[Is video-assisted thoracic surgery lobectomy better than minimally invasive open thoracotomy?].

This article reviews our experiences of the current video-assisted thoracic surgery (VATS) lobectomy and minimally invasive open thoracotomy for resection of lung cancer. Between August 1999 and April 2007 at Saiseikai Central Hospital, Tokyo, Japan, we performed VATS lobectomy in 243 patients with clinical stage I lung cancer. It is certain that VATS lobectomy is acceptable in view of its low invasiveness, mortality, morbidity. And from an oncological viewpoint, VATS lobectomy is not inferior to conventional lobectomy. Therefore, we consider VATS lobectomy to be one of the therapeutic options in patients with clinical stage I lung cancer. However, what is most important is to achieve an anatomic lobectomy and complete mediastinal lymph node dissection. It may be that it is not important for differences of approach methods.

Development of a high-efficiency high-resolution particle-induced x-ray emission system for chemical state analysis of environmental samples.

We have developed a high-efficiency high-resolution particle-induced x-ray emission (PIXE) system employing a von Hamos-type crystal spectrometer for a chemical state identification of trace elements in environmental samples. The energy resolution of the system was determined to be about 0.05% through the observation of Si Kalpha(1,2) x rays (1.74 keV) from elemental silicon. The throughput efficiency of the system was also evaluated quasitheoretically to be 1.6x10(-7) counts/incident proton for Si Kalpha(1,2) emission. To demonstrate a chemical state analysis using the high-resolution PIXE system, Si Kalpha(1,2) and Kbeta x-ray spectra for SiC, Si(3)N(4), and SiO(2) were measured and compared. The observed chemical shifts of the Si Kalpha(1,2) peaks for SiC, Si(3)N(4), and SiO(2) relative to elemental silicon were 0.20, 0.40, and 0.55 eV, respectively. The tendency of these shifts were well explained by the effective charges of the silicon atoms calculated by a molecular orbital method.

Preparation and root growth-modulatory activity of N-substituted 2-acetylamino-2-ethoxycarbonyl-3-(2-furyl)propanamides.

N-Substituted 2-acetylamino-2-ethoxycarbonyl-3-(2-furyl)propanamides (8) were synthesized through the reaction of amines (13) with 2-acetylamino-2-ethoxycarbonyl-3-(2-furyl)propanoic acid (3b), which was prepared via condensation of 2-(bromomethyl)furan (10b) with diethyl acetamidomalonate, followed by partial hydrolysis of the resultant diethyl ester (3a) in the presence of barium hydroxide. However, bulky amines such as tert-butylamine or 2-trifluoromethylaniline did not afford the corresponding diamides (8). The biological activity of the prepared diamides (8) as root growth modulators was examined by germination assay using rape and leek seeds. N-(5-Bromo-2-thiazolyl)- and N-(4-chloro-2-benzothiazolyl)-2-acetylamino-2-ethoxycarbonyl-3-(2-furyl)propanamides (8h, i) both potently inhibited the root growth of rape seedlings, but were less effective in the case of leek seeds. The herbicide 2,4-dichlorophenoxyacetic acid completely inhibited root growth in both cases.

Identification and characterization of testis specific ornithine decarboxylase antizyme (OAZ-t) gene: expression in haploid germ cells and polyamine-induced frameshifting.

BACKGROUND: Polyamines are known to play important roles in the proliferation and differentiation of many types of cells. However, in the testis, where polyamines such as spermidine and spermine exist in high concentrations, their roles still remains to be elucidated. RESULTS: We have cloned a testis-specific gene encoding an ornithine decarboxylase antizyme known to control intracellular concentrations of polyamines in a feedback manner. The mRNA encoding the protein named ornithine decarboxylase antizyme in testis (OAZ-t) was specifically expressed in haploid germ cells. In contrast, the mRNA level of somatic ornithine decarboxylase antizyme 1 (OAZ1) decreased markedly at the late stages of haploid germ cell differentiation. OAZ-t mRNA was first observed in 23-day-old mice, whereas the OAZ-t protein was detected much later, at 35 days after birth. Further experiments on OAZ-t revealed that polyamines were capable of inducing a frameshifting at the frameshift sequence of OAZ-t mRNA, resulting in the translation of OAZ-t, as was the case with the somatic OAZ1. Transfection of OAZ-t cDNA inactivated the ornithine decarboxylase activity in the HEK293 cells. CONCLUSIONS: Results indicate that the expression of OAZ-t is controlled at both transcriptional and translational levels, and that OAZ-t likely plays a key role in spermatogenesis by regulating the intracellular concentration of polyamines in haploid germ cells.

Isolation and characterization of a haploid germ cell-specific novel complementary deoxyribonucleic acid; testis-specific homologue of succinyl CoA:3-Oxo acid CoA transferase.

We have isolated a cDNA clone encoding a mouse haploid germ cell-specific protein from a subtracted cDNA library. Sequence analysis of the cDNA revealed high homology with pig and human heart succinyl CoA:3-oxo acid CoA transferase (EC 2.8.3.5), which is a key enzyme for energy metabolism of ketone bodies. The deduced protein consists of 520 amino acid residues, including glutamate 344, known to be the catalytic residue in the active site of pig heart CoA transferase and the expected mitochondrial targeting sequence enriched with Arg, Leu, and Ser in the N-terminal region. Thus, we termed this gene scot-t (testis-specific succinyl CoA:3-oxo acid CoA transferase). Northern blot analysis, in situ hybridization, and Western blot analysis demonstrated a unique expression pattern of the mRNA with rapid translation exclusively in late spermatids. The scot-t protein was detected first in elongated spermatids at step 8 or 9 as faint signals and gradually accumulated during spermiogenesis. It was also detected in the midpiece of spermatozoa by immunohistochemistry. The results suggest that the scot-t protein plays important roles in the energy metabolism of spermatozoa.