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KMID : 0624620090420040212
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BMB Reports
2009 Volume.42 No. 4 p.212 ~ p.216
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Fc fusion to Glucagon-like peptide-1 inhibits degradation by human DPP-IV, increasing its half-life in serum and inducing a potent activity for human GLP-1 receptor activation
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Kim Dong-Myung
Chu Seoung-Ho
Kim Se-Mi
Park Young-Woo
Kim Sung-Seob
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Abstract
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The short in vivo half-life of GLP-1 prevents it from being used clinically. This short half-life occurs because GLP-1 is rapidly degraded by dipeptidyl peptidases such as DPP-IV. To overcome this obstacle, a GLP-1/Fc was constructed and evaluated to determine if it was degraded by DPP-IV and in serum. When the degradation of GLP-1/Fc by human DPP-IV and rabbit serum was compared with that of GLP-1 it was found to be reduced by approximately 5- and 4-fold, respectively. Furthermore, GLP-1/Fc showed a potent activity for human GLP-1 receptor activation (EC50 approximately 6 nM). Taken together, these results indicate that GLP-1/Fc may have an extended half-life in vivo that occurs as a result of inhibition of degradation by human DPP-IV. Due to the extended half life, GLP-1/Fc may be useful for clinical treatments.
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KEYWORD
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Diabetes, Dipeptidyl peptidase-IV, GLP-1 receptor, Glucagonlike peptide-1, IgG-Fc
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