A novel acylated form of (d-Ala2)GIP with improved antidiabetic potential, lacking effect on body fat stores

Research output: Contribution to journalArticle

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Abstract

BACKGROUND: Rapid enzymatic degradation of the incretin hormone, glucose-dependent insulinotropic polypeptide (GIP), limits therapeutic use of the native peptide for diabetes. However, enzymatically stable analogues of GIP, such as (d-Ala2)GIP, have been generated, but are still susceptible to renal filtration.METHODS: The present study examines the in vitro and in vivo biological actions of a novel, acylated GIP analogue, (d-Ala2)GIP[Lys37PAL].RESULTS: In BRIN-BD11 cells, (d-Ala2)GIP[Lys37PAL] concentration-dependently stimulated (p
LanguageEnglish
Pages3407-3413
JournalBIOCHIMICA ET BIOPHYSICA ACTA
Volume1830
Issue number6
DOIs
Publication statusPublished - 18 Jun 2013

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Hypoglycemic Agents
Adipose Tissue
Glucose
Peptides
Incretins
Therapeutic Uses
Hormones
Kidney

Cite this

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abstract = "BACKGROUND: Rapid enzymatic degradation of the incretin hormone, glucose-dependent insulinotropic polypeptide (GIP), limits therapeutic use of the native peptide for diabetes. However, enzymatically stable analogues of GIP, such as (d-Ala2)GIP, have been generated, but are still susceptible to renal filtration.METHODS: The present study examines the in vitro and in vivo biological actions of a novel, acylated GIP analogue, (d-Ala2)GIP[Lys37PAL].RESULTS: In BRIN-BD11 cells, (d-Ala2)GIP[Lys37PAL] concentration-dependently stimulated (p",
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A novel acylated form of (d-Ala2)GIP with improved antidiabetic potential, lacking effect on body fat stores. / Martin, CM; Irwin, Nigel; Flatt, Peter; Gault, Victor.

Vol. 1830, No. 6, 18.06.2013, p. 3407-3413.

Research output: Contribution to journalArticle

TY - JOUR

T1 - A novel acylated form of (d-Ala2)GIP with improved antidiabetic potential, lacking effect on body fat stores

AU - Martin, CM

AU - Irwin, Nigel

AU - Flatt, Peter

AU - Gault, Victor

PY - 2013/6/18

Y1 - 2013/6/18

N2 - BACKGROUND: Rapid enzymatic degradation of the incretin hormone, glucose-dependent insulinotropic polypeptide (GIP), limits therapeutic use of the native peptide for diabetes. However, enzymatically stable analogues of GIP, such as (d-Ala2)GIP, have been generated, but are still susceptible to renal filtration.METHODS: The present study examines the in vitro and in vivo biological actions of a novel, acylated GIP analogue, (d-Ala2)GIP[Lys37PAL].RESULTS: In BRIN-BD11 cells, (d-Ala2)GIP[Lys37PAL] concentration-dependently stimulated (p

AB - BACKGROUND: Rapid enzymatic degradation of the incretin hormone, glucose-dependent insulinotropic polypeptide (GIP), limits therapeutic use of the native peptide for diabetes. However, enzymatically stable analogues of GIP, such as (d-Ala2)GIP, have been generated, but are still susceptible to renal filtration.METHODS: The present study examines the in vitro and in vivo biological actions of a novel, acylated GIP analogue, (d-Ala2)GIP[Lys37PAL].RESULTS: In BRIN-BD11 cells, (d-Ala2)GIP[Lys37PAL] concentration-dependently stimulated (p

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DO - 10.1016/j.bbagen.2013.03.011

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