Strategies for Fostering Synergy between Neuroscience Programs and Chemistry Departments.

The successful model of the Neuroscience Program at Concordia College is used as a source of illustrative examples in a presentation of strategies to foster synergy between neuroscience programs and chemistry departments. Chemistry is an increasing voice in the dialog of modern neuroscience. To be well-prepared to engage in this dialog, students must have strong chemistry training and be comfortable applying it to situations in neuroscience. The strategies presented here are designed to stimulate thought and discussion in the undergraduate neuroscience education community. Hopefully this will lead to greater interaction between chemistry and neuroscience at the undergraduate level in other institutions.

Establishment of a neurochemistry track under the new ACS guidelines.

The new guidelines put forth by the ACS for approved chemistry degrees provide departments with greater flexibility in designing their ACS majors. Under these guidelines, students receive foundational and in-depth chemistry training while allowing individual departments to use their creativity in developing a curriculum that best meets the needs of their students and plays to the strength of the department. The chemistry department at Concordia College has developed an ACS Neurochemistry track and shares how the program arose, some of the practical matters in developing it, and how it can be made to work well within a liberal arts college.

A rat brain bicistronic gene with an internal ribosome entry site codes for a phencyclidine-binding protein with cytotoxic activity.

The cloning and characterization of the gene for the fourth subunit of a glutamate-binding protein complex in rat brain synaptic membranes are described. The cloned rat brain cDNA contained two open reading frames (ORFs) encoding 8.9- (PRO1) and 9.5-kDa (PRO2) proteins. The cDNA sequence matched contiguous genomic DNA sequences in rat chromosome 17. Both ORFs were expressed within the structure of a single brain mRNA and antibodies against unique sequences in PRO1- and PRO2-labeled brain neurons in situ, indicative of bicistronic gene expression. Dicistronic vectors in which ORF1 and ORF2 were substituted by either two different fluorescent proteins or two luciferases indicated concurrent, yet independent translation of the two ORFs. Transfection with noncapped mRNA led to cap-independent translation of only ORF2 through an internal ribosome entry sequence preceding ORF2. In vitro or cell expression of the cloned cDNA led to the formation of multimeric protein complexes containing both PRO1 and PRO2. These complexes had low affinity (+)-5-methyl-10,11-dihydro-5H-dibenzo[a,d]cyclohepten-5,10-imine (MK-801)-sensitive phencyclidine-binding sites. Overexpression of PRO1 and PRO2 in CHO cells, but not neuroblastoma cells, caused cell death within 24-48 h. The cytotoxicity was blocked by concurrent treatment with MK-801 or by two tetrahydroisoquinolines that bind to phencyclidine sites in neuronal membranes. Co-expression of two of the other subunits of the protein complex together with PRO1/PRO2 abrogated the cytotoxic effect without altering PRO1/PRO2 protein levels. Thus, this rare mammalian bicistronic gene coded for two tightly interacting brain proteins forming a low affinity phencyclidine-binding entity in a synaptic membrane complex.