HBEGF
Description
The HBEGF (heparin binding EGF like growth factor) is a protein-coding gene located on chromosome 5.
Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of proteins that in humans is encoded by the HBEGF gene. HB-EGF is synthesized as a membrane-anchored mitogenic and chemotactic glycoprotein. This growth factor is produced by monocytes and macrophages and due to an affinity for heparin is termed HB-EGF. It has been shown to play a role in wound healing, cardiac hypertrophy, and heart development and function. First identified in the conditioned media of human macrophage-like cells, HB-EGF is an 87-amino acid glycoprotein that displays highly regulated gene expression. Ectodomain shedding results in the soluble mature form of HB-EGF, which influences the mitogenicity and chemotactic factors for smooth muscle cells and fibroblasts. The transmembrane form of HB-EGF is the unique receptor for diphtheria toxin and functions in juxtacrine signaling in cells. Both forms of HB-EGF participate in normal physiological processes and in pathological processes including tumor progression and metastasis, organ hyperplasia, and atherosclerotic disease. HB-EGF can bind two locations on cell surfaces: heparan sulfate proteoglycans and EGF-receptors effecting cell-to-cell interactions. HB-EGF has been shown to interact with NRD1, Zinc finger and BTB domain-containing protein 16, and BAG1. These interactions influence cell cycle progression, molecular chaperone regulation, cell survival, cellular functions, adhesion, and mediation of cell migration.
HBEGF is also known as DTR, DTS, DTSF, HEGFL.
