[A clinico-experimental study on the wrapping material for cerebral aneurysm].
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Biomedical subjects
Publications and source records attributed to T Moriyama.
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A family of von Recklinghausen's disease complicated by multiple diverse primary brain tumors was reported. Case 1. The proband, born in 1923, was admitted to the Nagasaki University Hospital on March 11, 1974, for evaluation of headache and hearing loss. Neurological examination disclosed: decreased visual acuity on the right: bilateral choked discs; anisocoria, right pupil wider than left; right blepharoptosis; artificially fixed right eye; right facial palsy; markedly impaired hearing with negative vestibular responses to caloric test; paralysis of the right soft palate and vocal cord; atrophy of the right side of the tongue; right claw hand with positive Froment's sign; left drop foot; loss of deep reflexes on the left arm and legs; positive Babinski on the right. Nerve conduction studies revealed failure to evoke muscle action potential in response to electric nerve stimulation on the left ulnar and right superficial peroneal nerves. Needle electromyography showed no motor unit potentials in the left first dorsal interosseus and right anterior tibial muscles. Sensory nerve action potentials could not be evoked on any nerves tested. X-ray films showed enlargement of the internal auditory passages, falx tumor on brain scan and carotid angiography, and spinal tumor on myelography. At craniotomy, a 7 X 5.5 X 4 cm falx meningioma was removed. At suboccipital craniotomy performed five weeks later, right acoustic neurinoma measuring 1.5 cm in diameter was removed. Case 2. This relative, born in 1945, was the son of the proband. A spinal meningioma at C 7-T 1 was removed in 1957. However, he could not walk after operation and died of pneumonia two years later.(ABSTRACT TRUNCATED AT 250 WORDS)
In our previous paper (Yanase, M. et al. (1983) Biochim. Biophys. Acta 733, 95-101) we reported that the Na+-dependent D-glucose uptake into brush-border membrane vesicles is decreased in rabbits with experimental Fanconi syndrome (induced by anhydro-4-epitetracycline). In the present paper we investigate the mechanism underlying this decrease. D-Glucose is taken up into the osmotically active space in anhydro-4-epitetracycline-treated brush-border membrane vesicles and exhibits the same distribution volume and the same degree of nonspecific binding and trapping as in control brush-border membrane vesicles. The passive permeability properties of control and anhydro-4-epitetracycline-treated brush-border membrane vesicles are shown to be the same as measured by the time-dependence of L-glucose efflux from brush-border membrane vesicles. D-Glucose flux was measured by the equilibrium exchange procedure at constant external and internal Na+ concentrations and zero potential. Kinetic analyses of Na+-dependent D-glucose flux indicate that Vmax in anhydro-4-epitetracycline-treated brush-border membrane vesicles (79.3 +/- 7.6 nmol/min per mg protein) is significantly smaller than in control brush-border membrane vesicles (141.3 +/- 9.9 nmol/min per mg protein), while the Km values in the two cases are not different from each other (22.3 +/- 0.9 and 27.4 +/- 1.8 mM, respectively). These results suggest that Na+-dependent D-glucose carriers per se are affected by anhydro-4-epitetracycline, and that this disorder is an important underlying mechanism in the decreased Na+-dependent D-glucose uptake into anhydro-4-epitetracycline-treated brush-border membrane vesicles.
An inhibitor of mouse factor B was purified from lysate of L cells by a human factor B-affinity column. The purified inhibitor was found to be homogeneous with a molecular weight of about 25,000 and identical to the 25K protein isolated from L cell-lysate by the coprecipitation method with anti mouse factor B. Hemolytic titration of the activity and PAGE-analysis of the inhibitor-factor B complex showed that 1 mol of inhibitor reacted with 1 mol of mouse factor B and inactivated its hemolytic activity.
The relationship between invasiveness and calcium dependency was examined in various strains of Yersinia enterocolitica and Y. pseudotuberculosis by using established cell lines. Infection with calcium-dependent bacteria resulted in the formation of microvilli and the adherence of bacteria on the cell surface, and the adherent bacteria were ingested 1.5 hr after infection. Morphological changes in the cells became visible 2 to 3 hr after infection, and intracellular multiplication of the ingested bacteria was noted. When the cells were incubated with bacteria at 37 C for 1.5 hr and then at 25 C, however, the morphological changes in the infected cells were not observed. No isogenic strains that had lost calcium dependency for growth at 37 C were able to elicit the morphological changes in the cells, though they possessed the ability to adhere to and penetrate the cells. The antigen(s) supposedly related to cytotoxicity of the calcium-dependent Yersinia was sought by using antibodies prepared against calcium-dependent bacteria and then absorbed with calcium-independent bacteria and with calcium-independent bacterial cytosol. Double diffusion tests between the antisera and bacterial cytosol extracts revealed the presence of an antigen which was a cytoplasmic substance common to all calcium-dependent but not calcium-independent strains of Y. enterocolitica and Y. pseudotuberculosis.
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Serum amylase isozyme was determined in 2 cases with normal urinary amylase but persistantly high serum amylase. Both cases showed dominant S-type amylase associated with tailing findings that was characteristic of macroamylasemia. Moreover, using the immunofixation method, the serum amylase was found to be bound with IgG (K) in case 1 and with IgA (L) in case 2.
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Two neutrophil chemotactic factors were isolated from the culture filtrates of Streptococcus sanguis ATCC 10556 and were chemically characterized as N-terminal blocked peptides of low molecular weight. One of the factors consisted of proline, valine, methionine, isoleucine and leucine and the other of methionine, isoleucine, leucine and phenylalanine. In both factors, methionine was detected as the sole N-terminal amino acid, but the amino group was blocked. The removal of N-terminal methionine yielded several N-terminal amino acids, suggesting that S. sanguis produced several N-terminal blocked methionyl peptides, all of which could be chemotactically active.
The effects of added maltose on the activities of a preparation of crude glucosyltransferases (GTases) and purified dextransucrase (DS) were investigated to elucidate the inhibition mechanism of maltose on the synthesis of water-insoluble glucan (ISG) in Streptococcus mutans HS-6. Tri- and tetra-saccharides produced by crude GTases from sucrose in the presence of maltose were identified as panose (4-alpha-isomaltosylglucose) and 4-alpha-isomaltotriosylglucose which were responsible for the activity of DS involved in crude GTases. Kinetic studies on crude GTases in the presence of maltose showed similar results to those of DS except that the synthesis of ISG in the crude GTases was inhibited. Comparative studies of soluble products of crude GTases and DS in the presence of maltose were performed employing gel filtration on Sephadex G-15. The existence of oligosaccharides above hexasaccharide was revealed as the products of DS but not of crude GTases. These findings were interpreted in terms of the previously proposed mechanism of ISG synthesis by S. mutans, i.e., ISG should be synthesized from the preformed soluble glucan. It was indicated that oligosaccharides above hexasaccharide are utilized for ISG synthesis in the crude GTases system. From these results, the inhibitory mechanism of added maltose on ISG synthesis by crude GTases is considered as follows: DS synthesizes a series of 4-alpha-isomaltodextrinylglucose from sucrose and maltose, and the increase of added maltose results in the decrease of oligosaccharides responsible for synthesis of ISG.
proteins which were able to bind noncovalently with mouse factor B were found in cells that are nonsecretors of factor B such as mouse-established monocytic cells and L cells but not in peritoneal resident macrophages. These proteins were isolated from lysates of L cells and separated into four distinct proteins by preparative SDS-polyacrylamide gel electrophoresis, with molecular weights of 25K , 28K , 33K, and 35K . The individual proteins formed a complex with purified mouse factor B at a molecular ratio of 1: 1 and inhibited its hemolytic activity. Proteins 25K and 28K inhibited the hemolytic activity of an activated form of factor B combined with cobra venom factor as well as that of the native form. These inhibitors did not affect the hemolytic activity of the second component of complement in mouse serum. The inhibitory activity of the 25K protein was partially inhibited by antiserum raised against it in rabbits.