Expression and pharmacological evaluation of fusion protein FGF21-L-Fc.
- Author:
Wen-Bing YAO
1
;
Gui-Ping REN
;
Yang HAN
;
Hong-Wei CAO
;
Hong-Mei GAO
;
Fang-Ming KAN
;
Qi WANG
;
De-Shan LI
Author Information
1. College of Life Science of Northeast Agricultural University, Harbin 150030, China.
- Publication Type:Journal Article
- MeSH:
3T3-L1 Cells;
Adipocytes;
metabolism;
Animals;
Blood Glucose;
metabolism;
Diabetes Mellitus, Experimental;
drug therapy;
metabolism;
Escherichia coli;
metabolism;
Fibroblast Growth Factors;
genetics;
pharmacology;
Glucose;
metabolism;
Immunoglobulin G;
genetics;
pharmacology;
Male;
Mice;
Recombinant Proteins;
genetics;
pharmacology
- From:
Acta Pharmaceutica Sinica
2011;46(7):787-792
- CountryChina
- Language:Chinese
-
Abstract:
FGF21 (fibroblast growth factor 21) is a recently described member of the FGF family. It has been previously demonstrated that FGF21 is a potent regulator of glucose homeostasis. To improve stability of FGF21 for better efficacy, a new form of recombinant FGF21 was generated by fusion of a full length FGF21 gene and the Fc fragment of human IgG4 with flexible linker sequence. To examine the glucose regulation activity of FGF21-L-Fc, 3T3-L1 pre-adipocytes were differentiated into adipocytes, and glucose uptake activity of FGF21-L-Fc was examined by glucose oxidase and peroxidase (GOD-POD) assay. The results showed that in comparison with wild type FGF21, FGF21-L-Fc was more potent in stimulation of glucose uptake by 3T3-L1. In vivo studies on the modified protein demonstrated that FGF-L-Fc had a better efficacy in lowering blood glucose of the STZ-induced diabetic animals and controlled glucose level for a longer time. The results provided a sound basis for further studies.
