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J. Biol. Chem., Vol. 269, Issue 4, 2541-2549, Jan, 1994
SA Thompson, S Higashiyama, K Wood, NS Pollitt, D Damm, G McEnroe, B Garrick, N Ashton, K Lau and N Hancock
Heparin-binding (HB) epidermal growth factor (EGF)-like growth factor
(HB-EGF), a member of the EGF protein family, is a potent mitogen for
fibroblasts, smooth muscle cells, and keratinocytes that was initially
identified as a secreted product of macrophage-like cells. HB-EGF and EGF
appear to act on target cells utilizing the same receptor, but HB- EGF is
distinguishable from EGF by its strong affinity for heparin. To facilitate
studies of structure-function relationships in HB-EGF, a bacterial
recombinant expression system was established that produced biologically
active HB-EGF with the expected disulfide bonding pattern. Mutagenesis and
protease digestion studies of the recombinant HB-EGF, coupled with
heparin-binding analyses of synthetic peptides, indicated that the
sequences within HB-EGF mediating its interaction with heparin are located
primarily in a stretch of 21 amino acids characterized by a high content of
lysine and arginine residues. Most of this heparin- binding domain lies in
an amino-terminal region of HB-EGF that has no counterpart in EGF, but a
portion of the 21-residue sequence extends into the EGF-like region of
HB-EGF. In addition, the mutagenesis and synthetic peptide studies
indicated that sequences in HB-EGF lying outside of the 21-residue stretch
can also influence the interaction with heparin. Finally, a synthetic
peptide derived from the 21-residue stretch was found to compete with
HB-EGF for binding to Chinese hamster ovary cells, suggesting that the
heparin-binding sequences in HB-EGF may also mediate the interaction of
this factor with cell surface heparan sulfate proteoglycan.
Characterization of sequences within heparin-binding EGF-like growth factor that mediate interaction with heparin
Scios Nova Inc., Mountain View, California 94043.
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