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Biomedical subjects

M Nishijima

Publications and source records attributed to M Nishijima.

At least 271 records · Page 15Linked to original sources
PubMed1980

Acyl phosphatidylglycerol of Escherichia coli.

Acyl phosphatidylglycerol, isolated from Escherichia coli, has been identified as 3-sn-phosphatidyl-1'-(3'-acyl)-sn-glycerol. The fatty acids of the diacylglycerol moiety of acyl phosphatidylglycerol resemble those of phosphatidylglycerol in composition. However, the monoacylglycerol moiety of this lipid contains more unsaturated fatty acids than the diacylglycerol part of this lipid or other phospholipids in E. coli. Furthermore, the fatty acids present in the monoacylglycerol moiety, were found to contain major amounts of an unsaturated acid identified as 7-tetradecenoic acid by combined gas-liquid chromatography-mass spectrometry. This acid was present only in low concentrations in most phospholipids of E. coli.

Diglycerides↗
PubMed1980

Purification and properties of a membrane-bound phospholipase A2 from rat ascites hepatoma 108A cells.

A phospholipase A2 bound tightly to the particulate fractions of rat ascites hepatoma cells was purified approximately 13,000-fold with a reasonably high yield (34%) by extraction with sodium cholate, ammonium sulfate fractionation, solubilization with sodium dodecyl sulfate, column chromatographies on Sephadex G-150 in the presence of sodium dodecyl sulfate, and on DEAE-cellulose and CM-cellulose in the presence of Triton X-100. The enzyme has a unique substrate specificity; namely, it preferentially hydrolyzes phosphatidylethanolamine and, to a lesser degree, phosphatidylglycerol. However, it does not attack phosphatidylcholine, phosphatidic acid or cardiolipin in the present experimental conditions. The final preparation shows both phospholipase A2 and lysophospholipase L2 activities, but neither lysophospholipase L1 nor lipase activity. The purified enzyme has a rather broad pH optimum ranging from 7 to 9, requires Ca2+, and is resistant to heat-treatment at 95 degree C for 5 min.

Animals↗
PubMed1980

[Gastric perforation in ventriculo-peritoneal shunt--a case report (author's transl)].

The case is a 69-year-old female who was admitted to our hospital under the diagnosis of normal pressure hydrocephalus secondary to cerebral infarction. V-P shunt was performed and postoperative course was uneventful until 7 months after operation, when she developed meningitis. Since then the level of consciousness became gradually worse down to akinetic mutism. Two years and 3 months after the operation she died of pneumonia. At autopsy peritoneal end of the shunt tube was found to have perforated the antero-inferior wall of the stomach. In this report, we discussed the mechanism of development of bowel perforation and preventive measures against this complication. As the causative factors it should be noted first that any foreign body in the peritoneal cavity is potentially able to cause bowel perforation. The second factor is the sharp tip of the peritoneal tube which perforates the bowel more easily. The third factor is the constant pressure at the same site of the bowel wall over a long period of time to cause necrosis of it. The fourth factor is the poor general condition of the patient with decreased resistance of the bowel wall against the foreign body. We therefore postulate for the prophylaxis and early diagnosis of this complication that a careful procedure with adequate tube is required at operation and a low grade fever and abdominal symptoms should not be overlooked afterward.

Aged↗
PubMed1980

Hydatidiform mole with a surviving coexisting fetus.

A case of hydatidiform mole with a coexistent live fetus--an extremely rare condition--is reported. This is the only known case with delivery of a surviving fetus in which the diagnosis was made antepartum, and the grounds for it are discussed. The rationale for allowing the pregnancy to continue after this diagnosis at the 20th week of pregnancy is also discussed. The values for numerous blood and urinary measurements of fetal and placental status are presented, and the mechanisms of some of these are discussed. Spontaneous labor occurred at the 32d week of pregnancy, and a 1435-g living female infant was delivered. The uterus was evacuated manually and the recovered contents are illustrated, described, and discussed. The infant showed no physical or mental abnormalities at the age of 12 months. Her weight and height were 7170 g and 67.7 cm, respectively, and she had good development.

Adult↗
PubMed1980

[Intracerebral hemorrhage from meningioma (author's transl)].

A case of asymptomatic convexity meningioma causing intracerebral hemorrhage and with an aneurysm of the branch of the middle cerebral artery is reported. Operation disclosed an encapsulated tumor of 4 cm in diameter and intracerebral hemorrhage was found medial to it. Histological diagnosis of the tumor was a malignant meningioma. The mechanism of hemorrhage and the relation between the tumor and occurrence of an aneurysm have been discussed with a review of the literature.

Adult↗
PubMed1979

Properties of purified detergent-resistant phospholipase A of Escherichia coli K-12. Inactivation, and protection with detergents and phospholipids.

A crude preparation of membrane-bound phospholipase A (detergent-resistant) in Escherichia coli K-12 cells was found to be quite stable or even apparently activated on incubation at 100 degrees C, but became strikingly thermolabile when it was highly purified and Triton X-100 was removed from the purified enzyme preparation. The rate of inactivation showed a biphasic temperature dependence: inactivation was rapid at 37 degrees C and also above 70 degrees C. Inactivation above 70 degrees C changed the mobility of the enzyme on sodium dodecyl sulfate/polyacrylamide gel electrophoresis, but inactivation at 37 degrees C did not affect the electrophoretic mobility. Triton X-100 effectively protected the enzyme against inactivation at 37 degrees C. The concentration required for the protection of the enzyme was more than its critical micelle concentration. Phospholipids, such as phosphatidylethanolamine, phosphatidylglycerol, cardiolipin, phosphatidylcholine, lysophosphatidylethanolamine, and lysophosphatidylcholine, also protected the enzyme against inactivation at 37 degrees C. These results suggest that the binding of hydrophobic compounds stabilizes the enzyme.

Cell Membrane↗
PubMed1979

Cardiolipin accumulation in the inner and outer membranes of Escherichia coli mutants defective in phosphatidylserine synthetase.

Mutants of Escherichia coli defective in phosphatidylserine synthetase (pss) make less phosphatidylethanolamine than normal cells, and they are temperature sensitive for growth. We have isolated a new mutant, designated RA2021, which is better than previously available strains in that the residual phosphatidylethanolamine level approaches 25% after 4 h at 42 degrees C. The total amount of phospholipid normalized to the density of the culture is about the same in RA2021 (pss-21) as in the isogenic wild-type RA2000 (pss(+)). Consequently, there is a net accumulation of polyglycerophosphatides in the mutant, particularly of cardiolipin. The addition of 10 to 20 mM MgCl(2) to a culture of RA2021 prolongs growth under nonpermissive conditions and prevents loss of cell viability, but it does not eliminate the temperature-sensitive phenotype. Divalent cations, like Mg(2+), do not correct the phospholipid composition of the mutant, but may act indirectly by balancing the negative charges of phosphatidylglycerol and cardiolipin. To determine the effects of the pss mutation on membrane composition, we have examined the subcellular distribution of the polyglycerophosphatides that accumulate in these strains. All of the excess anionic lipids of RA2021 are associated with the envelope fraction and are distributed equally between the inner and outer membranes. The protein compositions of the isolated membranes do not differ significantly in the mutant and wild type. The fatty acid composition of RA2021 is almost the same as wild type at 30 degrees C, but there is more palmitic and cyclopropane fatty acid at 42 degrees C. These results demonstrate that the modification of the polar lipid composition observed in pss mutants affects both membranes and that cardiolipin, which is not ordinarily present in large quantities, can accumulate in the outer membrane when it is overproduced by the cell. The altered polar headgroup composition of the outer membrane in pss mutants may account, in part, for their hypersensitivity to the aminoglycoside antibiotics.

CDPdiacylglycerol-Serine O-Phosphatidyltransferase↗
PubMed1978

Synthesis of acyl phosphatidylglycerol from phosphatidylglycerol in Escherichia coli K-12. Evidence for the participation of detergent-resistant phospholipase A and heat-labile membrane-bound factor(s).

The conversion of phosphatidylglycerol to acyl phosphatidylglycerol by extracts of Escherichia coli K-12 strains was examined under various conditions. The maximum rate of conversion was observed at pH 7.2 in the presence of 50% (v/v) diethyl ether and 10 mM CaCl2. This conversion was found to involve two sequential reactions: (1) The formation of 2-acyl glycerophosphoglycerol and 2-acyl glycerophosphoethanolamine from phosphatidylglycerol and phosphatidylethanolamine, respectively, by detergent-resistant phospholipase A in the presence of Ca2+ and (2) transfer of the acyl group of 2-acyl lysophospholipid to phosphatidylglycerol by a heat-labile factor(s) in the presence of diethyl ether. Neither fatty, acid acyl-CoA nor 1-acyl lysophospholipid could act as an acyl donor for phosphatidylglycerol. The heat-labile factor(s) was found in both the inner membrane and supernatant fractions.

Calcium↗
PubMed1977

Detergent-resistant phospholipase A of Escherichia coli K-12. Purification and properties.

Detergent-resistant phospholipase A, which is tightly bound to the outer membranes of Escherichia coli K-12 cells, was purified approximately 2000-fold to near homogeneity by solubilization with sodium dodecylsulfate and butan-1-ol, acid precipitation, acetone fractionation and column chromatographies on Sephadex G-100 in the presence of sodium dodecylsulfate and on DEAE-cellulose in the presence of Triton X-100. The final preparation showed a single band in the sodium dodecylsulfate gel system. The enzyme hydrolyzes both the 1-acyl and 2-acyl chains of phosphatidylethanolamine or phosphatidylcholine. It also attacks 1-acyl and 2-acylglycerylphosphorylethanolamine. Thus, this enzyme shows not only phospholipase A1 and lysophospholipase L1 activities but also phospholipase A2 and lysophospholipase L2 activities. The enzyme lost its activity completely on incubation at 80 degrees C for 5 min at either pH 6.4 or pH 8.0. It was stable in 0.5% sodium dodecylsulfate at below 40 degrees C. The enzyme was inactivated on incubation for 5 min at 90 degrees C in 1% sodium dodecylsulfate/1% 2-mercaptoethanol/4 M urea. The native and inactivated enzymes showed different protein bands with RF values corresponding to Mr 21 000 and Mr 28 000 respectively, in a sodium dodecylsulfate gel system. Triton X-100 seemed to protect the enzyme from inactivation. The purified enzyme was fully active on phosphatidylethanolamine in the presence of 0.0002% or 0.05% Triton X-100. The enzyme requires Ca2+. From its properties this enzyme seems to be identical with the enzyme purified from crude extracts of Escherichia coli B by Scandella and Kornberg. However, it differs from the latter in its positional specificity and susceptibility to sodium dodecylsulfate. Possible explanation of the difference of positional specificity of the two preparations is also described.

Drug Stability↗
PubMed1977

Positional specificity of phospholipase B of Penicillium notatum.

Phospholipase B[EC 3.1.1.5] of Penicillium notatum was shown to catalyze the following two reactions successively: diacylphospholipidlead to 1-monoacylphospholipid+fatty acid; and 1-monoacylphospholipid lead to glycerylphosphoryl-base+fatty acid. 1-Monoacylphospholipid was accumulated measurable in a reaction mixture containing methanol. An attempt to classify phospholipase B according to positional specificity is described.

Kinetics↗