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Diabetes, Vol 47, Issue 10 1619-1624, Copyright © 1998 by American Diabetes Association

ARTICLES

Glycated cholecystokinin-8 has an enhanced satiating activity and is protected against enzymatic degradation

FP O'Harte, MH Mooney, CM Kelly and PR Flatt
School of Biomedical Sciences, University of Ulster, Coleraine, Northern Ireland. fpm.oharte@ulst.ac.uk

Monoglycated cholecystokinin octapeptide (CCK-8) (glucitol-Asp1 adduct) modified at the NH2-terminus was prepared under hyperglycemic conditions, purified by high-performance liquid chromatography, and characterized by mass spectrometry (Mr 1228.4 Da) and peptide sequencing. CCK-8 (100 nmol/kg, i.p.) significantly (P < 0.001) reduced voluntary food intake of fasted mice for up to 30 min after its administration, compared with saline-administered controls. Glycated CCK-8 reduced food intake at 30-120 min (P < 0.01 to P < 0.001) and significantly reduced feeding compared with CCK-8 from 60 to 120 min (P < 0.01). In vitro plasma degradation studies indicated that glycated CCK-8 was resistant to the normal rapid enzymatic conversion to CCK fragments. This study demonstrated that CCK-8 is a potent short-term inhibitor of food intake, and that structural modification of this peptide by amino-terminal glycation leads to enhanced satiating activity, partially due to increased resistance to serum aminopeptidase degradation.
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Copyright © 1998 by the American Diabetes Association.