VEGF

CD31/PECAM-1, or platelet endothelial cell adhesion molecule 1, is a 130-kDa glycoprotein expressed on vascular and hematopoietic cells.  Depending on the cell type, CD31/PECAM-1 expression can be largely localized to cell junctions, playing a role in cell adhesion.  Aside from its role in cellular adhesion, CD31/PECAM-1 is also a large player in a variety of signaling pathways, such as angiogenesis, cell migration, leukocyte transmigration and more.  Specifically, the association and indication of angiogenesis in breast cancer is of interest, given that extensive research shows an

Proliferating cell nuclear antigen (PCNA) plays a crucial role in nucleic acid metabolism as it pertains to DNA replication and repair.  Most noted for its activation of subunits of DNA polymerase, it has also been found to interact with cell-cycle progression proteins.  Modifications of PCNA as a result of cellular response put PCNA in a pivotal position with DNA replication, DNA damage, and chromatin structure and function.  In response to DNA damage, PCNA is ubiquitinated and becomes part of the RAD-6 dependent DNA repair pathway, where it acts as a substrate with a variety of p

Hypoxia inducible factor 1 (HIF-1) is a protein that plays an essential role in hypoxia, or low levels of cellular oxygen.

The synaptonemal complex (SC) is a protein structure that forms during the synapsis of homologous chromosomes during meiosis. This structure is involved in the processes of chromosome synapsis, genetic recombination and subsequent chromosome segregation, and is essential for gametogenesis.

Epithelial-mesenchymal transition (EMT) is a natural process by which epithelial cells lose their polarity and intercellular adhesion, and gain the migratory invasive properties of mesenchymal stem cells that can differentiate into a variety of cell types. EMT is critical to many developmental processes including embryo development and wound healing. However, EMT is also a fundamental step in the initiation of metastasis during cancer progression.

Integrins are a family of transmembrane proteins involved in diverse processes including cell adhesion, signal transduction, cell migration, and differentiation. They exist as heterodimers consisting of noncovalently linked alpha and beta subunits. Integrin complexes span the plasma membrane and link the cytoskeleton with the extracellular matrix. In mammals there are 18 alpha and 8 beta subunits that can assemble into 24 distinct integrin heterodimers with alternative splicing adding even more diversity.

Hypoxia-inducible factor 1 (HIF-1) is a heterodimeric transcription factor consisting of alpha and beta subunits. The levels of functional HIF-1 in the cell depends on the level of oxygen allowing cells to respond to hypoxic conditions. HIF-1α is a ubiquitously expressed protein containing an oxygen-dependent degradation domain that under normal conditions regulates its constant degradation. HIF-1 beta, on the other hand, is a stable constitutively expressed protein that localizes to the nucleus.

Hypoxia-inducible factor 1 (HIF-1) allows cells to respond to changing levels of oxygen in the environment. HIF-1 is a heterodimeric transcription factor consisting of alpha and beta subunits. Under normal conditions HIF-1 alpha is continuously synthesized and degraded. HIF-1 alpha degradation is mediated through an oxygen-dependent degradation domain that is hydroxylated and leads to ubiquitylation and proteolysis. HIF-1 beta on the other hand is constitutively expressed and localizes to the nucleus.

VEGF is homodimeric, disulfide-linked glycoprotein cytokine that serves as the ligand for FLT1 (VEGFR-1 receptor) and FLK1 (VEGFR-2 receptor) tyrosine kinases. It is a key modulator of physiological angiogenesis, vasculogenesis, and endothelial cell growth during basic developmental processes such as embryogenesis, skeletal growth, and reproductive functions.

LYVE1 (lymphatic vessel endothelial hyaluronan receptor-1) is one of the most specific and widely used mammalian lymphatic endothelial markers.It is found in lymph nodes and at the luminal/abluminal surfaces of lymphatic vessels. It is a single-pass type I membrane protein that exists in a disulfide-linked homodimer form. LYVE1 undergoes ligand-dependent internalization and recycling at the cell surface, and exhibits ligand-specific transporter trafficking between intracellular organelles and the plasma membrane.