Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B- and E-cadherins as well as about ten other members which are found in adherens junctions (AJ), a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with beta-catenin, gama-catenin (also called plakoglobin) and p120 catenin. beta- catenin and gamma-catenin associate with alpha-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). Unlike beta- and gamma-catenin, p120 regulates cadherin adhesive activity and trafficking rather than having a structural role in the junctional complex (1–4). E-cadherin is considered an acting suppressor of invasion and growth of many epithelial cancers (1–3). Recent studies indicate that cancer cells have up-regulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-Cadherin cooperates with the FGF receptor, leading to over-expression of MMP-9 and cellular invasion (3). In endothelial cells, VE-cadherin signaling, expression and localization are correlated with vascular permeability and tumor angiogenesis (5,6).
Product | Size | List | Your Price | Qty | Ext Price | ||||
---|---|---|---|---|---|---|---|---|---|
Subtotal: | Subtotal: | ||||||||
Subtotal: | Subtotal: | ||||||||
Total Coupon Savings: | Total Coupon Savings: | () | |||||||
Your cart is currently empty. | |||||||||
- Coupon Code |