E2F-2 (viral E2-associated factor 2) is a 50 55 kDa member of the E2F/DP family of transcription factors. It is principally expressed by placenta, and forms a DNA activating E2F heterodimeric complex with DP-1 or-2. This complex, when active, promotes cell cycle progression. In quiescent cells, association with the retinoblastoma-tumor suppressor gene product termed pRB suppresses its activity. Human E2F 2 is 437 amino acids (aa) in length and contains a CDK2 binding region (aa 65 105), a DNA binding domain (aa 107 196), a dimerization segment (aa 197 289), a transactivation region (aa 359 437), and a pRB binding domain (aa 410 427). There are two potential alternate start sites at Met197 and Met342, and one splice variant that shows a two aa substitution for aa 349 437. Over aa 308 437, human E2F-2 is 72% aa identical to mouse E2F-2.
EBP1, also known as PA2G4, is an RNA-binding protein which belongs to the peptidase M24 family. It can be detected n several cell lines tested, including primary and transformed cell lines. EBP1 also present in pre-ribosomal ribonucleoprotein complexes and may be involved in ribosome assembly and the regulation of intermediate and late steps of rRNA processing. This protein is a transcriptional co-repressor of androgen receptor-regulated genes and other cell cycle regulatory genes through its interactions with histone deacetylases. PA2G4 can interact with the cytoplasmic domain of the ErbB3 receptor and may contribute to transducing growth regulatory signals. EBP1 has been implicated in growth inhibition and the induction of differentiation of human cancer cells. It seems to be involved in growth regulation. EBP1 also mediates cap-independent translation of specific viral IRESs (internal ribosomal entry site).
Cadherins are calcium-dependent cell adhesion proteins which preferentially interact with themselves in a homophilic manner in connecting cells; and thus may contribute to the sorting of heterogeneous cell type. E-cadherin (E-Cad); also known as CDH1 and CD324; is a calcium-dependent cell adhesion molecule the intact function of which is crucial for the establishment and maintenance of epithelial tissue polarity and structural integrity. Mutations in CDH1 occur in diffuse type gastric cancer; lobular breast cancer; and endometrial cancer. In human cancers; partial or complete loss of E-cadherin expression correlates with malignancy. During apoptosis or with calcium influx; E-Cad is cleaved by the metalloproteinase to produce fragments of about 38 kDa (E-CAD/CTF1); 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3); respectively. E-Cad has been identified as a potent invasive suppressor; as downregulation of E-cadherin expression is involved in dysfunction of the cell-cell adhesion system; and often correlates with strong invasive potential and poor prognosis of human carcinomas.
Cadherins are calcium-dependent cell adhesion proteins which preferentially interact with themselves in a homophilic manner in connecting cells, and thus may contribute to the sorting of heterogeneous cell type. E-cadherin (E-Cad), also known as CDH1 and CD324, is a calcium-dependent cell adhesion molecule the intact function of which is crucial for the establishment and maintenance of epithelial tissue polarity and structural integrity. Mutations in CDH1 occur in diffuse type gastric cancer, lobular breast cancer, and endometrial cancer. In human cancers, partial or complete loss of E-cadherin expression correlates with malignancy. During apoptosis or with calcium influx, E-Cad is cleaved by the metalloproteinase to produce fragments of about 38 kDa (E-CAD/CTF1), 33 kDa (E-CAD/CTF2) and 29 kDa (E-CAD/CTF3), respectively. E-Cad has been identified as a potent invasive suppressor, as downregulation of E-cadherin expression is involved in dysfunction of the cell-cell adhesion system, and often correlates with strong invasive potential and poor prognosis of human carcinomas.
Cdh1 is one of the substrate adaptor protein of the anaphase-promoting complex (APC) in the budding yeast Saccharomyces cerevisiae. Functioning as an activator of the APC/C, Cdh1 regulates the activity and substrate specificity of this ubiquitin E3-ligase.
E-Cadherin is a classical member of the cadherin superfamily. The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein composed of five extracellular cadherin repeats; a transmembrane region; and a highly conserved cytoplasmic tail. Mutations in this gene are correlated with gastric; breast; colorectal; thyroid; and ovarian cancers. Loss of function is thought to contribute to progression in cancer by increasing proliferation; invasion; and/or metastasis. The ectodomain of this protein mediates bacterial adhesion to mammalian cells; and the cytoplasmic domain is required for internalization. Identified transcript variants arise from mutation at consensus splice sites. Also; E-Cadherin has a potent invasive suppressor role and it is a ligand for integrin alpha-E/beta-7.
Endothelin-Converting Enzyme-1 (ECE-1) is a single-pass type I I transmembrane (TM) protein with a short cytoplasmic tail and a large ectodomain. ECE-1 is a zinc protease of the neprilysin (NEP) family, which also includes ECE-2, PEX, XCE, DINE, and Kell, and several NEP-like proteins. It is widely expressed and has several alternatively spliced forms that differ in their TM domain or cytoplasmic tail. All isoforms of ECE-1 are expressed in umbilical vein endothelial cells, polynuclear neutrophils, fibroblasts, atrium cardiomyocytes and ventricles. Endothelin-converting enzyme-1 is involved in the proteolytic processing of Endothelin-1 (EDN1), Endothelin-2 (EDN2), and Endothelin-3 (EDN3) to biologically active peptides. Defects in ECE1 are a cause of Hirschsprung disease, cardiac defects and autonomic dysfunction (HSCRCDAD). It is a form of Hirschsprung disease with skip-lesions defects, craniofacial abnormalities and other dysmorphic features, and autonomic dysfunction.
Endothelin-converting enzyme 2; also known as ECE-2; is a metalloprotease that possesses many properties consistent with it being a neuropeptide-processing enzyme. Endothelin-converting enzymes (ECEs) are the key enzymes in the endothelin (ET) biosynthesis that catalyze the conversion of big ET; the biologically inactive precursor of mature ET. Two enzymes; termed ECE-1 and ECE-2; have been molecularly identified. ECE-2 is found primarily in neural tissues; with high levels of expression in midbrain; cerebellum; hypothalamus; frontal cortex and spinal cord and moderate levels in hippocampus and striatum. ECE-2 is strongly down-regulated in inferior parietal lobe from Alzheimer disease patients (at protein level). ECE-2 converts big endothelin-1 to endothelin-1. It is involved in the processing of various neuroendocrine peptides; including neurotensin; angiotensin I; substance P; proenkephalin-derived peptides; and prodynorphin-derived peptides. ECE-2 may limit beta-amyloid peptide accumulation in brain. It may also have methyltransferase activity. A comparison of residues around the cleavage site revealed that ECE-2 exhibits a unique cleavage site selectivity that is related to but distinct from that of ECE-1.
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