FGF-1: From biology through engineering to potential medical applications

被引：12
作者：
Zakrzewska, Malgorzata [1 ,2 ]
Marcinkowska, Ewa [1 ]
Wiedlocha, Antoni [2 ]
机构：
[1] Univ Wroclaw, Fac Biotechnol, PL-50137 Wroclaw, Poland
[2] Univ Oslo, Rikshosp, Radium Hosp,,Ctr Canc Biomed, Ctr Med,Dept Biochem,Inst Canc Res, N-0027 Oslo, Norway
来源：
CRITICAL REVIEWS IN CLINICAL LABORATORY SCIENCES | 2008年 / 45卷 / 01期
关键词：
FGF-1; FGFR; recombinant protein; protein stability; activity; signaling; clinical application;
D O I：
10.1080/10408360701713120
中图分类号：
R446 [实验室诊断]; R-33 [实验医学、医学实验];
学科分类号：
1001 ;
摘要：
Human fibroblast growth factor 1 (FGF-1) is one of the best characterized members of the FGF superfamily. FGF-1 is a powerful mitogen exhibiting strong action on numerous different cell types. It plays a role in various stages of development and morphogenesis, as well as in angiogenesis and wound healing processes. Engineering of FGFs can bring many advantages. Design and construction of different mutants can contribute to a better understanding of the mechanism of action of protein growth factors. Moreover, application of FGFs as recombinant polypeptides in the treatment of wound and fracture healing, cardiovascular diseases and neurodegenerative diseases seems to be a rational medical approach. However, low thermal stability and high sensitivity to proteases limit the potential pharmaceutical use of wild-type FGFs. Thus, advanced protein design techniques and recombinant protein production can help to obtain new variants of FGFs with radically increased thermodynamic stability, prolonged half-life and improved proteolytic resistance. Such studies can provide a good starting point to convert short-lived and/or sensitive growth factors to effective therapeutic proteins.
引用
收藏
页码：91 / 135
页数：45
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