Tumor

c-Myc, a proto-oncogene, has documented involvement in cellular differentiation, cell growth, cell death and tumor formation.  Target genes of the Myc family include those that participate in cell survival, translation, transcription, metabolism and more.  On a more specific level, c-Myc is a transcription factor that can both activate and repress its target protein by way of DNA modifications.  This allows for the use of a c-Myc antibody in two manners; it can be used to monitor the actual c-Myc protein expression levels, or, it

FSH R, or follicle-stimulating hormone receptor, is a transmembrane G-protein coupled receptor that is expressed in the ovaries, uterus, and testes. The ligand for this receptor, considered to be the central hormone of mammalian reproduction, is called follicle stimulating hormone (FSH) [1]. In females, FSH R is essential for proper ovarian development and follicle maturation. In males, it is required for normal spermatogenesis.

The aryl hydrocarbon receptor (AHR) is a ligand activated transcription factor that controls the expression of a diverse set of genes. In the absence of ligand, AHR is retained in the cytoplasm. Upon ligand binding AHR translocates to the nucleus where it forms a heterodimer with aryl hydrocarbon receptor nuclear translocator (ARNT) (1). This receptor complex then recognizes AHR-response elements in target genes to regulate their transcription.

Succinate dehydrogenase (SDH) is a highly conserved protein complex located on the inner mitochondrial membrane where it functions during the Krebs cycle by oxidizing succinate to fumarate (1). This reaction is also important for feeding electrons into the electron transport chain. SDH complex contains four subunits: SDH-A, -B, -C, and -D. Mutation of SDH-A often leads to mitochondrial encephalopathy while mutations to subunits B, C, and D lead to tumors of the head and neck (1).

UV resistance-associated gene (UVRAG) is a tumor suppressor that is commonly mutated in colon and breast cancer. While UVRAG was discovered for its ability to complement UV sensitivity in xeroderma pigmentosum cells, its main functions are in autophagy, endocytosis, and apoptosis. During autophagy UVRAG interacts with Beclin 1 to promote autophagosome formation. UVRAG can also interact with VPS16 to recruit membrane fusion machinery to mediate autophagosome maturation.

Akt1 is one of three isoforms of Akt belonging to the AGC family of serine/threonine kinases (Akt1, Akt2, and Akt3). All Akt isoforms contain an N-terminal Plekstrin Homology (PH) domain, a C-terminal regulatory domain, and a central catalytic kinase domain (1). Akt is a major downstream target of the PI3-K signaling pathway. The Akt1 isoform is fully activated by phosphorylation at three sites- T308, T450, and S473. Akt1 resides in an inactive state due to intramolecular interactions between the PH domain and the kinase domain.

TSC2 is a tumor suppressor gene that encodes a 200 kDa protein called tuberin. TSC2 heterodimerizes with TSC1 to form a complex with GTPase-activating protein (GAP) activity. The C-terminus of TSC2 contains the GAP domain responsible for this catalytic activity. The complex was first discovered through its role in the tumor-forming condition Tuberous Sclerosis. Mutations in TSC1 and TSC2 can either destabilize the complex or compromise the GAP activity. The TSC1-TSC2 complex acts as a GAP for the small G-protein Rheb, expressed ubiquitously throughout the body (1).

TSC1 is a tumor suppressor gene that encodes a 130 kDa protein called hamartin. TSC1 was first identified as an oncogenic driver of Tuberous Sclerosis, a condition characterized by numerous benign tumors of the skin, brain, heart, and lungs. A mutation in TSC1 is responsible for the uncontrolled growth characteristic of these tumors. This discovery led to a greater understanding of the physiologic role of TSC1 as a negative cell cycle regulator. The distinct but related gene TSC2 encodes a 200 kDa protein called tuberin.

Matrix metalloproteinases (MMPs) are responsible for the degradation of extracellular matrix proteins. MMPs are essential for tissue remodeling during normal processes such as embryonic development as well as pathological conditions such as arthritis and tumor metastasis. MMP3, a member of the stromelysin family, has broad specificity for proteins such as collagens, fibronectin, proteoglycans, and elastin making it an important player in extracellular matrix remodeling. These activities are especially important during tumorigenesis by enhancing epithelial to mesenchymal transition.

The vertebrate fibroblast growth factor receptor (FGFR) family is an important group of proteins involved in embryonic development and the growth and proliferation of adult cells. Mutations in FGFR proteins can lead to pathologies including bone or limb defects and various forms of cancer. FGFR proteins are receptor tyrosine kinases that, upon ligand binding, dimerize and signal through the MAPK and PLCγ pathways.