Search PubMed⌕ Search

Biomedical subjects

S Nojima

Publications and source records attributed to S Nojima.

At least 127 records · Page 7Linked to original sources
PubMed1982

Liposomal membranes. XI. A suggestion to structural characteristics of acido-thermophilic bacterial membranes.

To understand the role of omega-cyclohexyl fatty acid residue of lipids in acido-thermophilic bacterial membranes, three unusual phosphatidylcholines, 1, 2-di-11-cyclohexylundecanoyl-L-alpha-phosphatidylcholine (11CYPC), 1,2-di-13-cyclohexyltridecanoyl-L-alpha-phosphatidylcholine (13CYPc), and 1-13-cyclohexyltridecanoyl-2-11-cyclohexylundecanoyl-L-alpha- phosphatidylcholine (1-13CY-2-11CYPC) were prepared and the steady-state fluorescence anisotropy of 1, 6-diphenylhexatriene (DPH) in the hydrophobic domain of these liposomal bilayers was determined. Compared with the case of dipalmitoyl (DPPC) or dimyristoyl phosphatidylcholine (DMPC), introducing the omega-cyclohexyl moiety onto lecithins makes the bilayers fluid below the phase transition temperature, while immobilizes them above the phase transition temperatures. The properties of the unusual phosphatidylcholine liposomes suggested by the steady-state fluorescence anisotropy investigation were in good agreement with those obtained from the thermotropic and permeability investigations. Results obtained are discussed from the view point of the role and function of lipid membranes of acido-thermophilic bacteria which contain unusual fatty acids.

Bacillus↗
PubMed1982

Transacylation between diacylphospholipids and 2-acyl lysophospholipids catalyzed by Escherichia coli extract.

When 2-acyl lysophosphatidylethanolamine, 2-acyl lysophosphatidylglycerol, and 2-acyl lysophosphatidylcholine were incubated with the envelope fraction of Escherichia coli in the presence of Mg2+ ion, they were acylated to the corresponding diacylphospholipids. The inner and outer membrane fractions both had acylation activity. 2-Acyl lysophosphatidylethanolamine was shown to be acylated at the 1-position by an endogenous acyl donor present in the envelope fraction. Under the conditions used, acylation was specific for 2-acyl lysophosphatidylethanolamine, and the 1-acyl isomer was not appreciably acylated. The acylation was resistant to N-ethylmaleimide and p-chloromercuribenzoate, but was inhibited by Cu2+ and Hg2+ ions. Ca2+ and Mg2+ ions stimulated the activity about 1.5-fold, but EDTA was not inhibitory. The activity had a broad pH optimum between 6 and 8. On boiling the envelope fraction, about 55% of the activity was lost rapidly, while the remainder was lost gradually. The endogenous acyl donor present in the envelope fraction was shown to be membrane phospholipids. The acylation was not observed with free fatty acids prepared by alkaline hydrolysis of the phospholipids. Studies with purified phospholipids showed that the major phospholipids of E. coli (phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin) and phosphatidic acid acted as acyl donors. Thus, transacylation between diacylphospholipids and 2-acyl lysophospholipids catalyzed by E. coli envelopes was demonstrated.

Acylation↗
PubMed1982

Synthesis of various phospholipids from 2-acyl lysophospholipids by Escherichia coli extract.

When 2-[14C]acyl lysophosphatidylethanolamine was incubated with the envelope fraction of E. coli in the presence of Mg2+ ion, phosphatidylethanolamine, acylphosphatidylglycerol and free fatty acid were produced. When 2-[14C]acyl lysophosphatidylglycerol was examined similarly, six phospholipids as well as free fatty acid were produced. These were dilysocardiolipin, lysocardiolipin, phosphatidylglycerol, cardiolipin, bis(monoacylglycero)phosphate and acylphosphatidylglycerol; they were identified by thin layer chromatography, acetolysis and mild alkaline hydrolysis. Studies with an E. coli mutant which is deficient in cardiolipin synthase showed that dilysocardioilipin, lysocardiolipin and cardiolipin were synthesized by cardiolipin synthase. Bis(monoacylglycero)phosphate as well as acylphosphatidylglycerol was produced by acylphosphatidylglycerol synthase. While phosphatidylglycerol and cardiolipin were produced predominantly from 2-acyl lysophosphatidylglycerol, almost the same amounts of dilysocardiolipin, lysocardiolipin and bis(monoacylglycero)phosphate were produced from the 1-acyl and 2-acyl isomers. Metabolites of 2-[14C]acyl lysophosphatidic acid were also examined. Phosphatidic acid, acylphosphatidylglycerol, free fatty acid and monoglyceride were produced, together with a small amount of diglyceride.

Escherichia coli↗
PubMed1982

Incorporation of spin-labeled ganglioside analogues into cell and liposomal membranes.

Ganglioside analogues (gangliosides) with an electron spin resonance label in a long aliphatic hydrocarbon chain were used to investigate the possible insertion of the sialoglycolipid into the plasma membrane of cells. Three types of ESR signals observed in the labeled glycolipids were distinguished. They characteristically indicate an isotropic tumbling motion of spin label in solution, the micellar state of the glycolipid, and an anisotropic motion in a lipid bilayer. Below CMC, gangliosidoide carrying one aliphatic hydrocarbon chain showed an isotropic tumbling motion. After the gangliosidoide had been incubated with liposomes or blood cells, there was an immediate change to an ESR signal showing an anisotropic motion. The signal was typical of the spin-label in liposomes prepared in the presence of spin-labeled sialoglycolipid. It can be concluded that the gangliosidoide was inserted into the lipid phase of liposomal or cellular membranes from the incubation medium. The overall splitting (2A parallel) of 5SL-gangliosidoides in membranes was larger than those of 5SL-galactosylceramide, 5SL-phosphatidylcholine, and 5SL-stearic acid, though the 2A parallel of 12SL-gangliosidoide was almost the same as those of other lipids having a nitroxide group in the 12-position of an acyl chain. This indicates that the head group movement is restricted in gangliosidoide molecules.

Animals↗
PubMed1982

Activation of histamine secretion from rat mast cells by phosphatidylserine analogues resistant to phospholipase A action.

In order to elucidate how phosphatidylserine enhances histamine release induced by concanavalin A from rat mast cells, two phosphatidylserine analogues were synthesized and their effects were examined. A dialkyl analogue of phosphatidylserine, both ester bonds of which are replaced by ether bonds, potentiated histamine secretion from mast cells stimulated by concanavalin A, although it was much less active than natural phosphatidylserine. An alkyl analogue of phosphatidylserine, in which an ether bond is present at the 1 position, showed almost the same low activity as the dialkyl analogue. It is suggested that deacylation of the incorporated phosphatidylserine by phospholipase A is not required for potentiation by phosphatidylserine and the existence of an ester bond at position 1 is important for phosphatidylserine to enhance concanavalin A-induced histamine secretion from mast cells.

Animals↗
PubMed1982

Incorporation of a ganglioside and spin-labeled ganglioside analogue into cell and liposomal membranes.

When an aqueous solution of a spin-labeled "two tail" gangliosidoid was incubated with liposomes or sheep erythrocytes, the broad single resonance line in the ESR spectrum disappeared and a signal showing an anisotropic motion appeared, indicating that the spin-labeled "two tail" gangliosidoid in the micellar state was transferred to the lipid phase of the acceptor membranes. The transfer was temperature- and time-dependent, irrespective of the acceptor membranes, indicating that the rate of transfer is determined by the escape of monomers from the micelles. The kinetics and temperature-dependence of the association of ganglioside II3NeuAc-GgOse4Cer with sheep erythrocytes was very similar to that of the "two tail" gangliosidoid, indicating that parts of ganglioside II3NeuAc-GgOse4Cer could be incorporated into the lipid phase of membranes via a similar mechanism.

Animals↗
PubMed1982

Physical properties and barrier functions of synthetic glyceroglycolipids.

Four glyceroglycolipids containing dipalmitylglycerol were synthesized. The thermotropic behavior and barrier function of aqueous suspensions of these glyceroglycolipids were studied. The gel to liquid crystalline phase transition temperatures of these glycolipids were higher than that of dipalmitoylphosphatidylcholine. The interaction between headgroups in glyceroglycolipids might be stronger than that in dipalmitoylphosphatidylcholine. Diglycosyl dipalmitylglycerols could form liposomes and function as a barrier against water-soluble small molecules (glucose, UmP, and H+) when assayed below their phase transition temperatures, like dipalmitoylphosphatidylcholine liposomes. The fundamental properties of glyceroglycolipid membranes so far examined were rather similar to those of phospholipid membranes, with the exception that the permeability rate of water through glycolipid membranes was higher than that through phospholipid membranes. This property might cause the apparent sensitivity difference between liposomes prepared from glycolipids and those from phospholipids to amphotericin B.

Amphotericin B↗
PubMed1982

Immunogenicity of liposomal model membranes sensitized with spin-labeled haptens and topographical distribution of haptens on the membranes.

The relation between the in vitro immunogenicity of phosphatidylcholine liposomes containing 2,4-dinitrophenyl-6-N-aminocaproylphosphatidylethanolamine (DNP-Cap-PE) as a hapten and the topographical distribution of the haptens on lipid membranes was studied. In distearoylphosphatidylcholine liposomes, the immunogenicity increased with increase of cholesterol content in the liposomal membranes. The electron spin resonance spectra of spin-labeled DNP-Cap-PE in distearoylphosphatidylcholine liposomes indicated that cholesterol affected the topographical distribution of spin-labeled DNP-Cap-PE on the membranes. In the absence of cholesterol, a considerable amount of haptens was clustered on the distearoylphosphatidylcholine membranes, but with increase of cholesterol, random distribution of the haptens on the membranes increased. The cholesterol-dependent change in the topographical distribution of the haptens on the membranes paralleled the change of immunogenicity, i.e., the immunogenicity was low when haptens were clustered on the liposomal membranes. Haptens arranged at a proper distance on the membranes may be required for optimum immune response.

Animals↗
PubMed1982

Intermolecular interaction between glycolipids and glycophorin on liposomal membranes.

The haptenic activity of Forssman glycolipid was affected by glycophorin, and the interaction of glycophorin with lectins was also affected by the glycolipids, when both glycophorin and Forssman glycolipid or globoside were incorporated into the same phosphatidylcholine liposomes. Glycophorin incorporated into phospholipid membranes could interact with lectins, whereas that in glyceroglycolipid membranes could not. These findings suggest that glycophorin and glycolipids may interact, affecting the conformation of their sugar residues, probably through a carbohydrate-carbohydrate interaction. Such an interaction may cause suppression or stimulation of the reactivity of glycoconjugates with lectins or antibodies. Lactosylceramide showed only a slight effect on the interaction between glycophorin and lectins. We suggest that the structure of the sugar residues as well as the lateral distribution of molecules was important for the intermolecular interaction.

Animals↗
PubMed1981

Studies on the interaction of Sendai virus with liposomal membranes. Sendai virus-induced agglutination of liposomes containing glycophorin.

Liposomes constituted with the major sialoglycoprotein of human erythrocytes, glycophorin, were used as models for studies on cell-virus interactions. Liposomes composed of egg yolk phosphatidylcholine, cholesterol and glycophorin were found to interact with the paramyxovirus HVJ to form aggregates. The aggregation process was temperature dependent: it was maximal at 0 degrees C and decreased with increase of the incubation temperature. The activity of viral neuraminidase is also temperature dependent, and it increases with increase of the incubation temperature; release of N-acetylneuraminic acid was negligible at 0 degrees C. Shift-up of the incubation temperature immediately cancelled HVJ-induced agglutination of liposomes. Viruses attached to liposomes seemed to be released into the supernatant when the 'virus-liposome' complex formed at 0 degrees C was incubated at 37 degrees C, possibly as a result of breakdown of the 'binding' site by neuraminidase. The characteristics of the interaction of HVJ with liposomes containing glycophorin appeared to be phenomenologically similar to those of HVJ-cell interaction.

Agglutination↗
PubMed1981

Haptenic activity of galactosyl ceramide and its topographical distribution on liposomal membranes. I. Effect of cholesterol incorporation.

The relation between the immune-reaction of phosphatidylcholine liposomes containing spin-labeled galactosyl ceramide with or without cholesterol and the topographical distribution of the glycolipid in membranes was studied. In egg yolk phosphatidylcholine liposomes, both immune agglutination and antibody binding occurred, irrespectively of the presence of cholesterol, though the motion of the fatty acyl chain of spin-labeled galactosyl ceramide was restricted by cholesterol. In dipalmitoyl phosphatidylcholine liposomes, unlike in egg yolk phosphatidylcholine liposomes, the immune-reaction depended on the cholesterol content. The electron spin resonance (ESR) spectra of spin-labeled galactosyl ceramide in dipalmitoyl phosphatidylcholine liposomes indicated that cholesterol affected the topographical distribution of spin-labeled galactosyl ceramide in the liposomes. Without cholesterol, most of the spin-labeled galactosyl ceramide was clustered on the dipalmitoyl phosphatidylcholine membrane, but with increase of cholesterol, random distribution of hapten on the membrane increased. The cholesterol-dependent change in the topographical distribution of hapten on the membranes was parallel with that of immune reactivity. 'Aggregates' composed solely of galactosyl ceramide did not show any binding activity with antibody. The findings suggest that the recognition of galactosyl ceramide by antibody depended on the topographical distribution of hapten molecules. Phosphatidylcholine and/or cholesterol may play roles as 'spacers' for the proper distribution of 'active' haptens on the membranes. The optimum density of haptens properly distributed on liposomal membranes is discussed.

Agglutination↗