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
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 -