Insulin signaling in adipocytes: Carbohydrate-signaling transcription factor ChREBP is the link between lipolytic enzyme Hormone-Sensitive Lipase and lipogenic enzyme ELOVL6

mTOR Signaling and the Tumor Microenvironment

Novel Insights into Hypoxia Induced AKT Signaling

Hypoxia is a common feature of most tumors and is a product of rapid cell growth and poor vascularization1. When oxygen availability is low in the tumor environment, the hypoxia inducing transcription factors (HIFs) regulate a variety of signaling programs that can affect the balance between tumor cell apoptosis2 and autophagy3.  In normoxia, HIFs are bound by the von Hippel-Lindau protein (VHL) in the cytosol where it is degraded by the proteasome, however, under hypoxia HIFs are translocated to the nucleus where they activate survival signals.

Pathway Highlight: Three key factors that contribute to cellular heterogeneity in apoptosis

Have you ever wondered why cells in the same population respond differently to an apoptotic stimulus? Apoptosis, a form of programmed cell death, is vital for the removal of unwanted or damaged cells. As with most cellular processes, too much or too little activation can be detrimental and lead to various diseases including autoimmune disorders and cancer.

The role of c-Fos in the regulation of the JC virus gene transcription

c-Fos is a member of the AP-1 transcription factor family under the Fos protein family umbrella, alongside Fra-1, Fra-2 and Fos-B.  Also in the AP-1 transcription family are the Jun proteins, c-Jun, Jun-B and Jun-D.  Each member of the AP-1 transcription family is a phosphonuclear protein composed of a carboxy-terminal leucine zipper domai

Pathway Highlight: Which caspase substrates contribute to the morphological features associated with apoptosis?

Apoptosis, or programmed cell death, is controlled by a caspase signal cascade that activates downstream signals to induce the morphological changes used to differentiate apoptosis from other forms of cell death.  Novus Biologicals offers a variety of antibodies and tools to detect the different morphological indicators of cell death. 

The use of apoptosis antibodies and controls in cell death research

Apoptosis is a method of programmed cell death that is notably characterized by a morphological change in cellular nuclei and membrane appearance.  Not to be confused with necrosis, apoptosis is a pathway that is induced by a variety of factors that activate cysteine proteases known as caspases to lead the cell to its ultimate death versus natural death of a cell.

The role of Parkin and autophagy in retinal pigment epithelial cell (RPE) degradation

The root of Parkinson’s disease (PD) points to a poorly regulated electron transport chain leading to mitochondrial damage, where many proteins need to work cohesively to ensure proper function.  The two key players of this pathway are PINK1, also known as PTEN or PARK6, and Parkin, also known as PARK2 - where PINK1 acts as an upstream effector of Parkin to regulate mitochondrial dynamics.  Mitochondria must maintain a healthy equilibrium and do so by undergoing a series of fission and fusion event

The use of the autophagy marker LC3 in western blot, immunocytochemistry and flow cytometry research applications as an indicator of autophagy

The process of autophagy, or lysosome-mediated degradation of damaged proteins and organelles in the cytosol, is a vital cellular process that acts as a quality control mechanism for proteins and organelles. The misregulation of autophagy can lead to an imbalance of cellular homeostasis and the subsequent development of disease.  Therefore, the study of autophagy is at the forefront of neuroscience and cancer research, among others.

4EBP1 and skeletal muscle protein synthesis

Eukaryotic translation initiation factor 4E binding protein 1, or 4EBP1, is an mRNA translational repressor protein that negatively regulates eukaryotic translation initiation factor 4E, or EIF4E.  EIF4E is a protein that forms a complex necessary to block the 5’ ends of mRNA with a 7-methyl-guanosine five-prime cap structure, which is important for normal translation of mRNA.  Specifically, the EIF4E complex recruits 40s ribosome subunits to scan mRNA in order to regulate protein synthesis.  When EIF4E is bound to 4EBP1, it is held in an