Expression of a fusion protein containing human epidermal growth factor and the collagen-binding domain of Vibrio mimicus metalloprotease

Kim, Dong-Gyun; Min, Mun-kyeong; Ahn, Soon Cheol; Kim, Joong Kyun; Kong, In‐Soo

doi:10.1007/s10529-008-9863-6

Cited by 13 publications

(20 citation statements)

References 16 publications

(54 reference statements)

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“…Many studies have attempted to overcome these tissue engineering problems [21]. Therefore, many researchers focused on diverse bioactive materials and investigated multifunctional and anti-rejection agents, including human growth factors [14].…”

Section: Introductionmentioning

confidence: 99%

“…These growth factors are produced by various cell types, and play key roles in tissue production, regeneration, and differentiation during wound healing [11,17,18,21,23,25]. Therefore, these molecules are important industrial compounds in tissue engineering [14,21]. The effect of growth factors on wound healing is well understood, and human epidermal growth factor (hEGF, 6 kDa) is known to have various functions in diverse epidermal cell types [2,9].…”

Section: Introductionmentioning

confidence: 99%

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Construction of Chimeric Human Epidermal Growth Factor Containing Short Collagen-Binding Domain Moieties for Use as a Wound Tissue Healing Agent

Kim¹,

Kim²,

Kim³

et al. 2015

Journal of Microbiology and Biotechnology

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Among the various human growth factors, epidermal growth factor (hEGF, consisting of 53 amino acids) has various effects on cell regeneration, stimulation of proliferation, migration of keratinocytes, formation of granulation tissues, and stimulation of fibroblast motility, which are important for wound healing. Owing to their multiple activities, EGFs are used as pharmaceutical and cosmetic agents. However, their low productivity, limited target specificity, and short half-life inhibit their application as therapeutic agents. To overcome these obstacles, we fused the collagen-binding domain (CBD) of Vibrio mimicus metalloprotease to EGF protein. About 18 or 12 amino acids (aa) (of the 33 total amino acids), which were essential for collagen-binding activity, were combined with the N- and C-termini of EGF. We constructed, expressed, and purified EGF (53 aa)-CBD (18 aa), EGF (53 aa)-CBD (12 aa), CBD (18 aa)-EGF (53 aa), and CBD (12 aa)-EGF (53 aa). These purified recombinant proteins increased the numbers of cells in treated specimens compared with non-treated specimens and control hEGF samples. The collagen-binding activities were also evaluated. Furthermore, CBD-hybridized hEGF induced phosphorylation of the EGF receptor. These results suggested that these fusion proteins could be applicable as small therapeutic agents in wound tissue healing.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Construction of Chimeric Human Epidermal Growth Factor Containing Short Collagen-Binding Domain Moieties for Use as a Wound Tissue Healing Agent

Kim¹,

Kim²,

Kim³

et al. 2015

Journal of Microbiology and Biotechnology

Self Cite

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“…Thus, EGF is an influential molecule involved in multiple biological processes. Epidermal growth factor is produced using genetic techniques, such as expression in E. coli [10,11], Bacillus brevis [12,13], or Pichia pastoris [14,15].…”

Section: Discussionmentioning

confidence: 99%

Expression of gallus epidermal growth factor (gEGF) with food-grade Lactococcus lactis expression system and its biological effects on broiler chickens

Zhou

Chen

Shi

et al. 2019

Preprint

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“…Thus, EGF is an in uential molecule involved in multiple biological processes. Epidermal growth factor is produced using genetic techniques, such as expression in E. coli [10,11], Bacillus brevis [12,13], or Pichia pastoris [14,15].…”

Section: Introductionmentioning

confidence: 99%

Expression of gallus epidermal growth factor (gEGF) with food-grade Lactococcus lactis expression system and its biological effects on broiler chickens

Zhou

Chen

Shi

et al. 2020

Preprint

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Background Epidermal growth factor (EGF) is a multifunctional polypeptide, which could be utilized to solve problems in the industry such as increasing growth performance of commercial broilers or enhancing resistance to diseases under adverse conditions. Thus far, very few studies have focused on the gallus epidermal growth factor (gEGF) despite the availability of a plethora of studies on mammalian EGF. The aim of this study was to express gallus epidermal growth factor (gEGF) using a food-grade Lactococcus lactis expression system and to investigate its biological effects on broiler chickens. Results A recombinant Lactococcus lactis, which produced the secretary form of bioactive gEGF at 2.67 μg/mL in culture supernatant, was generated. In vitro testing denoted that gEGF promoted the proliferation of UMNSAH/DF-1 cells. Sixty-three 5-day-old broiler chickens were divided into three groups and treated with either M17 medium (C, as control), supernatant of LL-pNZ8149 fermentation product (P-LL), or supernatant of LL-pNZ8149-gEGF fermentation product (gEGF-P-LL). Body weight (BW), average daily gain (ADG), and the gain:feed ratio of the gEGF-P-LL group were significantly higher than those of the other groups during the two-week study. In addition, two weeks after therapy, the indices of spleen and thymus gland, levels of serum IgA, IgG and duodenum mucosal sIgA were all significantly higher in the gEGF-P-LL group than in the other groups. Moreover, the villus height of the duodenum, jejunum and ileum and crypt depth of the jejunum of the gEGF-P-LL group were significantly higher than those of the other groups, while the crypt depth of the duodenum showed the opposite pattern during the two-week study. Conclusions The bioactive gEGF could be expressed with Lactococcus lactis expression system. Furthermore, gEGF has the potential to enhance growth performance, immune function, and intestinal development in broiler chickens.

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Expression of a fusion protein containing human epidermal growth factor and the collagen-binding domain of Vibrio mimicus metalloprotease

Cited by 13 publications

References 16 publications

Construction of Chimeric Human Epidermal Growth Factor Containing Short Collagen-Binding Domain Moieties for Use as a Wound Tissue Healing Agent

Construction of Chimeric Human Epidermal Growth Factor Containing Short Collagen-Binding Domain Moieties for Use as a Wound Tissue Healing Agent

Expression of gallus epidermal growth factor (gEGF) with food-grade Lactococcus lactis expression system and its biological effects on broiler chickens

Expression of gallus epidermal growth factor (gEGF) with food-grade Lactococcus lactis expression system and its biological effects on broiler chickens

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