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Volumn 172, Issue 1, 2013, Pages 144-151

A depot-forming glucagon-like peptide-1 fusion protein reduces blood glucose for five days with a single injection

Author keywords

Drug delivery; Elastin like polypeptide; Glucagon like peptide 1; Peptide; Subcutaneous depot

Indexed keywords

BLOOD GLUCOSE LEVEL; ELASTIN-LIKE POLYPEPTIDES; GLUCAGON-LIKE PEPTIDE-1; PROLONGED RELEASE; PROTEOLYTIC STABILITY; SUBCUTANEOUS DEPOT; SYSTEMIC CIRCULATION; THERMALLY RESPONSIVE;

EID: 84883514263     PISSN: 01683659     EISSN: 18734995     Source Type: Journal    
DOI: 10.1016/j.jconrel.2013.07.021     Document Type: Article
Times cited : (91)

References (48)
  • 1
    • 43249090768 scopus 로고    scopus 로고
    • Prevention and treatment of type 2 diabetes: Current role of lifestyle, natural product, and pharmacological interventions
    • N.P. Hays, P.R. Galassetti, and R.H. Coker Prevention and treatment of type 2 diabetes: current role of lifestyle, natural product, and pharmacological interventions Pharmacol. Ther. 118 2008 181 191
    • (2008) Pharmacol. Ther. , vol.118 , pp. 181-191
    • Hays, N.P.1    Galassetti, P.R.2    Coker, R.H.3
  • 2
    • 77953160144 scopus 로고    scopus 로고
    • Minireview: Update on incretin biology: Focus on glucagon-like peptide-1
    • P.L. Brubaker Minireview: update on incretin biology: focus on glucagon-like peptide-1 Endocrinology 151 2010 1984 1989
    • (2010) Endocrinology , vol.151 , pp. 1984-1989
    • Brubaker, P.L.1
  • 3
    • 0031758346 scopus 로고    scopus 로고
    • Glucagon-like peptide 1 (GLP-1): A potent gut hormone with a possible therapeutic perspective
    • M.A. Nauck Glucagon-like peptide 1 (GLP-1): a potent gut hormone with a possible therapeutic perspective Acta Diabetol. 35 1998 117 129
    • (1998) Acta Diabetol. , vol.35 , pp. 117-129
    • Nauck, M.A.1
  • 4
    • 21744440422 scopus 로고    scopus 로고
    • Structure and function studies of glucagon-like peptide-1 (GLP-1): The designing of a novel pharmacological agent for the treatment of diabetes
    • DOI 10.1002/dmrr.553
    • H.X. Hui, H.N. Zhao, and R. Perfetti Structure and function studies of glucagon-like peptide-1 (GLP-1): the designing of a novel pharmacological agent for the treatment of diabetes Diabetes Metab. Res. Rev. 21 2005 313 331 (Pubitemid 40945953)
    • (2005) Diabetes/Metabolism Research and Reviews , vol.21 , Issue.4 , pp. 313-331
    • Hui, H.1    Zhao, X.2    Perfetti, R.3
  • 5
    • 34248223285 scopus 로고    scopus 로고
    • Biology of Incretins: GLP-1 and GIP
    • DOI 10.1053/j.gastro.2007.03.054, PII S001650850700580X
    • L.L. Baggio, and D.J. Drucker Biology of incretins: GLP-1 and GIP Gastroenterology 132 2007 2131 2157 (Pubitemid 46711096)
    • (2007) Gastroenterology , vol.132 , Issue.6 , pp. 2131-2157
    • Baggio, L.L.1    Drucker, D.J.2
  • 6
    • 64649104158 scopus 로고    scopus 로고
    • From the triumvirate to the ominous octet: A new paradigm for the treatment of type 2 diabetes mellitus
    • R.A. DeFronzo From the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus Diabetes 58 2009 773 795
    • (2009) Diabetes , vol.58 , pp. 773-795
    • Defronzo, R.A.1
  • 7
    • 57649234120 scopus 로고    scopus 로고
    • The incretin system and its role in type 2 diabetes mellitus
    • J.J. Holst, T. Vilsboll, and C.F. Deacon The incretin system and its role in type 2 diabetes mellitus Mol. Cell. Endocrinol. 297 2009 127 136
    • (2009) Mol. Cell. Endocrinol. , vol.297 , pp. 127-136
    • Holst, J.J.1    Vilsboll, T.2    Deacon, C.F.3
  • 8
    • 2542479899 scopus 로고    scopus 로고
    • Minireview: Glucagon-like peptides regulate cell proliferation and apoptosis in the pancreas, gut, and central nervous system
    • DOI 10.1210/en.2004-0015
    • P.L. Brubaker, and D.J. Drucker Minireview: glucagon-like peptides regulate cell proliferation and apoptosis in the pancreas, gut, and central nervous system Endocrinology 145 2004 2653 2659 (Pubitemid 38686211)
    • (2004) Endocrinology , vol.145 , Issue.6 , pp. 2653-2659
    • Brubaker, P.L.1    Drucker, D.J.2
  • 10
    • 67651173077 scopus 로고    scopus 로고
    • Incretin-based therapies for type 2 diabetes mellitus
    • J.A. Lovshin, and D.J. Drucker Incretin-based therapies for type 2 diabetes mellitus Nat. Rev. Endocrinol. 5 2009 262 269
    • (2009) Nat. Rev. Endocrinol. , vol.5 , pp. 262-269
    • Lovshin, J.A.1    Drucker, D.J.2
  • 11
    • 79953040963 scopus 로고    scopus 로고
    • An overview of once-weekly glucagon-like peptide-1 receptor agonists - Available efficacy and safety data and perspectives for the future
    • S. Madsbad, U. Kielgast, M. Asmar, C.F. Deacon, S.S. Torekov, and J.J. Holst An overview of once-weekly glucagon-like peptide-1 receptor agonists - available efficacy and safety data and perspectives for the future Diabetes Obes. Metab. 13 2011 394 407
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 394-407
    • Madsbad, S.1    Kielgast, U.2    Asmar, M.3    Deacon, C.F.4    Torekov, S.S.5    Holst, J.J.6
  • 13
    • 77953859640 scopus 로고    scopus 로고
    • Once weekly exenatide compared with insulin glargine titrated to target in patients with type 2 diabetes (DURATION-3): An open-label randomised trial
    • M. Diamant, L. Van Gaal, S. Stranks, J. Northrup, D. Cao, K. Taylor, and M. Trautmann Once weekly exenatide compared with insulin glargine titrated to target in patients with type 2 diabetes (DURATION-3): an open-label randomised trial Lancet 375 2010 2234 2243
    • (2010) Lancet , vol.375 , pp. 2234-2243
    • Diamant, M.1    Van Gaal, L.2    Stranks, S.3    Northrup, J.4    Cao, D.5    Taylor, K.6    Trautmann, M.7
  • 14
    • 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
    • DOI 10.2337/diabetes.52.3.751
    • J.G. Kim, L.L. Baggio, D.P. Bridon, J.P. Castaigne, M.F. Robitaille, L. Jette, C. Benquet, and D.J. Drucker Development and characterization of a glucagon-like peptide 1-albumin conjugate - the ability to activate the glucagon-like peptide 1 receptor in vivo Diabetes 52 2003 751 759 (Pubitemid 36323583)
    • (2003) Diabetes , vol.52 , Issue.3 , 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
  • 17
    • 84874227739 scopus 로고    scopus 로고
    • Parenteral controlled delivery and pharmacokinetics of therapeutic peptides and proteins
    • CRC Press
    • A.K. Banga Parenteral controlled delivery and pharmacokinetics of therapeutic peptides and proteins Therapeutic Peptides and Proteins 2005 CRC Press 177 227
    • (2005) Therapeutic Peptides and Proteins , pp. 177-227
    • Banga, A.K.1
  • 18
    • 84874245248 scopus 로고    scopus 로고
    • Injectable protease-operated depots of glucagon-like peptide-1 provide extended and tunable glucose control
    • M. Amiram, K.M. Luginbuhl, X. Li, M.N. Feinglos, and A. Chilkoti Injectable protease-operated depots of glucagon-like peptide-1 provide extended and tunable glucose control Proc. Natl. Acad. Sci. U. S. A. 110 2013 2792 2797
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 2792-2797
    • Amiram, M.1    Luginbuhl, K.M.2    Li, X.3    Feinglos, M.N.4    Chilkoti, A.5
  • 19
    • 2542628131 scopus 로고    scopus 로고
    • Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides
    • DOI 10.1021/bm034215n
    • D.E. Meyer, and A. Chilkoti Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides Biomacromolecules 5 2004 846 851 (Pubitemid 38702255)
    • (2004) Biomacromolecules , vol.5 , Issue.3 , pp. 846-851
    • Meyer, D.E.1    Chilkoti, A.2
  • 21
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • N.J. Greenfield Using circular dichroism spectra to estimate protein secondary structure Nat. Protoc. 1 2006 2876 2890
    • (2006) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 22
    • 4344667831 scopus 로고    scopus 로고
    • A recombinant human glucagon-like peptide (GLP)-1-albumin protein (Albugon) mimics peptidergic activation of GLP-1 receptor-dependent pathways coupled with satiety, gastrointestinal motility, and glucose homeostasis
    • DOI 10.2337/diabetes.53.9.2492
    • L.L. Baggio, Q. Huang, T.J. Brown, and D.J. Drucker A recombinant human glucagon-like peptide (GLP)-1-albumin protein (albugon) mimics peptidergic activation of GLP-1 receptor-dependent pathways coupled with satiety, gastrointestinal motility, and glucose homeostasis Diabetes 53 2004 2492 2500 (Pubitemid 39145610)
    • (2004) Diabetes , vol.53 , Issue.9 , pp. 2492-2500
    • Baggio, L.L.1    Huang, Q.2    Brown, T.J.3    Drucker, D.J.4
  • 24
    • 0037312818 scopus 로고    scopus 로고
    • Glucagon-like peptides: Regulators of cell proliferation, differentiation, and apoptosis
    • DOI 10.1210/me.2002-0306
    • D.J. Drucker Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis Mol. Endocrinol. 17 2003 161 171 (Pubitemid 36183142)
    • (2003) Molecular Endocrinology , vol.17 , Issue.2 , pp. 161-171
    • Drucker, D.J.1
  • 27
    • 0036200174 scopus 로고    scopus 로고
    • Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: Examples from the the elastin-like polypeptide system
    • DOI 10.1021/bm015630n
    • D.E. Meyer, and A. Chilkoti Genetically encoded synthesis of protein-based polymers with precisely specified molecular weight and sequence by recursive directional ligation: examples from the elastin-like polypeptide system Biomacromolecules 3 2002 357 367 (Pubitemid 34257157)
    • (2002) Biomacromolecules , vol.3 , Issue.2 , pp. 357-367
    • Meyer, D.E.1    Chilkoti, A.2
  • 28
  • 29
    • 9344234999 scopus 로고    scopus 로고
    • Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion
    • DOI 10.1110/ps.04931604
    • K. Trabbic-Carlson, L. Liu, B. Kim, and A. Chilkoti Expression and purification of recombinant proteins from Escherichia coli: comparison of an elastin-like polypeptide fusion with an oligohistidine fusion Protein Sci. 13 2004 3274 3284 (Pubitemid 39557797)
    • (2004) Protein Science , vol.13 , Issue.12 , pp. 3274-3284
    • Trabbic-Carlson, K.1    Liu, L.2    Kim, B.3    Chilkoti, A.4
  • 30
    • 0033152181 scopus 로고    scopus 로고
    • Elastic molecular machines in metabolism and soft-tissue restoration
    • DOI 10.1016/S0167-7799(99)01306-2, PII S0167779999013062
    • D.W. Urry Elastic molecular machines in metabolism and soft-tissue restoration Trends Biotechnol. 17 1999 249 257 (Pubitemid 29249012)
    • (1999) Trends in Biotechnology , vol.17 , Issue.6 , pp. 249-257
    • Urry, D.W.1
  • 31
    • 28744446565 scopus 로고    scopus 로고
    • Epitope tagging for tracking elastin-like polypeptides
    • DOI 10.1016/j.biomaterials.2005.10.018, PII S0142961205009269
    • S.R. Ong, K.A. Trabbic-Carlson, D.L. Nettles, D.W. Lim, A. Chilkoti, and L.A. Setton Epitope tagging for tracking elastin-like polypeptides Biomaterials 27 2006 1930 1935 (Pubitemid 41759487)
    • (2006) Biomaterials , vol.27 , Issue.9 , pp. 1930-1935
    • Ong, S.R.1    Trabbic-Carlson, K.A.2    Nettles, D.L.3    Lim, D.W.4    Chilkoti, A.5    Setton, L.A.6
  • 32
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides
    • DOI 10.1038/15100
    • D.E. Meyer, and A. Chilkoti Purification of recombinant proteins by fusion with thermally-responsive polypeptides Nat. Biotechnol. 17 1999 1112 1115 (Pubitemid 29533553)
    • (1999) Nature Biotechnology , vol.17 , Issue.11 , pp. 1112-1115
    • Meyer, D.E.1    Chilkoti, A.2
  • 33
    • 3843121153 scopus 로고    scopus 로고
    • Glucagon-like peptide-1: The basis of a new class of treatment for type 2 diabetes
    • DOI 10.1021/jm030630m
    • L.B. Knudsen Glucagon-like peptide-1: the basis of a new class of treatment for type 2 diabetes J. Med. Chem. 47 2004 4128 4134 (Pubitemid 39045416)
    • (2004) Journal of Medicinal Chemistry , vol.47 , Issue.17 , pp. 4128-4134
    • Knudsen, L.B.1
  • 34
    • 0029111540 scopus 로고
    • Characterisation of the processing by human neutral endopeptidase 24.11 of GLP-1(7-36) amide and comparison of the substrate specificity of the enzyme for other glucagon-like peptides
    • K. Hupe-Sodmann, G.P. McGregor, R. Bridenbaugh, R. Goke, B. Goke, H. Thole, B. Zimmermann, and K. Voigt Characterisation of the processing by human neutral endopeptidase 24.11 of GLP-1(7-36) amide and comparison of the substrate specificity of the enzyme for other glucagon-like peptides Regul. Pept. 58 1995 149 156
    • (1995) Regul. Pept. , vol.58 , pp. 149-156
    • Hupe-Sodmann, K.1    McGregor, G.P.2    Bridenbaugh, R.3    Goke, R.4    Goke, B.5    Thole, H.6    Zimmermann, B.7    Voigt, K.8
  • 35
    • 78049365082 scopus 로고    scopus 로고
    • Metabolism and excretion of the once-daily human glucagon-like peptide-1 analog liraglutide in healthy male subjects and its in vitro degradation by dipeptidyl peptidase IV and neutral endopeptidase
    • M. Malm-Erjefalt, I. Bjornsdottir, J. Vanggaard, H. Helleberg, U. Larsen, B. Oosterhuis, J.J. van Lier, M. Zdravkovic, and A.K. Olsen Metabolism and excretion of the once-daily human glucagon-like peptide-1 analog liraglutide in healthy male subjects and its in vitro degradation by dipeptidyl peptidase IV and neutral endopeptidase Drug Metab. Dispos. 38 2010 1944 1953
    • (2010) Drug Metab. Dispos. , vol.38 , pp. 1944-1953
    • Malm-Erjefalt, M.1    Bjornsdottir, I.2    Vanggaard, J.3    Helleberg, H.4    Larsen, U.5    Oosterhuis, B.6    Van Lier, J.J.7    Zdravkovic, M.8    Olsen, A.K.9
  • 36
    • 44349157048 scopus 로고    scopus 로고
    • Preparation and characterization of a novel exendin-4 human serum albumin fusion protein expressed in Pichia pastoris
    • DOI 10.1002/psc.942
    • Y.S. Huang, Z. Chen, Y.Q. Chen, G.C. Ma, J.F. Shan, W. Liu, and L.F. Zhou Preparation and characterization of a novel exendin-4 human serum albumin fusion protein expressed in Pichia pastoris J. Pept. Sci. 14 2008 588 595 (Pubitemid 351736454)
    • (2008) Journal of Peptide Science , vol.14 , Issue.5 , pp. 588-595
    • Huang, Y.-S.1    Chen, Z.2    Chen, Y.-C.3    Ma, G.-C.4    Shan, J.-F.5    Liu, W.6    Zhou, L.-F.7
  • 37
    • 67449164292 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic evaluation of site-specific PEGylated glucagon-like peptide-1 analogs as flexible postprandial-glucose controllers
    • S.Y. Chae, Y.G. Chun, S. Lee, C.H. Jin, E.S. Lee, K.C. Lee, and Y.S. Youn Pharmacokinetic and pharmacodynamic evaluation of site-specific PEGylated glucagon-like peptide-1 analogs as flexible postprandial-glucose controllers J. Pharm. Sci. 98 2009 1556 1567
    • (2009) J. Pharm. Sci. , vol.98 , pp. 1556-1567
    • Chae, S.Y.1    Chun, Y.G.2    Lee, S.3    Jin, C.H.4    Lee, E.S.5    Lee, K.C.6    Youn, Y.S.7
  • 38
    • 0037045845 scopus 로고    scopus 로고
    • Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and β-cell function in type 2 diabetes: A parallel-group study
    • DOI 10.1016/S0140-6736(02)07952-7
    • M. Zander, S. Madsbad, J.L. Madsen, and J.J. Holst Effect of 6-week course of glucagon-like peptide 1 on glycaemic control, insulin sensitivity, and beta-cell function in type 2 diabetes: a parallel-group study Lancet 359 2002 824 830 (Pubitemid 34233752)
    • (2002) Lancet , vol.359 , Issue.9309 , pp. 824-830
    • Zander, M.1    Madsbad, S.2    Madsen, J.L.3    Holst, J.J.4
  • 39
    • 9444231814 scopus 로고    scopus 로고
    • Chronic exposure to GLP-IR agonists promotes homologous GLP-1 receptor desensitization in vitro but does not attenuate GLP-1R-dependent glucose homeostasis in vivo
    • L.L. Baggio, J.G. Kim, and D.J. Drucker Chronic exposure to GLP-IR agonists promotes homologous GLP-1 receptor desensitization in vitro but does not attenuate GLP-1R-dependent glucose homeostasis in vivo Diabetes 53 2004 S205 S214
    • (2004) Diabetes , vol.53
    • Baggio, L.L.1    Kim, J.G.2    Drucker, D.J.3
  • 42
    • 84883256420 scopus 로고    scopus 로고
    • Future directions for peptide therapeutics development
    • 10.1016/j.drudis.2013.05.011
    • A.A. Kaspar, and J.M. Reichert Future directions for peptide therapeutics development Drug Discov. Today 2013 10.1016/j.drudis.2013.05.011
    • (2013) Drug Discov. Today
    • Kaspar, A.A.1    Reichert, J.M.2
  • 43
    • 0036001387 scopus 로고    scopus 로고
    • Pharmaceutical strategies utilizing recombinant human serum albumin
    • DOI 10.1023/A:1015396825274
    • V.T. Chuang, U. Kragh-Hansen, and M. Otagiri Pharmaceutical strategies utilizing recombinant human serum albumin Pharm. Res. 19 2002 569 577 (Pubitemid 34553662)
    • (2002) Pharmaceutical Research , vol.19 , Issue.5 , pp. 569-577
    • Tuan Giam Chuang, V.1    Kragh-Hansen, U.2    Otagiri, M.3
  • 44
    • 33645078890 scopus 로고    scopus 로고
    • Biology and therapeutic potential of GLP-1 in the treatment of diabetes
    • J.M.E. Chee, and W. Chia Biology and therapeutic potential of GLP-1 in the treatment of diabetes Drug Discov. Today Dis. Mech. 2 2005 295 301
    • (2005) Drug Discov. Today Dis. Mech. , vol.2 , pp. 295-301
    • Chee, J.M.E.1    Chia, W.2
  • 46
    • 0031766395 scopus 로고    scopus 로고
    • FDA perspective on peptide formulation and stability issues
    • C.H. Niu, and Y.Y. Chiu FDA perspective on peptide formulation and stability issues J. Pharm. Sci. 87 1998 1331 1334
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1331-1334
    • Niu, C.H.1    Chiu, Y.Y.2
  • 47
    • 0343247711 scopus 로고    scopus 로고
    • Biodegradation and biocompatibility of PLA and PLGA microspheres
    • DOI 10.1016/S0169-409X(97)00048-3, PII S0169409X97000483
    • M.S. Shive, and J.M. Anderson Biodegradation and biocompatibility of PLA and PLGA microspheres Adv. Drug Deliv. Rev. 28 1997 5 24 (Pubitemid 27497671)
    • (1997) Advanced Drug Delivery Reviews , vol.28 , Issue.1 , pp. 5-24
    • Anderson, J.M.1    Shive, M.S.2
  • 48
    • 65549096370 scopus 로고    scopus 로고
    • Poly(ethylene glycol)-modified proteins: Implications for poly(lactide-co-glycolide)-based microsphere delivery
    • S.S. Pai, R.D. Tilton, and T.M. Przybycien Poly(ethylene glycol)-modified proteins: implications for poly(lactide-co-glycolide)-based microsphere delivery AAPS J. 11 2009 88 98
    • (2009) AAPS J. , vol.11 , pp. 88-98
    • Pai, S.S.1    Tilton, R.D.2    Przybycien, T.M.3


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