Abstract Glucagon-like peptide-1 (7-36) amide (GLP-1) is the
most potent physiological insulinotropic hormone in humans. We
produced large amounts of a GLP-1 analogue, [Ser8, Gln26,
Asp34]-GLP-1, which is resistant to trypsin-digestion, as part
of a chimeric rice seed storage protein, a 26 kDa globulin, in
genetically modified rice seeds. Junction sites between GLP-1
analogue and globulin were replaced by tryptic cleavage sites.
The highest level of GLP-1 analogue accumulation was %20–
50 lg per seed. We found that GLP-1 analogue derived from
trypsin-digested genetically modified rice seeds stimulated insulin
secretion from a mouse pancreatic beta-cell line, MIN6.
Ó 2005 Federation of European Biochemical Societies. Published
by Elsevier B.V. All rights reserved.
Keywords: Glucagon-like peptide-1; Insulin; Diabetes;
Globulin; Genetically modified rice