A Case of Liposarcoma With Peritonitis Due to Jejunal Perforation

A 21-year-old man, who had been treated for congenital dilatation of the bile duct 13 years previously, presented with an acute abdomen. The physical examination suggested peritonitis, and an emergent laparotomy was performed. A perforation was foundin the jejunum approximately 100 cm distal to the ligament of Treitz, followed by resection of a 60-cm jejunal segment. No tumorous lesions were found during the operation, and the resected jejunal segment showed only focal myxomatous thickening of the serosa. Despite intensive therapy, he died of uncontrollable septic shock 2 days after the operation. Unexpectedly, however, histological examination revealed a liposarcoma, showing an unclassifiable histology. From the distribution of the lesion and the histological findings, it is thought that a primary lesion was somewhere else, covered by severe adhesions due to the previous operation, and that the tumor cells spreading from it could have caused the jejunal perforation through vascular involvement. Although extremely rare, liposarcomas in the abdomen can cause intestinal perforation. It is important for both clinicians andpathologists to carefully investigate the cause of an unusual clinical presentation such as intestinal perforation

Regulated interaction between polypeptide chain elongation factor-1 complex with the 26S proteasome during Xenopus oocyte maturation

BACKGROUND: During Xenopus oocyte maturation, the amount of a 48 kDa protein detected in the 26S proteasome fraction (p48) decreased markedly during oocyte maturation to the low levels seen in unfertilized eggs. The results indicate that the interaction of at least one protein with the 26S proteasome changes during oocyte maturation and early development. An alteration in proteasome function may be important for the regulation of developmental events, such as the rapid cell cycle, in the early embryo. In this study, we identified p48. RESULTS: p48 was purified by conventional column chromatography. The resulting purified fraction contained two other proteins with molecular masses of 30 (p30) and 37 (p37) kDa. cDNAs encode elongation factor-1γ and δ were obtained by an immuno-screening method using polyclonal antibodies against purified p48 complex, which recognized p48 and p37. N-terminal amino acid sequence analysis of p30 revealed that it was identical to EF-1β. To identify the p48 complex bound to the 26S proteasome as EF-1βγδ, antibodies were raised against the components of purified p48 complex. Recombinant EF-1 β,γ and δ were expressed in Escherichia coli, and an antibody was raised against purified recombinant EF-1γ. Cross-reactivity of the antibodies toward the p48 complex and recombinant proteins showed it to be specific for each component. These results indicate that the p48 complex bound to the 26S proteasome is the EF-1 complex. MPF phosphorylated EF-1γ was shown to bind to the 26S proteasome. When EF-1γ is phosphorylated by MPF, the association is stabilized. CONCLUSION: p48 bound to the 26S proteasome is identified as the EF-1γ. EF-1 complex is associated with the 26S proteasome in Xenopus oocytes and the interaction is stabilized by MPF-mediated phosphorylation

ユリ根中トリプシンインヒビター(LTI-II-4)の精製とその性質

Several proteins from lily bulb for foodstuffs showed strong inhibitory activity toward bovine trypsin. A trypsin inhibitor (LTI-II-4) was purified from lily bulb by a method including column chromatographies on CM-Sepharose CL-6B and DEAE-Sepharose GL-6B and high-pressure liquid chromatography. Purified LTI-II-4 had a molecular weight of 21,000. The amino acid composition was characterized by high contents of glycine, aspartic acid and serine. The inhibitor contained 4 halfcystines in its constituent amino acids. The N-terminal 25 and the C-terminal 3 residues of LTI-II-4 were sequenced. The Inhibitor was stable in a wide pH range under 50℃ and was unstable at the higher temperatures than 80℃. The reactivesite amino acid of LTI-II-4 was assumed to be lysine. The inhibitor didn\u27t inhibit elastase and subtilisin. From these results, the inhibitor LTI-II-4 is assumed to belong to the Kunitz soybean trypsin inhibitor family

Fostering the ability to apply nursing theory to practice : Focus on student perception

本研究の目的は，看護学部 1 年次の授業科目「看護理論と看護実践への活用」の履修後における学生の内面に形成された看護理論に関する認識を明らかにし，教育活動上の成果及び課題を明らかにすることである。 本調査により，学生の看護理論に関する関心は88.4％と高く，実践に活用したい意思も高いことが明らかとなった。受講後の学生の内面に形成された看護理論に関する認識として【看護理論の必要性】【看護実践への活用】【援助の取り組み姿勢】【よりよい看護の追及】【自己を高める】【今後の展望】【理論家の人物像からの刺激】の 7カテゴリーが抽出された。 看護理論は難しいと言われているが， 1 年次においても看護理論の意義や活用意思等の認識がもて，将来の自己の在りかたを模索する姿勢を築くことが可能であることが示された。journal articl

A Simple and Rapid Method for Standard Preparation of Gas Phase Extract of Cigarette Smoke

Cigarette smoke consists of tar and gas phase: the latter is toxicologically important because it can pass through lung alveolar epithelium to enter the circulation. Here we attempt to establish a standard method for preparation of gas phase extract of cigarette smoke (CSE). CSE was prepared by continuously sucking cigarette smoke through a Cambridge filter to remove tar, followed by bubbling it into phosphate-buffered saline (PBS). An increase in dry weight of the filter was defined as tar weight. Characteristically, concentrations of CSEs were represented as virtual tar concentrations, assuming that tar on the filter was dissolved in PBS. CSEs prepared from smaller numbers of cigarettes (original tar concentrations = 20 mg/ml), the curves were shifted rightward. Accordingly, the cytotoxic activity was detected in PBS of the second reservoir downstream of the first one with larger numbers of cigarettes. CSEs prepared from various cigarette brands showed comparable concentration-response curves for cytotoxicity. Two types of CSEs prepared by continuous and puff smoking protocols were similar regarding concentration-response curves for cytotoxicity, pharmacology of their cytotoxicity, and concentrations of cytotoxic compounds. These data show that concentrations of CSEs expressed by virtual tar concentrations can be a reference value to normalize their cytotoxicity, irrespective of numbers of combusted cigarettes, cigarette brands and smoking protocols, if original tar concentrations are <= 15 mg/ml

Agonist-promoted Ubiquitination Differentially Regulates Receptor Trafficking of Endothelin Type A and Type B Receptors

Two types of G protein-coupled receptors for endothelin-1 (ET-1), ET type A receptor (ETAR) and ETBR, closely resemble each other, but upon ET-1 stimulation, they follow totally different intracellular trafficking pathways; ETAR is recycled back to plasma membrane, whereas ETBR is targeted to lysosome for degradation. However, the mechanisms for such different fates are unknown. Here we demonstrated that ETBR but not ETAR was ubiquitinated on the cell surface following ET-1 stimulation and that ETBR was internalized and degraded in lysosome more rapidly than ETAR. The mutant ETBR (designated 5KR mutant) in which 5 lysine residues in the C-tail were substituted to arginine was not ubiquitinated, and its rates of internalization and degradation after ET-1 stimulation became slower, being comparable with those of ETAR. Confocal microscopic study showed that following ET-1 stimulation, ETAR and 5KR mutant of ETBR were co-localized mainly with Rab11, a marker of recycling endosome, whereas ETBR was co-localized with Rab7, a marker of late endosome/lysosome. In the 5KR mutant, ET-1-induced ERK phosphorylation and an increase in the intracellular Ca2+ concentration upon repetitive ET-1 stimulation were larger. A series of ETBR mutants (designated 4KR mutant), in which either one of 5 arginine residues of the 5KR mutant was reverted to lysine, were normally ubiquitinated, internalized, and degraded, with ERK phosphorylation being normalized. These results demonstrate that agonist-induced ubiquitination at either lysine residue in the C-tail of ETBR but not ETAR switches intracellular trafficking from recycling to plasma membrane to targeting to lysosome, causing decreases in the cell surface level of ETBR and intracellular signaling