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

CM Martin; Nigel Irwin; Peter Flatt; Victor Gault

doi:10.1016/j.bbagen.2013.03.011

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

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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

Original language	English
Pages (from-to)	3407-3413
Journal	BIOCHIMICA ET BIOPHYSICA ACTA
Volume	1830
Issue number	6
DOIs	https://doi.org/10.1016/j.bbagen.2013.03.011
Publication status	Published (in print/issue) - 18 Jun 2013

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SDG 3 Good Health and Well-being

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10.1016/j.bbagen.2013.03.011

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

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",

author = "CM Martin and Nigel Irwin and Peter Flatt and Victor Gault",

year = "2013",

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doi = "10.1016/j.bbagen.2013.03.011",

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volume = "1830",

pages = "3407--3413",

journal = "BIOCHIMICA ET BIOPHYSICA ACTA",

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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

U2 - 10.1016/j.bbagen.2013.03.011

DO - 10.1016/j.bbagen.2013.03.011

M3 - Article

VL - 1830

SP - 3407

EP - 3413

JO - BIOCHIMICA ET BIOPHYSICA ACTA

JF - BIOCHIMICA ET BIOPHYSICA ACTA

IS - 6

ER -

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

Abstract

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