Title |
Latent transforming growth factor β-binding protein-3 and fibulin-1C interact with the extracellular domain of the heparin-binding EGF-like growth factor precursor
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Published in |
BMC Molecular and Cell Biology, January 2002
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DOI | 10.1186/1471-2121-3-2 |
Pubmed ID | |
Authors |
Joanna S Brooke, Jeong-Heon Cha, Leon Eidels |
Abstract |
The membrane-bound cell-surface precursor and soluble forms of heparin-binding epidermal growth factor-like growth factor (HB-EGF) contribute to many cellular developmental processes. The widespread occurrence of HB-EGF in cell and tissue types has led to observations of its role in such cellular and tissue events as tumor formation, cell migration, extracellular matrix formation, wound healing, and cell adherence. Several studies have reported the involvement of such extracellular matrix proteins as latent transforming growth factor beta-binding protein, TGF-beta, and fibulin-1 in some of these processes. To determine whether HB-EGF interacts with extracellular matrix proteins we used the extracellular domain of proHB-EGF in a yeast two-hybrid system to screen a monkey kidney cDNA library. cDNA clones containing nucleotide sequences encoding domains of two proteins were obtained and their derived amino acid sequences were evaluated. |
Mendeley readers
Geographical breakdown
Country | Count | As % |
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Demographic breakdown
Readers by professional status | Count | As % |
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Professor | 1 | 17% |
Student > Master | 1 | 17% |
Researcher | 1 | 17% |
Professor > Associate Professor | 1 | 17% |
Other | 0 | 0% |
Unknown | 1 | 17% |
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Unknown | 1 | 17% |