Abstract
Glucagon-like peptide-1 (7–36) amide (GLP-1), a gut hormone released into the blood stream after feeding, can stimulate insulin secretion by potentiating the insulinotropic action of glucose. An expression vector pET-22bG8, encoding a fusion protein containing eight tandem repeat GLP-1 ([Ser8, Gln26, Asp34]-GLP-1) analogues, was constructed and transformed into the Escherichia coli BL21(DE3) strain over-expressing the His-tagged fusion protein under the IPTG promoter. SDS-PAGE and Western blot analysis demonstrated that the His-tagged GLP-1 fusion protein migrated as a single protein with a molecular weight of 32 kDa. Following chronic (10 days) oral administration (20 mg kg−1 day−1) of the fusion protein to diabetic rats, serum glucose levels were significantly lowered from 26 ± 2.5 to 7.9 ± 1.4 mmol/l. Further studies are needed to evaluate the potential use for GLP-1 analogue short peptide in the treatment of diabetes mellitus.
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This research was supported by 863 Project funds (No. 2002AA213061) in P. R. China.
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J. H. Hou and R. X. Yan contributed equally to this work.
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Hou, J., Yan, R., Ding, D. et al. Oral administration of a fusion protein containing eight GLP-1 analogues produced in Escherichia coli BL21(DE3) in streptozotocin-induced diabetic rats. Biotechnol Lett 29, 1439–1446 (2007). https://doi.org/10.1007/s10529-007-9427-1
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DOI: https://doi.org/10.1007/s10529-007-9427-1