Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10873626 | FEBS Letters | 2005 | 4 Pages |
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 â20-50 μg 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.
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Authors
Koichi Sugita, Saori Endo-Kasahara, Yoshifumi Tada, Yang Lijun, Hiroshi Yasuda, Yuji Hayashi, Takahito Jomori, Hiroyasu Ebinuma, Fumio Takaiwa,