Pseudo-Meigs Syndrome Caused by a Giant Uterine Leiomyoma with Cystic Degeneration: A Case Report.

Pseudo-Meigs syndrome is defined as secondary accumulation of ascites and hydrothorax associated with a pelvic tumor other than benign ovarian tumors such as fibroma, which usually resolve after surgical removal of the tumor. Here we report a case of pseudo-Meigs syndrome caused by a giant uterine leiomyoma, which was initially suspected to be ovarian cancer. A 37-year-old nulliparous woman presented with a 5-month history of abdominal distension and anorexia. Abdominal ultrasonography revealed a giant cystic lesion and solid mass in the peritoneal cavity, along with plentiful ascites. Chest X-ray images showed a small pleural effusion on the right side. The patient was referred to our hospital for treatment of suspected ovarian cancer and peritonitis carcinomatosis. Although serum CA125 level was elevated (up to 331.8 U/mL), magnetic resonance imaging showed a giant sub-serosal uterine leiomyoma with cystic degeneration (27 × 15 × 13 cm). A small dermoid cyst was also detected in the right ovary. Ascites was drained and the patient underwent myomectomy and ovarian cystectomy. The patient had a degenerated leiomyoma with no pathological evidence of malignancy. Because symptoms disappeared postoperatively and serum CA125 returned to normal, without recurrence of ascites, pseudo-Meigs syndrome was diagnosed.

Familial interstitial pneumonia complicated by lung cancer in 2 sisters.

A 29-year-old woman was referred to our hospital because of progressive dyspnea on exertion, and her 36-year-old sister was also referred for the evaluation of an abnormal chest radiograph. Radiologic and pathologic findings of the 2 sisters resembled each other closely. In both cases, computed tomography revealed diffuse reticulation, micronodules, diffusely distributed interlobular septal thickening, and an ill-defined nodule in the left lower lobe. Radiologic-pathologic correlation revealed that the reticulation and micronodules corresponded to centrilobular and perilobular fibrosis without architectural lung distortion and that the nodules represented pulmonary adenocarcinoma. To our knowledge, this is the first report of familial interstitial pneumonia complicated by lung cancer in 2 family members, suggesting a possible etiologic association between familial interstitial pneumonia and lung cancer.

Maize phosphoenolpyruvate carboxylase. Mutations at the putative binding site for glucose 6-phosphate caused desensitization and abolished responsiveness to regulatory phosphorylation.

Phosphoenolpyruvate carboxylases (PEPC, EC 4.1.1.31) from higher plants are regulated by both allosteric effects and reversible phosphorylation. Previous x-ray crystallographic analysis of Zea mays PEPC has revealed a binding site for sulfate ion, speculated to be the site for an allosteric activator, glucose 6-phosphate (Glc-6-P) (Matsumura, H., Xie, Y., Shirakata, S., Inoue, T., Yoshinaga, T., Ueno, Y., Izui, K., and Kai, Y. (2002) Structure (Lond.) 10, 1721-1730). Because kinetic experiments have also supported this notion, each of the four basic residues (Arg-183, -184, -231, and -372' on the adjacent subunit) located at or near the binding site was replaced by Gln, and the kinetic properties of recombinant mutant enzymes were investigated. Complete desensitization to Glc-6-P was observed for R183Q, R184Q, R183Q/R184Q (double mutant), and R372Q, as was a marked decrease in the sensitivity for R231Q. The heterotropic effect of Glc-6-P on an allosteric inhibitor, l-malate, was also abolished, but sensitivity to Gly, another allosteric activator of monocot PEPC, was essentially not affected, suggesting the distinctness of their binding sites. Considering the kinetic and structural data, Arg-183 and Arg-231 were suggested to be involved directly in the binding with phosphate group of Glc-6-P, and the residues Arg-184 and Arg-372 were thought to be involved in making up the site for Glc-6-P and/or in the transmission of an allosteric regulatory signal. Most unexpectedly, the mutant enzymes had almost lost responsiveness to regulatory phosphorylation at Ser-15. An apparent lack of kinetic competition between the phosphate groups of Glc-6-P and of phospho-Ser at 15 suggested the distinctness of their binding sites. The possible roles of these Arg residues are discussed.