Recombinant Mouse Reelin Protein

Reelin is secreted by Cajal-Retzius cells in the embryo (1, 4, 11). In the adult, it is expressed in the subventricular zone, rostral migratory stream, olfactory bulb, and in the CA1, CA3, and dentate gyrus regions of the hippocampus, as well as in cerebellar granule cells, pyramidal cells of the entorhinal cortex, GABA interneurons, and glial cells (1, 6, 12, 13). Reelin utilizes the receptors VLDLR and ApoE R2, which have been suggested to have divergent roles in Reelin-mediated neuronal migration (1, 2, 6, 12). It has also been shown to interact with Integrin alpha3 beta1 and APP (1, 6, 14, 15). During cortical plate development, Reelin controls cell-cell interactions critical for proper neuronal migration and positioning (1, 2, 4, 5, 11, 12, 16). In the adult, it plays a role in dendrite growth and maturation, and synapse formation (2, 6, 15). Additionally, Reelin has been shown to modulate synaptic transmission and plasticity by regulating the subunit composition and conductivity of NMDA receptors (2, 6, 17). Mutation of the human RELN gene results in lissencephaly with cerebellar hypoplasia (11, 18). In addition, abnormal Reelin expression in human brain has been associated with a variety of cognitive pathological conditions including autism, schizophrenia, bipolar disorder, major depression, and Alzheimer’s disease (1, 6, 11, 13, 19, 20). Reelin deficiency found in Reeler mutant mice causes ataxia, tremors, and impaired motor coordination (4, 16). Peripherally, Reelin is important in the development of neuromuscular junctions. But instead of utilizing the locally expressed ApoE R2 and VLDLR, this function requires the serine protease activity of Reelin (3, 21).