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Biomedical subjects

J Zborowski

Publications and source records attributed to J Zborowski.

At least 37 records · Page 2Linked to original sources
PubMed1983

Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane.

It is shown that the trypsin-treatment of rat liver mitochondria, depleted of the outer membrane, causes a strong inactivation of phosphatidylserine decarboxylase. This inactivation is dependent on trypsin concentration and the time of digestion in a similar manner as the inactivation of cytochrome oxidase. Under these conditions only a moderate inactivation of succinate dehydrogenase is observed. Phosphatidylserine decarboxylase is thus localized in the outer leaflet of the inner mitochondria membrane or, at least, is accessible from the outer surface of the inner membrane.

Animals↗
PubMed1983

The metabolism of CDP-diacylglycerol and phosphatidylinositol in the microsomal fraction of rat liver. Effects of chlorpromazine, magnesium and manganese.

1. The metabolism of CDPdiacylglycerol and phosphatidylinositol was measured using substrates bound to the microsomal membranes of rat liver. 2. Chlorpromazine inhibited the degradation of [14C]CDPdiacylglycerol and the concomitant inositol-independent release of 14C in water-soluble products in the presence of various concentrations of Mg2+ and Mn2+. 3. The activity of CDPdiacylglycerol inositol phosphatidyltransferase was measured by determining the rate of incorporation of [3H]inositol into phosphatidylinositol, and by the inositol-dependent release of water-soluble 14C from [14C]CDPdiacylglycerol. Both of these parameters were inhibited by chlorpromazine in incubations that contained rate-limiting concentrations of Mg2+. However, chlorpromazine stimulated the reaction when 20 mM Mg2+, 0.5 mM Mn2+, 2 mM Mn2+ or 20 mM Mn2+ was added to the incubations. 4. Low concentrations of chlorpromazine increased an inositol-exchange reaction in the presence of 0.5 mM Mn2+ whereas higher concentrations of chlorpromazine inhibited. Chlorpromazine had relatively less effect on the inositol-exchange reaction at higher concentrations of Mn2+. 5. The action of chlorpromazine in decreasing the breakdown of CDPdiacylglycerol and in stimulating its conversion to phosphatidylinositol could explain part of the mechanism by which this compound and other amphiphilic cations increase the synthesis of acidic phospholipids.

Animals↗
PubMed1982

Transfer properties of the bovine brain phospholipid transfer protein. Effect of charged phospholipids and of phosphatidylcholine fatty acid composition.

The monolayer technique has been used to study the transfer of [14C]phosphatidylinositol from the monolayer to phosphatidylcholine vesicles. An equivalent transfer rate was found for egg phosphatidylcholine, dioleoylphosphatidylcholine, dielaidoylphosphatidylcholine and dipalmitoylphosphatidylcholine. A reduced transfer rate was found for a shorter-chain derivative, dimyristoylphosphatidylcholine, and for species with two polyunsaturated fatty acid chains such as dilinoleoylphosphatidylcholine, diheptadecadienoylphosphatidylcholine, dilinolenoylphosphatidylcholine and diether and dialkyl derivatives. No activity was found for 1,3-dipalmitoylphosphatidylcholine. The presence of up to 5 mol% phosphatidylinositol in egg phosphatidylcholine vesicles had no effect on the transfer rate. Introduction of more than 5 mol% phosphatidylinositol or phosphatidic acid into the phosphatidylcholine vesicles gradually decreased the rate of phosphatidylinositol transfer from the monolayer. 20 mol% acidic phospholipid was nearly completely inhibitory. Transfer experiments between separate monolayers of phosphatidylcholine and phosphatidylinositol showed that the protein-bound phosphatidylcholine is readily exchanged for phosphatidylinositol, but the protein-bound phosphatidylinositol exchange for phosphatidylcholine occurs at a 20-times lower rate. The release of phosphatidylinositol is dependent on the lipid composition and the concentration of charged lipid in the acceptor membrane, but also on the ratio between donor and acceptor membranes. The main transfer protein from bovine brain which transfers phosphatidylinositol and phosphatidylcholine transfers also phosphatidylglycerol, but not phosphatidylserine or phosphatidic acid. The absence of significant changes in the surface pressure indicate that the phosphatidylinositol and phosphatidylcholine transfer is not accompanied by net mass transfer.

Animals↗
PubMed1982

Transfer properties of the bovine brain phospholipid transfer protein. Specificity towards phosphatidylcholine analogs and the inhibitory effect of sphingomyelin.

A coupled transport of phosphatidylinositol from the monolayer to phosphatidylcholine vesicles, and a phosphatidylcholine transport in the reverse direction in the presence of bovine brain transfer protein is demonstrated. No significant amounts of protein accumulate at the interface during the transfer reaction. The transfer protein from bovine brain shows a lower specificity for phosphatidylcholine than does the transfer protein from bovine liver. Relative to egg phosphatidylcholine a low transfer rate is found for derivatives with a chain length of 14 carbon atoms and a distance between phosphorus and nitrogen of 6 carbon atoms. The gel state of phosphatidylcholine does not reduce the transfer reaction as catalyzed by the bovine brain protein. The transfer of phosphatidylinositol is inhibited by sphingomyelin. The presence of 200 mM K+ or 1mM Ca2+ does not affect the transfer activity of the bovine brain protein. Divalent ions at concentrations higher than 5 mM cause a fusion of vesicles with monolayers. The pH optimum of the phosphatidylinositol transfer reaction is 8.

Animals↗
PubMed1980

Effect of phospholipid composition on the surface potential of liposomes and the activity of enzymes incorporated.

1. Microsomes of rat liver and brain and mitochondria of rat liver and guinea-pig brown adipose tissue were solubilized with the nonionic detergent Lubrol-WX and the solubilized material was incorporated into liposomes of various phospholipid composition. In proteoliposomes thus formed the kinetics of arylsulphatase, glycerol-3-phosphate dehydrogenase, monoamine oxidase and acetylcholinesterase were measured. 2. It was shown that the apparent Km values of arylsulphatase and glycerol-3-phosphate dehydrogenase were higher in liposomes prepared with negatively charged phospholipids and lower in liposomes containing positively charged organic amines, as compared with th Km value of enzymes incorporated into liposomes prepared from phosphatidylcholine alone. The opposite was true for monoamine oxidase and acetylcholinesterase, i.e. enzymes possessing cationic substrates. Phospholipid composition did not essentially influence the activity of the enzymes extrapolated for infinite substrate concentration (V values). 3. As compared with proteoliposomes made from phosphatidylcholine, the binding constant (Ka) of 8-anilino-1-naphthalene sulphonate was higher when the vesicles contained acidic phospholipids or bis(hexadecanyl)phosphate and lower when they contained organic amines. 4. A correlation between changes of the surface potential calculated from Ka values of anilino-naphthalene sulphonate and variations in apparent Km values of the four enzymes under investigation indicates that the activity of membrane-bound enzymes may be modulated by charged phospholipids due to decreasing or increasing substrate concentration in the unstirred layer, as predicted from the Boltzmann distribution.

Acetylcholinesterase↗
PubMed1980

Decarboxylation of phosphatidylserine by rat liver mitochondria.

1. The decarboxylation of phosphatidylserine was studied using particles obtained by sonication of rat liver mitochondria as the source of the enzyme, and liposomes prepared from total microsomal phospholipids labelled in phosphatidylserine. The reaction was followed by measuring formation of either CO2 or phosphatidylethanolamine. 2. The reaction was inhibited when isotonic sucrose was substituted by equiosmotic solutions of electrolytes (acetate or phosphate). 3. Optimum pH for the reaction was 5.0 - 5.2. 4. At pH 7.4 the reaction was stimulated by the cytoplasmic fraction from rat liver, most likely due to the action of phospholipid transfer protein(s). 5. The reaction was stimulated by Mg2+ and Mn2+. Maximum stimulation occurred at 2 - 3 mM-concentration of the divalent cation.

Animals↗
PubMed1977

Synthesis of phospholipids in mitochondria and other membrane fractions of rabbit reticulocytes.

1. Reticulocytosis of 40-50% was obtained in rabbits by daily bleeding. Reticulocytes (plus erythrocytes) were subfractionated into plasma membrane fraction, mitochondria and the post-mitochondrial fraction. 2. In all fractions, fatty acids were incorporated into phospholipids. This process was ATP dependent and represented acylation of lysophospholipids. 3. Incorporation of fatty acids into lysophosphatidic and phosphatidic acids occurred only in the presence of sn-glycerol 3-phosphate and was observed in mitochondria and the post-mitochondrial fraction. It represents a two-step acylation of sn-glycerol 3-phosphate. 4. Incorporation of phosphorylcholine from CDPcholine into phosphatidylcholine was observed in the mitochondrial and the post-mitochondrial fractions. This activity was correlated with NADPH-cytochrome c reductase and was probably connected with the remnants of the endoplasmic reticulum.

Animals↗
PubMed1977

Leakage of sucrose from phosphatidylcholine liposomes induced by interaction with serum albumin.

Liposomes composed of rat-liver phosphatidylcholine rapidly lose entrapped sucrose when incubated in presence of blood or of solutions of bovine serum albumin. The phenomenon can not be ascribed to phospholipase A activity, since no such activity towards phosphatidylcholine substrates could be detected in various albumin preparations. Upon gel filtration on Sepharose 4B or Sephadex G-100 of incubated mixtures of radioactive liposomes and albumin, association of phosphatidylcholine with the albumin could be demonstrated. No measurable quantities of protein were found associated with liposomes. The albumin-associated phosphatidylcholine is hydrolyzed by pancreatic phospholipase A more slowly than free liposomal phosphatidylcholine, indicating a non-lamellar orientation of the associated phospholipid. The binding of phosphatidylcholine to albumin proceeds at a slow rate: increase of the amount of phosphatidylcholine bound continues over a period of several hours reaching a maximum at approx. 1 mol of phosphatidylcholine per mol of albumin. The process is reversible as indicated by transfer of albumin-associated radioactive phosphatidylcholine to unlabeled liposomes. The association between albumin and phosphatidylcholine is believed to be of the same type as described recently by Jonas (Jonas, A. (1976) Biochim. Biophy. Acta 427, 325-336). The consequences of these observations are discussed with respect to the use of liposomes as carriers to introduce substances into cells.

Blood↗
PubMed1977

Cardiolipin synthesis during the cell cycle of the yeast Saccharomyces cervisiae.

Cardiolipin synthesis was studied during the aerobic synchronous growth of aerobically grown yeast Saccharomyces cerevisiae. The time course of the synthesis was stepwise and the rise in cardiolipin level in cells coincided in time with the increase in cytochrome oxidase activity. This finding supports the notion of discontinuous completion of the inner mitochondrial membrane and hints at a close relation between cardiolipin and cytochrome oxidase activity.

Aerobiosis↗