonmercaptalbumin and on human serum albumin in the elderly by high-performance liquid chromatography. Int J Pept Protein Res 1988, 31:435-442.
    • (1988) Int J Pept Protein Res , vol.31 , pp. 435-442
    • Era, S.1    Hamaguchi, T.2    Sogami, M.3    Kuwata, K.4    Suzuki, E.5    Miura, K.6    Kawai, K.7    Kitazawa, Y.8    Okabe, H.9    Noma, A.10
  • 25
    • 0025139919 scopus 로고
    • Determination of cysteine on low-density lipoproteins using the fluorescent probe, 5-iodoacetamidofluoresceine
    • Coleman R.D., Kim T.W., Gotto A.M., Yang C.Y. Determination of cysteine on low-density lipoproteins using the fluorescent probe, 5-iodoacetamidofluoresceine. Biochim Biophys Acta 1990, 1037:129-132.
    • (1990) Biochim Biophys Acta , vol.1037 , pp. 129-132
    • Coleman, R.D.1    Kim, T.W.2    Gotto, A.M.3    Yang, C.Y.4
  • 26
    • 0025074449 scopus 로고
    • Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100
    • Yang C.Y., Kim T.W., Weng S.A., Lee B.R., Yang M.L., Gotto A.M. Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100. Proc Natl Acad Sci U S A 1990, 87:5523-5527.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 5523-5527
    • Yang, C.Y.1    Kim, T.W.2    Weng, S.A.3    Lee, B.R.4    Yang, M.L.5    Gotto, A.M.6
  • 27
    • 0020328167 scopus 로고
    • Immunological identification of two sulfhydryl-containing fragments of human plasma fibronectin
    • Smith D.E., Mosher D.F., Johnson R.B., Furcht L.T. Immunological identification of two sulfhydryl-containing fragments of human plasma fibronectin. J Biol Chem 1982, 257:5831-5838.
    • (1982) J Biol Chem , vol.257 , pp. 5831-5838
    • Smith, D.E.1    Mosher, D.F.2    Johnson, R.B.3    Furcht, L.T.4
  • 28
    • 0017880356 scopus 로고
    • Human alpha1-antitrypsin. Characterization and N- and C-terminal sequences
    • Morii M., Odani S., Koide T., Ikenaka T. Human alpha1-antitrypsin. Characterization and N- and C-terminal sequences. J Biochem 1978, 83:269-277.
    • (1978) J Biochem , vol.83 , pp. 269-277
    • Morii, M.1    Odani, S.2    Koide, T.3    Ikenaka, T.4


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