Teratocarcinoma-derived growth factor 1(TDGF1) is a Cell membrane protein and contains 1 EGF-like domain. The protein plays an essential role in embryonic development and tumor growth. Mutations in this gene are associated with forebrain defects. It also may play a role in the determination of the epiblastic cells that subsequently give rise to the mesoderm.
Cripto/TDGF1 is a member of the epidermal growth factor (EGF)- Cripto, Frl-1, and Cryptic (CFC) family. EGF-CFC family member proteins share a variant EGF-like motif, a conserved cysteine-rich domain, and a C-terminal hydrophobic region. Before gastrulation, Cripto is asymmetrically expressed in a proximal–distal gradient in the epiblast, and subsequently is expressed in the primitive streak and newly formed embryonic mesoderm. These proteins play key roles in intercellular signaling pathways during vertebrate embryogenesis. Mutations in Cripto/TDGF1 can cause autosomal visceral heterotaxy. Cripto/TDGF1 is involved in left-right asymmetric morphogenesis during organ development. Cripto signalling is essential for the conversion of a proximal–distal asymmetry into an orthogonal anterior–posterior axis. The mechanism of inhibitory effects of the Cripto includes both cancer cell apoptosis, activation of c-Jun-NH(2)-terminal kinase and p38 kinase signaling pathways and blocking of Akt phosphorylation. Thus, Cripto is a unique target, and Immunohistochemistry to Cripto could be of therapeutic value for human cancers.
Plexin Domain-Containing Protein 1 (PLXDC1) is a single-pass type I membrane protein that belongs to the plexin family. Secreted PLXDC1 is localized predominantly at the tight junctions of vascular endothelial cells and to a lesser extent at the luminal surface of vascular endothelial cells. PLXDC1 is expressed in fibrovascular membrane with increased expression in individuals with proliferative diabetic retinopathy. It can detect in endothelial cells from colorectal cancer, and in endothelial cells from primary cancers of the lung, liver, pancreas, breast and brain. PLXDC1 interacts with NID1 and may also interact with CTTN. It plays a important role in endothelial cell capillary morphogenesis, the proliferation and maintenance of neovascular endothelial cells in the formation of fibrovascular membranes (FVMs).
ANTXR1 contains 1 VWFA domain and belongs to the ATR family. ATR (Ataxia telangiectasia and Rad3 related) and ATM (Ataxia telangiectasia mutated) are closely related kinases that are activated by DNA damage. They are serine-threonine protein kinases and belongs to the phosphatidylinositol 3' kinase-like kinase (PIKK) family. Upon recruitment by the DNA damage binding proteins/complexes (ATRIP for ATR; MRN for ATM); ATM/ATR initiate the DNA damage checkpoint by phosphorylating a number of key proteins. ANTXR1 interacts with extracellular matrix proteins and with the actin cytoskeleton. It functions in cell attachment and migration. ANTXR1 also mediates adhesion of cells to type 1 collagen and gelatin; reorganization of the actin cytoskeleton and promotes cell spreading. It plays a role in the angiogenic response of cultured umbilical vein endothelial cells.
Anthrax Toxin Receptor 1 (ANTXR1) is a single-pass type I membrane protein that belongs to the ATR family. ANTXR1 contains one VWFA domain and binds PA through the VWA domain. ANTXR1 is highly expressed in tumor endothelial cells. ANTXR1 plays a role in cell attachment and migration. ANTXR1 interacts with extracellular matrix proteins and the actin cytoskeleton; it mediates adhesion of cells to type 1 collagen and gelatin; reorganization of the actin cytoskeleton and promotes cell spreading. It is also involved in the angiogenic response of cultured umbilical vein endothelial cells; up-regulated in cultured angiogenic umbilical vein endothelial cells. Defects in ANTXR1 are associated with susceptibility to hemangioma capillary infantile (HCI).
Telomeric repeat binding factor 1 (TRF1), also known as TERF1, the shelterin complex, which modulates the telomere structures. TRF1 protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Pin2/TRF1 was originally identified as a protein bound to telomeric DNA (TRF1) and as a protein involved in mitotic regulation (Pin2). Pin2/TRF1 negatively regulates telomere length and importantly, its function is tightly regulated during the cell cycle, acting as an important regulator of mitosis. TRF1 can be bound and modulated by two nucleolar GTP-binding proteins, nucleostemin (NS) and guanine nucleotide binding protein-like 3-like (GNL3L), which exhibit apparently opposite effects on the protein degradation of TRF1. TRF1/TERF1 may has association with cancer. TRF1 may play a significant role in cell differentiation in non-small cell lung cancer (NSCLC). The expression level of TRF1 protein is significantly reduced in kidney cancer and the level is negatively correlated with malignant degree of the cancer. TRF1 expression in malignant gliomas cells, may play a role in the malignant progression of astroglial brain tumors.
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