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

Expression of a fusion protein containing human epidermal growth factor and the collagen-binding... Human epidermal growth factor (hEGF) is a polypeptide of 53 amino acids, is an important autocrine/paracrine factor in the human body, and is used in the pharmaceutical and cosmetics industries. We constructed a fusion hEGF protein with a collagen-binding domain (CBD) composed of 33 amino acids from Vibrio mimicus metalloprotease (VMCBD). The CBD segment of the metalloprotease was fused at the C terminus of the hEGF protein. The recombinant fusion protein was expressed in Escherichia coli and purified. The purified hEGF protein promoted greater growth of human/A-431 cells than did the control hEGF. The fusion EGF protein also showed collagen-binding activity with type I collagen. In contrast, hEGF did not bind to type I collagen. These results suggest that recombinant hEGF protein fused to VMCBD may be able to remain for a long period at injured epidermal tissue acting as a healing agent. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Letters Springer Journals

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

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References (19)

Publisher
Springer Journals
Copyright
Copyright © 2008 by Springer Science+Business Media B.V.
Subject
Life Sciences; Biochemistry, general; Applied Microbiology; Biotechnology; Microbiology
ISSN
0141-5492
eISSN
1573-6776
DOI
10.1007/s10529-008-9863-6
pmid
18931974
Publisher site
See Article on Publisher Site

Abstract

Human epidermal growth factor (hEGF) is a polypeptide of 53 amino acids, is an important autocrine/paracrine factor in the human body, and is used in the pharmaceutical and cosmetics industries. We constructed a fusion hEGF protein with a collagen-binding domain (CBD) composed of 33 amino acids from Vibrio mimicus metalloprotease (VMCBD). The CBD segment of the metalloprotease was fused at the C terminus of the hEGF protein. The recombinant fusion protein was expressed in Escherichia coli and purified. The purified hEGF protein promoted greater growth of human/A-431 cells than did the control hEGF. The fusion EGF protein also showed collagen-binding activity with type I collagen. In contrast, hEGF did not bind to type I collagen. These results suggest that recombinant hEGF protein fused to VMCBD may be able to remain for a long period at injured epidermal tissue acting as a healing agent.

Journal

Biotechnology LettersSpringer Journals

Published: Oct 19, 2008

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