| First Author | Raab G | Year | 1997 |
| Journal | Biochim Biophys Acta | Volume | 1333 |
| Issue | 3 | Pages | F179-99 |
| PubMed ID | 9426203 | Mgi Jnum | J:45088 |
| Mgi Id | MGI:1101716 | Doi | 10.1016/s0304-419x(97)00024-3 |
| Citation | Raab G, et al. (1997) Heparin-binding EGF-like growth factor. Biochim Biophys Acta 1333(3):F179-99 |
| abstractText | HB-EGF is a heparin-binding member of the EGF family that was initially identified in the conditioned medium of human macrophages. Soluble mature HB-EGF is proteolytically processed from a larger membrane-anchored precursor and is a potent mitogen and chemotactic factor for fibroblasts, smooth muscle cells but not endothelial cells. HB-EGF activates two EGF receptor subtypes, HER1 and HER4 and binds to cell surface HSPG. The transmembrane form of HB-EGF is a juxtacrine growth and adhesion factor and is uniquely the receptor for diphtheria toxin. HB-EGF gene expression is highly regulated, for example by cytokines, growth factors, and transcription factors such as MyoD. HB-EGF has been implicated as a participant in a variety of normal physiological processes such as blastocyst implantation and wound healing, and in pathological processes such as tumor growth, SMC hyperplasia and atherosclerosis. |
