Human epidermal growth factor excreted by recombinant Escherichia coli K-12 has the correct N-terminus and is fully bioactive

Huang, RC; Lam, E.; Chen, Y-H.; Lam, TL; Liu, D.; Ma, MC; Siu, KL; Sivakesava, S.; Xu, ZN; Wong, Roderick; Wong, Wan Keung

doi:10.1016/s0032-9592(99)00024-2

Cited by 20 publications

(23 citation statements)

References 17 publications

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“…On the other hand, the exact structural composition and purity of a recombinant product could also affect its performance. Research findings strongly support that authentic rEGF with high purity is remarkably stable, despite its maintenance and usage in the absence of protein stabilizers [12]. In addition, among the great variety of rEGF isoforms reported in the literature, so far, only the authentic form has been shown to exhibit high efficacies, despite through simply topical administration, in promoting wound healing [30].…”

Section: Disparities In Performance Among Different Regf Isoformsmentioning

confidence: 80%

“…A major drawback of the fusion approach is the formation of rEGF as variants possessing different peptide lengths (Table 1) [11][12][13][14][15][16][17][18][19][20][21][22]. Moreover, the EGF derivatives were commonly shown to exhibit lower levels of bioactivity and stability [17,[22][23][24].…”

Section: Approaches Of Expressing Recombinant Egfmentioning

confidence: 99%

“…Moreover, the EGF derivatives were commonly shown to exhibit lower levels of bioactivity and stability [17,[22][23][24]. Later on, pragmatic approaches were developed for the production of not only bioactive and stable rEGF, but also a product available at a much reduced price [11][12].…”

Section: Approaches Of Expressing Recombinant Egfmentioning

confidence: 99%

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2017

JAPLR

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Human epidermal growth factor (EGF) is a functionally versatile polypeptide comprising 53 amino acids (aa). Due to the ability of EGF to stimulate epidermal growth and proliferation, numerous research studies have been conducted to explore its potential applications in cosmetic, skin care and medication. The emergence of recombinant DNA technology has facilitated the production of a great variety of recombinant EGF (rEGF) isoforms. However, increasing evidence supports that rEGF isoforms exhibit different levels of stability and potency. This review discusses how the less bioactive rEGF isoforms may mystify the identity and even the functional properties of authentic rEGF, which shares the same primary structure as native EGF. The identity crisis, the time-consuming, costly and labor-intensive patenting and drug regulatory processes act together to result in underrating the functional applications of authentic rEGF, which have been shown to be effective and safe in promoting treatments of a variety of skin disorders such as diabetic foot ulcers (DFU).

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Section: Disparities In Performance Among Different Regf Isoformsmentioning

confidence: 80%

Section: Approaches Of Expressing Recombinant Egfmentioning

confidence: 99%

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2017

JAPLR

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“…The EGF in the supernatant from an induced EGF-expressing recombinant E. coli culture was readily purified by conventional chromatographic procedures (Huang et al, 1999), and was shown to be pure by high pressure liquid chromatography (Figure 3.3) and 5DS-PAGE (Figure 3.4). The N-terminus of the purified hEGF was authentic (thus: cleavage of the OmpA signal peptide was precise, and degradation from the N-terminus was absent or minimal after excretion of the protein).…”

Section: Scale-up Of Egf Productionmentioning

confidence: 99%

Applications, and Efficient Large-Scale Production, of Recombinant Human Epidermal Growth Factor

Wong

Lam²,

Huang³

et al. 2001

Biotechnology and Genetic Engineering Reviews

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“…In the early 2000s, employing rhEGF prepared from an engineered Escherichia coli excretion system [3][4][5][6], and working with a local hospital, United Christian Hospital, in Hong Kong, we reported the use of rhEGF to successfully enhance the healing rate of DFU [7]. In our protocol, rhEGF resuspended in aqueous cream was demonstrated to be able to dramatically improve the efficacy of complete recovery of DFU wounds.…”

Section: Introductionmentioning

confidence: 96%

Effective Treatment of an Unhealed Incision of a Diabetic Patient with Recombinant Human Epidermal Growth Factor

Wong¹

2015

Mod Chem Appl

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A facile protocol, which involves topical application of recombinant human Epidermal Growth Factor (rhEGF), was previously developed by our group and shown to be effective in treating diabetic foot ulcers, when working in conjunction with debridement surgery. In this communication, using the same approach of rhEGF application, despite the absence of debridement, our findings demonstrated that the protocol worked equally well on a hard-to-heal wound, which remained unhealed subsequent to surgical removal of the great saphenous vein from the left thigh of a diabetic patient. After treatment with rhEGF for 10 d, the wound was shown to heal readily and finally achieved complete healing. The success of rhEGF in the healing process is concluded to be attributable to both the fine quality and sufficient dosage of rhEGF.

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Human epidermal growth factor excreted by recombinant Escherichia coli K-12 has the correct N-terminus and is fully bioactive

Cited by 20 publications

References 17 publications

Untitled

Untitled

Applications, and Efficient Large-Scale Production, of Recombinant Human Epidermal Growth Factor

Effective Treatment of an Unhealed Incision of a Diabetic Patient with Recombinant Human Epidermal Growth Factor

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