RRC ID 41863
著者 Shin SY, Yokoyama T, Takenouchi T, Munekata E.
タイトル The chemical synthesis and binding affinity to the EGF receptor of the EGF-like domain of heparin-binding EGF-like growth factor (HB-EGF).
ジャーナル J Pept Sci
Abstract Heparin-binding EGF-like growth factor (HB-EGF), which belongs to the EGF-family of growth factors, was isolated from the conditioned medium of macrophage-like cells. To investigate the effect of N- and C-terminal residues of the EGF-like domain of HB-EGF in the binding affinity to the EGF receptor on A431 cell. We synthesized HB-EGF(44-86) corresponding to the EGF-like domain of HB-EGF and its N- or C-terminal truncated peptides. Thermolytic digestion demonstrated three disulfide bond pairings of the EGF-like domain in HB-EGF is consistent with that of human-EGF and human-TGF-alpha. HB-EGF(44-86) showed high binding affinity to EGF-receptor, like human-EGF. The truncation of the C-terminal Leu86 residue from HB-EGF(44-86), HB-EGF(45-86) or HB-EGF(46-86) caused a drastic reduction in the binding affinity to the EGF receptor. These results suggest that the EGF-like domain of HB-EGF plays an important role in the binding to the EGF receptor, and its C-terminal Leu86 residue is necessary for binding with the EGF-receptor. In addition, the deletion of the two N-terminal residues (Asp44-Pro45) from HB-EGF(44-86) caused a 10-fold decrease in relative binding affinity to the EGF receptor. This indicates that the two N-terminal residues of the EGF-like domain of HB-EGF are necessary for its optimal binding affinity to the EGF receptor.
巻・号 9(4)
ページ 244-50
公開日 2003-4-1
DOI 10.1002/psc.450
PMID 12725245
MeSH Amino Acid Sequence Binding Sites Cell Line, Tumor Epidermal Growth Factor / chemical synthesis Epidermal Growth Factor / chemistry* Epidermal Growth Factor / metabolism* ErbB Receptors / metabolism* Heparin-binding EGF-like Growth Factor Humans Intercellular Signaling Peptides and Proteins Peptide Fragments / chemical synthesis Protein Binding Protein Structure, Tertiary Transforming Growth Factor alpha / chemistry
IF 1.877
引用数 4
WOS 分野 CHEMISTRY, ANALYTICAL BIOCHEMISTRY & MOLECULAR BIOLOGY
リソース情報
ヒト・動物細胞 A431(RCB0202)