For 3 days, rats received daily bilateral microinjections of d-amphetamine or saline into either the nucleus accumbens or the caudate putamen. On Days 1 and 3, each animal was tested for stereotypy and locomotion (number of grid crossings). Microinjections of d-amphetamine into the nucleus accumbens but not the caudate putamen produced an increase in locomotion but had no effect on stereotypy, whereas d-amphetamine microinjections into the caudate-putamen but not the nucleus accumbens produced an increase in stereotypy but had no effect on locomotion, The results are discussed in terms of the role of limbic and striatal dopamine systems in mediating these behaviors.

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Antibodies were prepared to mammalian CNS neurofilament proteins (NFPs) and the antibody specificities were compared using a sensitive immunoblotting method. This procedure was used to detect and characterize cross-reactive proteins and their degradation products in neurofilament preparations. NFPs were prepared by axon flotation. Rabbits were immunized with 200,000, 140,000, and 70,000 NFPs (200K, 140K, and 70K) that had been electrophoretically purified by polyacrylamide gel electrophoresis (PAGE). By immunohistofluorescence it was shown that all antisera stained similar filamentous structures in rat cerebellar neurons. By use of a horseradish peroxidase-conjugated indirect antibody procedure, however, differences were detected in the cross-reactivities of the antisera to rat NFPs, separated by PAGE and electrophoretically transferred to nitrocellulose membranes. Each antiserum exhibited strong binding to the homologous NFP and, thus, was suitable for the detection of cross-reactive polypeptides and proteolytic degradation products derived exclusively from the individual NFPs. Anti-200K, anti-140K, or anti-70K was applied to overloaded two-dimensional nitrocellulose blots of NFPs prepared by axon flotation. Each of the three sera detected a group of unique nonoverlapping polypeptides, some of which were identified as NFP degradation products. A different group of polypeptides was cross-reactive with antiserum to purified glial fibrillary acidic protein. The immunostaining of polypeptides on nitrocellulose was far more sensitive for detecting NFP degradation products than was staining polyacrylamide gels with Coomassie blue. Titers for the antisera were two to three orders of magnitude higher with the immunoblotting procedure than with immunohistologic methods. The sensitivity and the specificity of the described methods suggest their usefulness for examining proteolytic cleavage products of NFPs under a variety of conditions.

This article describes a model employed by the Academic Collaborative to Support Medical Education in Liberia to augment medical education in a postconflict setting where the health and educational structures and funding are very limited. We effectively utilized a cohort of visiting US pediatric faculty and trainees for short-term but recurrent clinical work and teaching. This model allows US academic medical centers, especially those with smaller residency programs, to provide global health experiences for faculty and trainees while contributing to the strengthening of medical education in the host country. Those involved can work toward a goal of sustainable training with a strengthened host country specialty education system. Partnerships such as ours evolve over time and succeed by meeting the needs of the host country, even during unanticipated challenges, such as the Ebola virus outbreak in West Africa.

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