Document Detail


Cell migration-promoting and apoptosis-inhibiting activities of Bm-TFF2 require distinct structure basis.
MedLine Citation:
PMID:  20816935     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human trefoil factors (TFFs) play an important role in wound healing, epithelial restitution and anti-inflammatory effects in the gastrointestinal tract by stimulating cell migration and inhibiting cell apoptosis. In our previous study, Bm-TFF2, an amphibian trefoil factor, which is isolated from the skin secretions of frog Bombina maxima, has much stronger activities than human TFFs. We believe that the expression of the recombinant Bm-TFF2 in vitro is useful to decipher its role in amphibian skin repair. Bm-TFF2 contains 12 cysteine residues and has two TFF-domains. In this study, we expressed full-length of Bm-TFF2 and its single-domain truncations (Bm-TFF2-D1 and Bm-TFF2-D2, each contains a single TFF-domain of Bm-TFF2). The recombinant proteins, including full-length and its single-domain truncations of Bm-TFF2, can promote the migration of human epithelial AGS cells and wound healing of rat intestinal epithelial IEC-6 cells. However, only the full-length of Bm-TFF2, but not its single-domain truncations, can inhibit ceramide-induced apoptosis in AGS cells. In summary, it is the first time to use the recombinant Bm-TFF2 and its truncations to investigate its structure-function relationship. And we report that full-length and each domain of Bm-TFF2 can induce cell migration but only the full-length of Bm-TFF2 can suppress apoptosis, indicating that cell migration-promoting and apoptosis-inhibiting activities of Bm-TFF2 require distinct structure basis.
Authors:
Guoyu Yu; Yong Zhang; Yang Xiang; Ping Jiang; Zhongming Chen; Wenhui Lee; Yun Zhang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-09-09
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  400     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2010 Oct 
Date Detail:
Created Date:  2010-10-04     Completed Date:  2010-11-23     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  724-8     Citation Subset:  IM    
Copyright Information:
Copyright © 2010 Elsevier Inc. All rights reserved.
Affiliation:
Key Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences & Yunnan Province, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650223, China.
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MeSH Terms
Descriptor/Qualifier:
Animals
Anura
Apoptosis*
Cell Line, Tumor
Cell Movement*
Humans
Mitogen-Activated Protein Kinase 1 / metabolism
Mitogen-Activated Protein Kinase 3 / metabolism
Peptides / chemistry,  genetics,  physiology*
Phosphorylation
Protein Structure, Tertiary / genetics
Rats
Recombinant Proteins / genetics
Regeneration
Skin Physiological Phenomena*
Wound Healing*
Chemical
Reg. No./Substance:
0/Peptides; 0/Recombinant Proteins; 146046-78-8/trefoil factor; EC 2.7.11.24/Mitogen-Activated Protein Kinase 1; EC 2.7.11.24/Mitogen-Activated Protein Kinase 3

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