Resection of liver metastasis from alpha-fetoprotein-producing early gastric cancer: report of a case.

We herein present a case of resected synchronous solitary liver metastasis from alpha-fetoprotein (AFP)-producing early gastric cancer. A 61-year-old woman, who was diagnosed at a routine medical checkup as having early gastric cancer with a liver tumor, came to our hospital for surgery. Her serum AFP level was high at 910 ng/ml. An examination was performed to determine whether the liver tumor was primary hepatocellular carcinoma or metastasis from early gastric cancer. She had no evidence of either a hepatitis B or C virus infection, and her liver function was normal. A biopsy specimen from the gastric cancer predominantly revealed moderately differentiated adenocarcinoma, but a focally trabecular pattern compatible with AFP-producing gastric cancer was also observed. Preoperatively, it was concluded that the liver tumor was metastasis from an AFP-producing early gastric cancer. We thus performed distal gastrectomy and a posterior segmentectomy of the liver. Her serum AFP level decreased to the normal range within 2 weeks after the operation. An immunohistological examination revealed that AFP-positive cells were present in both the gastric cancer and liver tumor. One year after the operation, there was no sign of recurrence.

[A case of hepatocellular carcinoma with reduction of primary tumor and disappearance of multiple lung metastasis].

A 62-year-old male patient was admitted for spontaneous rupture of hepatocellular carcinoma. He also had multiple lung metastases and liver dysfunction. So neither operation nor trans-arterial embolization could be performed. He had been administered UFT (400 mg/day) orally every day. After 5 months of daily administration, there was complete disappearance of multiple lung metastasis and reduction of the primary tumor. This case suggests that UFT is effective for some advanced hepatocellular carcinoma with extrahepatic metastasis.

Developmental changes of gamma-aminobutyric acid (GABA) and putative amino acid neurotransmitters in the organotypic culture of newborn mouse cerebellum.

The quantitative changes and metabolism of GABA and putative amino acid neurotransmitters during early developmental stages in the organotypic culture of newborn mouse cerebellum were examined by using the high-performance liquid chromatograph (HPLC) technique. D-[U-14C]Glucose was used as a precursor of amino acids. To analyze amino acid neurotransmitters, explants were incubated for 4 weeks under standard conditions. The amount of GABA linearly increased from 8.7 +/- 1.3 nmol/mg protein (2 days in vitro, 2 DIV) to 26.5 +/- 6.1 nmol/mg protein (15 DIV) and was saturated after that (24.0 +/- 3.6 nmol/mg protein at 30 DIV). During the period of GABA increase, the capability for GABA synthesis from [14C]glucose increased rapidly from 3.03 +/- 0.67 nCi/mg protein (2 DIV, 3 h incubation) to 9.32 +/- 1.34 nCi/mg protein (15 DIV, 3 h incubation). In the case of glutamic acid, a putative neurotransmitter of granule cell parallel fibers in the cerebellum, the amount in explants was nearly constant during incubation, in contrast with the fact that the amount in vivo gradually increased. However, the capability for glutamic acid synthesis from [14C]glucose increased from 10.80 +/- 3.01 nCi/mg protein (2 DIV, 1 h incubation) to 27.62 +/- 4.71 nCi/mg protein (22 DIV, 1 h incubation). In the case of taurine, found in abundance in fetal brain and supposed to play a specific role in the development and maturation of the central nervous system, the amount in explants decreased from 139.8 +/- 4.0 nmol/mg protein (2 DIV) to 54.0 +/- 0.8 nmol/mg protein (30 DIV).(ABSTRACT TRUNCATED AT 250 WORDS)

Uptake and metabolism of choline in the organotypic culture of newborn mouse cerebellum.

The uptake and metabolism of [methyl-14C]choline in the organotypic culture of newborn mouse cerebellum was examined. Explants of 8 day in vitro (8 DIV) were incubated for 48 h under standard conditions with 21.0 microM [14C]choline at 35 degrees C. During the first hour of incubation, most of the [14C]choline incorporated was transferred to phosphocholine. The amount of [14C]phosphocholine increased gradually at the initial rate of 0.95 +/- 0.17 nmol/mg protein/h and saturated after 7 h (4.31 +/- 1.30 nmol/mg protein). The synthesis of [14C]phospholipids was observed after a distinct time lag. About 96% of the radioactivity in the lipids was incorporated into phosphatidylcholine. The amount of phosphatidylcholine increased linearly up to 48 h of incubation: 11.9 +/- 2.10 nmol/mg protein at 24 h and 21.9 +/- 2.43 nmol/mg protein at 48 h. From double-label studies it was found that phosphocholine was a precursor of phosphatidylcholine. The content of [14C]choline within explants remained nearly constant through the incubation period. Acetylcholine synthesis in mouse cerebellum culture was relatively low, and the content remained constant through the incubation period (0.006 +/- 0.003 nmol/mg protein). Activities of acetylcholine synthesis of cerebral and cerebellar homogenates were compared. Phosphatidylcholine synthesized in mouse cerebellum culture separated into two spots on thin layer chromatograph using silica gel G plates. Gas chromatographs suggested that the separation depends on the difference in fatty acid composition.

Change of galactolipids and metabolism of fatty acids in the organotypic culture of myelinating mouse brain.

The concentrations of cerebrosides and sulfatides, myelin-characteristic galactolipids, can be determined in organotypic culture of newborn mouse cerebellum by high-performance liquid chromatography. These galactolipids can be detected at 9-days in vitro explants and increased steadily until the explants were more tan 3 weeks old. The levels of nonhydroxycerebroside, hydroxycerebroside, nonhydroxysulfatide, hydroxysulfatide, and monogalactosyl diacylglycerol were 0.3, 0.6, 0.3, 0.2, and 0.3 nmol/mg protein at 9 days in vitro, respectively, and 1.0, 2.7, 0.9, 0.4, and 0.6 at 21 days in vitro, respectively. When serum was removed from the feeding medium after 9 days, the levels of these lipids did not increase and myelination failed to occur. When a 17 day explant was kept in medium containing [1-14C]lignoceric acid for 4 days, considerable radioactivity was taken up by the explant and incorporated into nonhydroxy- and hydroxycerebrosides, sulfatides and sphingomyelin. Most of the radioactivity in the alpha-hydroxy fatty acids was found in cerebronic acid, the product of lignoceric acid alpha-hydroxylation. Similar explants also took up [1-14C]palmitic acid when it was added to the medium. The radioactivity was, however, mostly incorporated into neutral lipids and glycerophospholipids. These observations indicate that the cultured mouse cerebellum explants synthesize and accumulate myelin-characteristic lipids as does brain in vivo.

UDP-galactose hydrolysis in brain and its effect on cerebroside synthesis.

The enzymatic hydrolysis of UDP-galactose in rat and calf brain was studied. The hydrolysis occurs in two steps: The first is the conversion of UDP-galactose to galactose-1-phosphate catalyzed by nucleotide pyrophosphatase (EC 3.6.1.9), and the second is the conversion of the latter to free galactose by alkaline phosphatase (EC 3.1.3.1). The overall conversion has a pH optimum of 9.0, but there is considerable activity at pH 7.4, which is the optimum for UDP-galactose:ceramide galactosyltransferase in the synthesis of cerebrosides. Preparations from cytosol from calf brain cerebellum or stem that were enriched in UDP-galactose hydrolytic activity inhibit cerebroside synthesis under conditions optimal for the synthesis. Microsome-rich and nuclear debris fractions contain the highest apparent specific activity among the subcellular fractions studied. Hydrolysis of UDP-galactose occurs in all areas of brain, brainstem having the highest activity. The apparent specific activity in jimpy mouse brain homogenate is nearly twice as high as in the control brain homogenate.

Effect of calcium on the endogenous phosphorylation of mouse brain microsomes in vitro.

1. The endogenous phosphorylation of mouse brain microsomes was studied using the technique of acrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS). 2. It was found that specific proteins and lipids in brain microsomes were phosphorylated by the terminal phosphate of ATP under appropriate conditions. Six peaks of radioactivity were observed on SDS-polyacrylamide gel electrophoresis of 32Pi-labelled brain microsomes. The peaks were designated as P-I, P-II, P-III, P-IV, P-V, and P-VI. The peaks from P-I to P-V, which consist of phosphoproteins, underwent rapid dephosphorylation. On the other hand, P-VI, which consists of phospholipids, remained unaffected even after the complete hydrolysis of added ATP. 3. With the addition of 100 muM CaCl2 to the assay medium, the phosphorylation of brain microsomal proteins was stimulated; in the regions of P-I, P-II, and P-III, the amounts of 32Pi incorporation were approximately twice the 32Pi incorporation in the absence of Ca2+. On the other hand, 32Pi incorporation into P-VI was unaffected irrespective of the presence or absence of 100 muM CaCl2. In the presence of higher concentrations of Ca2+ (1-10 mM), the phosphorylation of all components was inhibited.