Secretory expression and characterization of a recombinant-deleted variant of human hepatocyte growth factor in<i>Pichia pastoris</i>

Liu, Zhimin; Zhao, Hongfeng; Xue, Cong; Deng, Bingbing; Zhang, Wei; Xiong, Xiang-Hua; Yang, Bing-Fen; Yao, Xue-Qin

doi:10.3748/wjg.v11.i45.7097

Cited by 5 publications

(1 citation statement)

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“…The generation of rcHGF was higher than the previously reported production of rhHGF using insect (Wang et al, 2000;Yee et al, 1993) or mammalian cells (Nakamura et al, 1989). The use of other production systems, for instance the yeast Pichia pastoris (Liu et al, 2005) may yield even higher quantities of >500 mg/L recombinant HGF. When the effects of post-transcriptional modifications such as glycosylation (Fukuta et al, 2005) are fully known in vivo, the use of other production systems, such as non-eukaryotic cells may offer a tool for mass production of rcHGF.…”

Section: Discussionmentioning

confidence: 47%

In vitro and in vivo bioactivity of recombinant canine hepatocyte growth factor

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Hoffmann

et al. 2008

The Veterinary Journal

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Hepatocyte growth factor (HGF) is crucial for the development and regeneration of the liver and offers a possible new therapeutic strategy for the treatment of canine liver disease. In this study, the in vitro and in vivo bioactivity of recombinant canine HGF (rcHGF) produced with a baculoviral expression system in insect cells was measured.In vitro rcHGF induced mitogenesis, motogenesis, and phosphorylated the HGF receptor c-MET and its downstream mediators PKB and ERK1/2 in two canine epithelial cell lines. After a partial hepatectomy (phx) in dogs, rcHGF increased phosphorylation of c-MET, PKB and ERK1/2. A moderate increase was seen with the cell cycle protein PCNA in rcHGF treated livers, but no HGF-induced increase in liver weight was seen 7 days after phx. Furthermore, rcHGF treated livers showed lower levels of the key mediator of apoptosis, caspase-3, at 7 days after phx. It is concluded that rcHGF is a biologically active protein in vitro and in vivo and the baculoviral expression system supplies sufficient amounts of rcHGF for future clinical studies in dogs.

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