3D endoscopy affords the surgeon improved depth of field and stereoscopic vision. Our data demonstrate that 3D endoscopy does not result in significantly different perioperative or postoperative outcomes vs 2D endoscopic surgery.

Fractures of the posterior elements functionally decompress the spinal canal and thereby allow for cervical traction to be safely implemented in patients with spondyloptosis. Safe restoration of anatomic alignment in the neurologically intact spondyloptotic patient is crucial to minimize the extent of surgical stabilization and create a long-term stable construct of the fracture dislocation.

We previously identified a partial expressed sequence tag clone corresponding to NARG2 in a screen for genes that are expressed in developing neurons and misexpressed in transgenic mice that lack functional N-methyl-D-aspartate receptors. Here we report the first characterization of the mouse and human NARG2 genes, cDNAs and the proteins that they encode. Mouse and human NARG2 consist of 988 and 982 amino acids, respectively, and share 74% identity. NARG2 does not display significant homology to other known genes, and lower organisms such as Saccharomyces cerevisiae, Drosophila melanogaster and Fugu rubripes appear to lack NARG2 orthologs. In vitro translation of the mouse cDNA yields a 150 kDa protein. NARG2 localizes to the nucleus in transfected cells, and deletion of a canonical basic nuclear localization signal suggests that this and other sequences in the protein cooperate for nuclear targeting.NARG2 consists of 16 exons in both mice and humans, 11 of which are identical in length, and alternative splicing is evident in both species. Exon 10 is the largest, and exhibits a much higher rate of nonsynonymous nucleotide substitution than the others. In addition, NARG2 contains (S/T)PXX motifs (11 in mouse NARG2, six in human NARG2). Northern blot analysis and RNase protection demonstrated that NARG2 is expressed at relatively high levels in dividing and immature cells, and that it is down-regulated upon terminal differentiation. The results indicate that NARG2 encodes a novel (S/T)PXX motif-containing nuclear protein, and suggest that NARG2 may play an important role in the early development of a number of different cell types.Keywords: human; mouse P19 embryonic carcinoma cells; cDNA; nuclear protein; SPXX.The N-methyl-D-aspartate (NMDA) receptor, a glutamategated ion channel that is permeable to Ca [5][6][7]. Programs of gene expression are also critical for brain development [8][9][10]. In an earlier study we used cDNA microarray analysis of mice that lack NMDAR1, the obligatory subunit for NMDA receptor function, to screen for genes that are abnormally expressed in the developing brain in the absence of NMDA receptors. A group of three genes was identified (termed NMDA receptor-regulated genes): NARG1, NARG2 and NARG3 [11]. These genes lack homology with one another, but all three are expressed at the highest levels in the neonatal brain and fail to be appropriately down-regulated in NMDAR1 knockout animals. NARG1 (now termed mNAT1) combines with its evolutionarily conserved cosubunit, mARD1, to form a functional acetyltransferase that may facilitate entry into the G 0 phase of the cell cycle [12,13] in higher animals, as it does in yeast. The significance of NARG3 is unknown, as NARG3 cDNAs corresponding to the longest NARG3 transcript on Northern blots lack an open reading frame (N. Sugiura and R. Corriveau, unpublished observations). Here we report the cDNA sequence and exon-intron structure of the mouse and human NARG2 genes, and provide evidence that NARG2 encodes a nuclear protein that is expressed ...