Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1994-3-4
|
| pubmed:abstractText |
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.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogens,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/heparin-binding EGF-like growth...
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jan
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
28
|
| pubmed:volume |
269
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
N
|
| pubmed:pagination |
2541-9
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:8300582-Amino Acid Sequence,
pubmed-meshheading:8300582-Animals,
pubmed-meshheading:8300582-Binding Sites,
pubmed-meshheading:8300582-CHO Cells,
pubmed-meshheading:8300582-Cell Division,
pubmed-meshheading:8300582-Cell Line,
pubmed-meshheading:8300582-Chromatography, High Pressure Liquid,
pubmed-meshheading:8300582-Cloning, Molecular,
pubmed-meshheading:8300582-Cricetinae,
pubmed-meshheading:8300582-Epidermal Growth Factor,
pubmed-meshheading:8300582-Escherichia coli,
pubmed-meshheading:8300582-Heparin,
pubmed-meshheading:8300582-Humans,
pubmed-meshheading:8300582-Intercellular Signaling Peptides and Proteins,
pubmed-meshheading:8300582-Mice,
pubmed-meshheading:8300582-Mitogens,
pubmed-meshheading:8300582-Molecular Sequence Data,
pubmed-meshheading:8300582-Recombinant Fusion Proteins,
pubmed-meshheading:8300582-Recombinant Proteins,
pubmed-meshheading:8300582-Tumor Cells, Cultured
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
Characterization of sequences within heparin-binding EGF-like growth factor that mediate interaction with heparin.
|
| pubmed:affiliation |
Scios Nova Inc., Mountain View, California 94043.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|