베이직 섬유아 세포 성장인자의 안정화 요인 검색

Abstract

Fibroblast growth factor1 (FGF1), the paracrine that activates signaling tyrosine kinase FGF receptors (FGFRs) with heparin or heparan sulfate (HS), is generally known to play important roles in embryonic development, wound healing, neurogenesis, angiogenesis, nutrient stress, glycaemic control and insulin sensitivity and therefore regarded as one of potential therapeutic proteins. However, FGFs must overcome low stability to be used as a medication. Our study based on structures model of paracrine FGFs (FGF1/FGF2) that tightly binds to heparin and BME showed that sulfur compound or reducing agents improved stability although requiring relatively high concentration to show the effect. The results will help studying and enhancing the stability of FGF1.nesis, angiogenesis, nutrient stress, glycaemic control and insulin sensitivity and therefore regarded as one of potential therapeutic proteins. However, FGFs must overcome low stability to be used as a medication. Our study based on structures model of paracrine FGFs (FGF1/FGF2) that tightly binds to heparin and BME showed that sulfur compound or reducing agents improved stability although requiring relatively high concentration to show the effect. The results will help studying and enhancing the stability of FGF1.