Co-expression of human protein disulfide isomerase (hPDI) enhances secretion of bovine follicle-stimulating hormone (bFSH) in Pichia pastoris
文献类型： 外文期刊
作者： Huo, Xiangdong 1 ; Liu, Yueyong 2 ; Wang, Xu 2 ; Ouyang, Pingkai 2 ; Niu, Zhengdong 2 ; Shi, Yuhu 3 ; Qiu, Bingsheng;
作者机构： 1.Xinjiang Acad Agr Sci, Inst Microbiol, Urumqi 830000, Peoples R China
2.Xinjiang Acad Agr Sci, Inst Microbiol, Urumqi 830000, Peoples R China; Nanjing Univ Technol, Coll Life Sci & Pharmaceut Engn, Nanjing 210009, Peoples R China; Chinese Acad Sci, Inst Microbiol, Beijing 100080, Peoples R China
3.Xinjiang Acad Agr Sci, Inst Microbiol, Urumqi 830
关键词： bovine follicle-stimulating hormone;protein disulfide isomerase;Pichia pastoris;HIGH-LEVEL SECRETION;ENDOPLASMIC-RETICULUM;GLYCOPROTEIN HORMONES;EXPRESSION SYSTEM;QUALITY-CONTROL;BETA-SUBUNIT;YEAST;OVEREXPRESSION;GONADOTROPINS;CEREVISIAE
期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.65； 五年影响因子：1.548 ）
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收录情况： SCI
摘要： Bovine follicle-stimulating hormone (bFSH) is a pituitary gonadotropin composed of two non-covalently associated polypeptide subunits, which must be glycosylated, folded, and assembled as a heterodimer to be biologically active. Low-level expression of the recombinant bFSH is the factor that limits its usefulness as a superovulation treatment for cows. To increase the production of recombinant bFSH, human protein disulfide isomerase (hPDI) was expressed simultaneously in engineered Pichia strains. The secretion characteristics of bFSH with or without hPDI were examined. The co-expression of bFSH and hPDI is increased to 1.56 mg/l of heterodimer in the culture medium, which is 6-fold higher when compared with the control strain carrying the bFSH gene only. These results may be generally applicable to increase the expression of other glycoprotein hormones in yeast. (C) 2007 Published by Elsevier Inc.
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