Hepatocyte Cell Adhesion Molecule (HEPACAM) is a single-pass type I membrane protein that localizes to the cytoplasmic side of the cell membrane. HEPACAM includes a signal sequence (amino acid 1-33), an extracellular region (amino acid 34-240) with one Ig-like C2-type domain and one Ig-like V-type domain, a transmembrane segment (amino acid 241-261), and a cytoplasmic domain (amino acid 262 - 416). The cytoplasmic domain plays an important role in regulation of cell-matrix adhesion and cell motility. HEPACAM acts as a homodimer and dimer formation occurs predominantly through cis interactions on the cell surface. HEPACAM is involved in cell motility and cell-matrix interactions. The expression of this gene is down-regulated or undetectable in many cancer cell lines, so this may be a tumor suppressor gene.
Hepatocyte growth factor receptor (HGF R) is a glycosylated receptor tyrosine kinase that plays a central role in epithelial morphogenesis and cancer development. HGF R is synthesized as a single chain precursor which undergoes cotranslational proteolytic cleavage. Mature HGF R is a disulfide-linked dimer composed of a 50 kDa extracellular α chain and a 145 kDa transmembrane β chain. Proteolysis and alternate splicing generate additional forms of human HGF R which either lack of the kinase domain, consist of secreted extracellular domains, or are deficient in proteolytic separation of the α and β chains. The sema domain, which is formed by both α and β chains of HGF R, mediates both ligand binding and receptor dimerization. HGF stimulation induces HGF R downregulation via internalization and proteasomedependent degradation. Paracrine induction of epithelial cell scattering and branching tubulogenesis results from the stimulation of HGF R on undifferentiated epithelium by HGF released from neighboring mesenchymal cells.
Hepcidin（HAMP）is a secreted protein that belongs to the hepcidin family.It is expressed in liver, heart and brain. It is involved in the maintenance of iron homeostasis, and it is necessary for the regulation of iron storage in macrophages, and for intestinal iron absorption. The preproprotein is post-translationally cleaved into mature peptides of 20, 22 and 25 amino acids, and these active peptides are rich in cysteines, which form intramolecular bonds that stabilize their beta sheet structures.
Human epidermal growth factor receptor 2 (HER2) is a type of membrane glycoprotein; and belongs to the epidermal growth factor (EGF) receptor family. HER2 plays a key role in development; cell proliferation and differentiation. HER2 has been reported to associate with malignancy and a poor prognosis in numerous carcinomas; including breast; prostate; ovarian; lung cancers and so on. HER2 is activated by dimerization and not activated by EGF; TGF-alpha and amphiregulin. Interaction with PTK6 increases its intrinsic kinase activity.It is heterodimer with EGFR; ERBB3 and ERBB4. HER2 associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. It implicated in transcriptional activation of CDKN1A and the function of the protein involves STAT3 and SRC. And also it involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth.
Epidermal growth factor receptor 2 (HER2), also known as ErbB2, NEU, and CD340, is a type I membrane glycoprotein, and belongs to the epidermal growth factor (EGF) receptor family. HER2 protein cannot bind growth factors due to the lacking of ligand binding domain of its own and autoinhibited constitutively. However, HER2 forms a heterodimer with other ligand-bound EGF receptor family members, therefore stabilizes ligand binding and enhances kinase-mediated activation of downstream molecules. HER2 plays a key role in development, cell proliferation and differentiation. HER2 gene has been reported to associate with malignancy and a poor prognosis in numerous carcinomas, including breast, prostate, ovarian, lung cancers and so on.
ErbB3, also known as Her3(human epidermal growth factor receptor3), is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound glycoprotein has a neuregulin binding domain but has not an active kinase domain., and therefore can not mediate the intracellular signal transduction through protein phosphorylation. However, its heterodimer with ErbB2 or other EGFR members responsible for tyrosine phosphorylation forms a receptor complex with high affinity, and initiates the related pathway which lead to cell proliferation or differentiation. ErbB3 has been shown to implicated in numerous cancers, including prostate, bladder, and breast tumors. This protein has different isoforms derived from alternative splicing variants, and among which, the secreted isoform lacking the intermembrane region modulates the activity of membrane-bound form.
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