Very low-density lipoprotein receptor (VLDLR) mediates the binding and uptake of apoE-containing lipoproteins, such as VLDL and beta-VLDL []. It prevents the migration of retinal vascular endothelial cells into the photoreceptor cell layer and subretinal space []and mediates an anti-angiogenic signal in the retina []. It is involved in adipose tissue inflammation and mediates VLDL-induced lipid accumulation and induction of inflammation and ER stress in adipocytes and macrophages [].
Reelin is an extracellular matrix serine protease that regulates neuronal migration during embryonic development and acts as a modulator of synaptic transmission in the adult brain []. Reelin acts on its receptors, VLDLR and ApoER2, acting on cytoskeleton, controlling migration and subsequently positioning and stabilizing the cortical neurons [, , ]. In the adult brain, reelin stabilizes the actin cytoskeleton by inducing cofilin phosphorylation. Decreased Reelin expression causes destabilization of neurons, which could have implications for brain disorders, such as epilepsy and schizophrenia [].
This entry represents the EGF-like domains found in Tenascin and Reelin proteins. A common feature of all EGF-like domains is that they are found in theextracellular domain of membrane-bound proteins or in proteins known to besecreted (exception: prostaglandin G/H synthase). The EGF-like domain includessix cysteine residues which have been shown to be involved in disulfide bonds.The structure of several EGF-like domains has been solved. The fold consistsof two-stranded β-sheet followed by a loop to a C-terminal shorttwo-stranded sheet []. Tenascins are extracellular matrix glycoproteins that act both as integrin ligands and as modifiers of fibronectin-integrin interactions to regulate cell adhesion, migration, proliferation and differentiation. Tenascins are usually composed of repeated epidermal growth factor (EGF)-like domains, fibronectin-type III (FNIII) domains and a C-terminal fibrinogen related domain (FReD) [].Reelin is an extracellular matrix serine protease that regulates neuronal migration during embryonic development and acts as a modulator of synaptic transmission in the adult brain []. Reelin acts on its receptors, VLDLR and ApoER2, acting on cytoskeleton, controlling migration and subsequently positioning and stabilizing the cortical neurons [, , ]. In the adult brain, reelin stabilizes the actin cytoskeleton by inducing cofilin phosphorylation. Decreased Reelin expression causes destabilization of neurons, which could have implications for brain disorders, such as epilepsy and schizophrenia [].
