Tryptophan-derived indole compounds have been widely investigated as antioxidants and as free-radical scavengers. Indole-3-propionic acid (IPA), one of these compounds, is a deamination product of tryptophan. In the present study, we used Mongolian gerbils to investigate IPA's neuroprotective effects against ischemic damage and its antioxidative effects in the hippocampal CA1 region (CA1) after 5 min of transient forebrain ischemia. The repeated oral administration of IPA (10 mg/kg) for 15 days before ischemic surgery protected neurons from ischemic damage. In this group, the percentage of cresyl violet-positive neurons in the CA1 was 56.8% compared with that in the sham group. In the vehicle-treated group, glial fibrillary acidic protein (GFAP)-, S-100-, and vimentin-immunoreactive astrocytes and ionized calcium-binding adapter molecule 1 (Iba-1)- and isolectin B4 (IB4)-immunoreactive microglia were activated 4 days after ischemia/reperfusion, whereas in the IPA-treated ischemic group, GFAP, S-100, Iba-1, and IB4, but not vimentin, immunoreactivity was distinctly lower than that in the vehicle-treated ischemic groups. The administration of IPA significantly decreased the level of 4-hydroxy-2-nonenal, a marker of lipid peroxidation, in ischemic hippocampal homogenates compared with that in the vehicle-treated ischemic groups at various times after ischemia/reperfusion. In addition, immunostaining for 8-hydroxy-2'-deoxyguanosine showed DNA damage in pyramidal neurons in the ischemic CA1 was significantly lower in the IPA-treated ischemic groups than in the vehicle-treated ischemic groups. These results suggest that IPA protects neurons from ischemia-induced neuronal damage by reducing DNA damage and lipid peroxidation.

Somatostatin 28 immunoreactivity (Sst28-ir) identifies a specific subset of mossy fiber terminals in the adult mouse cerebellum. By using double-labeling immunohistochemistry, we determined that Sst28-ir is associated with presynaptic mossy fiber terminal rosettes, and not Purkinje cells, Golgi cells, or unipolar brush cells. Sst28-ir mossy fibers are restricted to the central zone (lobules VI/VII) and nodular zone (lobules IX, X) of the vermis, and the paraflocculus and flocculus. Within each transverse zone the mossy fiber terminal fields form a reproducible array of parasagittal stripes. The boundaries of Sst28-ir stripes align with a specific array of Purkinje cell stripes revealed by using immunocytochemistry for the small heat shock protein HSP25. In the cerebellum of the homozygous weaver mouse, in which a subpopulation of HSP25-ir Purkinje cells are located ectopically, the corresponding Sst28-ir mossy fiber projection is also ectopic, suggesting a role for a specific Purkinje cell subset in afferent pattern formation. Likewise, in the scrambler mutant mouse, Sst28-ir mossy fibers show a very close association with HSP25-ir Purkinje cell clusters. HSP25 itself does not appear to be critical for normal patterning, however: in the KJR mouse, which does not express cerebellar HSP25, Sst28 expression appears to be normal. Likewise, the Purkinje cell patterning antigens zebrin II and HSP25 are expressed normally in both Sst- and Sst-receptor knockout mice, suggesting that somatostatinergic transmission is not necessary for Purkinje cell stripe formation.

Cdk5 is ubiquitously expressed in all tissues, but its activators, p35 and p39, are principally found in brain, and Cdk5 activity has mostly been associated with brain development, particularly neuronal differentiation and migration. Here we show that the p35 transcript and protein are also present in the testis, and an active Cdk5⅐p35 complex exists in this tissue as well. Cdk5 and p35 are prominently observed in elongating spermatid tails, particularly over the tail outer dense fibers (ODF). The appearance of Cdk5⅐p35 proceeds from the proximal to the distal end of elongating spermatids, coinciding with the proximal to distal assembly of ODF along the length of the tail axoneme. Incidentally, increased Cdk5⅐p35 activity is observed in isolated elongating spermatids and at a time when elongating spermatids appear in the developing testis, suggesting a role for Cdk5⅐p35 in spermiogenesis. The presence of Cdk5 and p35 in ODF isolated from rat sperm tails implies a strong association among these proteins. In vitro ODF phosphorylation by Cdk5⅐p35 and decreased in vivo sperm tail ODF phosphorylation in p35-deficient mice indicate that Cdk5⅐p35 is an integral component of ODF and that ODF is a functional Cdk5⅐p35 target in the testis. Our results demonstrate for the first time that Cdk5⅐p35 may participate in the regulation of sperm tail development via a mechanism involving ODF phosphorylation. Apparently, as in brain development, Cdk5⅐p35 plays a part in testis development.

No abstract

This study investigated the boundary of anserine bursa with the recommended injection site and shape on the insertion area of pes anserinus (PA), with the aim of improving clinical practice. Eighty six legs from 45 Korean cadavers were investigated. The mixed gelatin solution was injected to identify the shape of anserine bursa, and then the insertion site of the PA tendons was exposed completely and carefully dissected to identify the shape of the PA. The sartorius was inserted into the superficial layer and gracilis, and the semitendinosus was inserted into the deep layer on the medial surface of the tibia. The number of the semitendinosus tendons at the insertion site varied: 1 in 66% of specimens, 2 in 31%, and 3 in 3%. The gracilis and semitendinosus tendons were connected to the deep fascia of leg. Overall, the shape of the anserine bursa was irregularly circular. Most of the anserine bursa specimens reached the proximal line of the tibia, and some of the specimens reached above the proximal line of the tibia. In the medial view of the tibia, the anserine bursa was located posteriorly and superiorly from the tibia's midline, and it followed the lines of the sartorius muscle. The injection site for anserine bursa should be carried out at 20° from the vertical line medially and inferiorly, 15 or 20 mm deeply, and at the point of about 20 mm medial and 12 mm superior from inferomedial point of tibial tuberosity.