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PubMed1991

Identification of low molecular weight GTP-binding proteins and their sites of interaction in subcellular fractions from skeletal muscle.

The presence of low molecular weight GTP-binding proteins was investigated in subcellular fractions from skeletal muscle. Skeletal muscle homogenate, transverse tubules, triads, sarcoplasmic reticulum membranes, and cytosol fractions were separated in sodium dodecyl sulfate-gel electrophoresis and blotted onto nitrocellulose. The presence of GTP-binding proteins was explored by incubation of these blots with [alpha-32P] GTP. GTP labeled two polypeptides of Mr = 23,000 and 29,000 in all the fractions examined. Binding of [alpha-32P]GTP was specific and dependent on Mg2+. The 23-kDa polypeptide was labeled to a higher extent with [alpha-32P]GTP than the 29-kDa polypeptide, although both were enriched in transverse tubule fractions. A GTP-binding polypeptide of 40 kDa was also enriched in transverse tubule preparations and identified as Gi alpha by immunostaining with anti-Gi alpha. Using a blot overlay approach and [alpha-32P]GTP-labeled cytosolic components, several polypeptides were identified that interact with the 23- and 29-kDa GTP-binding proteins. Among these components were polypeptides of Mr = 60,000, 47,000, 44,000, 42,000, and 38,000, which were mainly of cytosolic origin but also associated with triads and transverse tubule membranes. The 47-, 44-, 42-, and 38-kDa polypeptides were found to be structurally related to the glycolytic enzymes enolase, 3-phosphoglyceric phosphokinase, aldolase, and glycoeraldehyde-3-phosphate dehydrogenase, respectively. The purified glycolytic enzymes specifically bound the 23- and 29-kDa GTP-binding proteins under both denaturing and nondenaturing conditions. The association of the GTP-binding proteins with these polypeptides was resistant to detergents such as 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS), Triton X-100, and Tween. A 23-kDa GTP-binding protein purified from chromaffin cells bound to a 157-kDa polypeptide in triads and chromaffin cell membranes. The 157-kDa polypeptide was a minor component in these membranes and not related to the subunits of the dihydropyridine receptor. In view of the proposed function of low molecular weight GTP-binding proteins in processes such as membrane communication and secretion coupling, the association of these proteins with transverse tubules and triads in skeletal muscle is discussed in terms of a role in signal transmission.

Animals↗

PubMed1980

[Glycerolipid biosynthesis in vivo in subcellular fractions of greening wheat sprouts].

The kinetics of [I-14C]acetate incorporation into the glycerolipids of subcellular fractions during the greening of dark-grown wheat sprouts were studied. Up to 80% of the label were incorporated into neutral lipids in the darkness. The main labelled polar lipids were phosphatidic acid, phosphatidyl choline and phosphatidyl glycerol. The synthesis of the latter two compounds was predominantly coupled with the microsomal fraction. Illumination increased the galactolipid formation in the plastids, particularly that of galactosyldiacylglycerol. The role of phosphatidic acid and phosphatidyl choline as possible precursors of the galactolipid biosynthesis in developing plastids is discussed.

Acetates↗

PubMed1979

Influence of subcellular fractions of mammalian testes on the mutagenic activity of nitrofurans toward Escherichia coli; presence of a co-mutagen-like factor.

The activation of nitrofurans to mutagenic intermediates by testicular tissue was investigated. AF-2 and nitrofurazone were tested in a microsomal suspension assay with strain E. coli K-12 343/113 as indicator and subcellular fractions from rabbit testes. Different mutation patterns were observed in the presence or absence of testicular homogenate, indicating the presence of different mutagenic intermediates. The frequency of arg+ reversion increased proportionally to the homogenate concentration suggesting that the nitrofurans were activated by testicular components to intermediates that induced base-pair substitutions. Other experiments showed that a component of low molecular weight, present in the soluble fraction of homogenates of testes from rabbits, rats and monkeys, was responsible for the increased mutation frequency. It is concluded that this "co-mutagen-like" factor either alters the metabolism of nitrofurans in E. coli and/or promotes the formation of base-pair substitution-type mutations. This direct interaction between a nonenzymic component of mammalian testes and the mutation induction/expression process in E. coli suggests the role of co-mutagen-like factors in the sensitivity of testes to nitrofurans.

Animals↗

PubMed1984

Preparation and characterization of subcellular fractions suitable for studies of drug metabolism from the trunk kidney of the Northern pike (Esox lucius) and assay of certain enzymes of xenobiotic metabolism in these subfractions.

The present study was designed to prepare and characterize subcellular fractions from the trunk kidney of the Northern pike (Esox lucius), with special emphasis on the preparation of a microsomal fraction suitable for studying xenobiotic metabolism. The purity of the different fractions obtained by differential centrifugation, as well as the recovery of different organelles, was determined using both enzyme markers and morphological examination with the electron microscope. Finally, the subcellular distributions of several drug-metabolizing enzymes (NADPH-cytochrome c reductase, NADH-ferricyanide reductase, glutathione transferase, epoxide hydrolase) were determined. With the exception of NADPH-cytochrome c reductase, the subcellular distributions obtained here for drug metabolizing and marker enzymes closely resembled those reported for rat liver. NADPH-cytochrome c reductase was apparently partially solubilized here from microsomal vesicles by an endogenous protease, which reduced its usefulness as a marker enzyme and raises questions concerning the measurement of activities catalyzed by the cytochrome P-450 system in these subfractions. In other respects the microsomes and supernatant fraction prepared here from the trunk kidney of the pike seem to be as well suited for investigations of drug metabolism as are the corresponding fractions from rat and pike liver.

Animals↗

PubMed1990

Ferromagnetic isolation of endosomes: a novel method for subcellular fractionation of Xenopus oocytes.

A novel method has been developed using ferric particles to label endosomes, and to achieve magnetic sorting of the various endocytic compartments involved in lipoprotein uptake into cells. Ferric particles conjugated to a receptor-recognized ligand are bound to coated membrane pits and become internalized into the cytoplasm inside coated vesicles. After apparent fusion of the vesicles to tubular endosomes, the conjugates accumulate and finally discharge into multivesicular endosomes. Pulse-chase experiments elucidate the pathway of internalized conjugates and allow both early compartments (pinosomes and tubular endosomes) and late compartments (multivesicular endosomes and storage organelles) to be selectively labelled. After ferroloading of the various transport compartments, the cells are homogenized and subcellularly fractionated. Sorting of labelled endosomes is performed by a specially designed "free-flow" magnetic chamber. Prophase I-arrested oocytes of the toad Xenopus laevis are used as a model system for studying the transport pathway and the conversion of the yolk precursor vitellogenin. It is possible to follow the route of internalization of vitellogenin-iron conjugates via coated pits, coated vesicles, uncoated vesicles, tubular endosomes, multivesicular endosomes, and light primordial yolk platelets. These endosomes shuttle the ferric particles together with the vitellogenin from oolemma to performed heavy yolk organelles which are still growing. In addition, these various compartments can be isolated according to their function and subjected to electron microscopy and to gel electrophoresis for detailed characterization of their limiting membranes as well as their contents.

Animals↗

PubMed1977

Phospholipases A1 and A2 in subcellular fractions and plasma membranes of Krebs II ascites cells.

A method is described for the localization and characterization of phospholipases A1 and A2 (EC3.1.1.4) in Krebs II ascites cells, particularly in the plasma membranes. Cells were lysed with a Dounce homogenizer in an isotonic sucrose medium. Plasma membranes sediment with mitochondria and lysosomes during subcellular fractionation and are finally isolated on a continuous sucrose gradient. The membranes are localized at two levels in the gradient, at densities of 1.06 and 1.15, in which 5'-nucleotidase (EC 3.1.3.5) activity exhibits a 9- and 21-fold purification, respectively. Total contamination by endoplasmic reticulum, lysosomes, and mitochondria is 17 percent for the low-density membrane fraction and 25 percent for the high-density fraction. The phospholipases A present in Krebs II cells are active at pH 4.0 and pH 7.5. At the 2 pH values, they have A1 and A2 specificities. The intracellular distribution of acidic forms is comparable to that of acid phosphatase (EC 3.1.3.1), while neutral forms are localized like lactate dehydrogenase (EC 1.1.1.27). A small proportion of neutral phospholipase A2 has the same repartition on the sucrose gradient as nicotinamide adenine dinucleotide diaphorase (EF 1.6.4.3), an endoplasmic reticulum marker, and as 5'-nucleotidase, a plasma membrane marker.

Animals↗

PubMed1975

On the localisation of d-tubocurarine in rat liver lysosomes in vivo by electron microscopy and subcellular fractionation.

After i.v. injection in the rat, d-tubocurarine is taken up and concentrated by the liver. A method is developed for the visualisation of d-tubocurarine inside the liver cell by electron microscopy. Glutaraldehyde fixed liver blocks were immersed in an ammonium molybdate solution; d-tubocurarine was precipitated at sites of high concentration by molybdate, to form an insoluble d-tubocurarine-molybdate complex. This precipitate was found predominantly at the surface of lysosome-like particles, but also inside these organelles. In subcellular fractionation experiments, d-tubocurarine was found with a high relative specific "activity" in the lysosomal fraction, lending support to a lysosomal localisation of d-tubocurarine.

Acid Phosphatase↗

PubMed1985

Rat liver subcellular fractions catalyze aerobic binding of 1-nitro[14C]pyrene to DNA.

The recently characterized environmental mutagen and potential carcinogen 1-nitropyrene (NP) is known to bind DNA in Salmonella typhimurium, and also in anaerobic incubations catalyzed by purified xanthine oxidase. In this study we show that rat liver S9 supernatant, microsomal and cytosolic subcellular fractions are also able to catalyze the binding of 1-nitropyrene labeled with 14C to calf thymus DNA in vitro. In incubations conducted under air, S9 and microsomes from Charles River CD rats were the most active fractions, and NADPH was required for maximum activity (25-100 pmole NP bound/mg DNA/mg protein in 1 hr). S9 and microsomes had about one-fourth the activity under nitrogen, although less of this activity was NADPH-dependent. Binding in cytosolic incubations was generally low (1 to 5 pmole NP/mg DNA/mg protein in 1 hr), was somewhat enhanced under N2, and was more extensive in the absence of NADPH. Treatment of rats (Harlan Sprague-Dawley) with the inducing agents phenobarbital (PB), Aroclor 1254 (A), or 3-methylcholanthrene (3-MC) enhanced NADPH-dependent binding in aerobic S9 (2- to 5-fold) and microsomal (10- to 20-fold) incubations. The effects of induction regimen on binding assays conducted under N2 were more equivocal: 3-MC produced a 2-fold increase in binding in both S9 and microsomes, while the other two agents decreased binding from 50 to 75%. These results indicate that classic cytochrome P-450 inducers were able to stimulate activation of NP, but that this activation is not mediated solely by cytochrome P-450.

Aerobiosis↗

PubMed2000

Identification of distinct lymphocyte subsets responding to subcellular fractions of Mycobacterium bovis bacille calmette-Guérin (BCG).

In order to investigate the ability of Mycobacterium bovis BCG vaccination to induce immune responses toward different classes of mycobacterial antigens and the cell populations involved in such responses, proliferation of distinct human lymphocyte subsets from BCG-vaccinated donors in response to different subcellular fractions of BCG was analysed and compared with that of not sensitized subjects. Proliferation of different cell subsets was evaluated by flow cytometric determination of bromodeoxyuridine incorporated into DNA of dividing cells and simultaneous identification of cell surface markers. Although a certain degree of variability was observed among different donors, after 6 days of in vitro stimulation BCG-vaccinated subjects displayed, as a mean, a stronger blastogenic response to all the classes of antigens compared with non-sensitized ones. PPD, culture filtrates and membrane antigens induced a predominant proliferation of CD4+ T cells. In contrast, preparations enriched in cytosolic antigens elicited strong proliferation of gammadelta+ T cells which, as a mean, represented 55% of the proliferating cells. Although to a lesser extent, proliferation of gammadelta+ T cells was also elicited by preparations enriched in membrane and cell wall antigens. In response to the latter preparation proliferation of CD4+ T cells and CD16+/CD3- (natural killer (NK)) cells was observed, as well. In particular, cell wall antigens were found to induce significantly higher levels of proliferation of NK cells compared with all the other classes of antigens.

Adult↗

PubMed1999

Comparison of the chromium distribution in organs and subcellular fractions of normal and diabetic rats by using enriched stable isotope Cr-50 tracer technique.

The enriched stable isotope 50Cr(III) tracer technique combined with neutron activation analysis was used to examine the intracellular distribution of Cr(III) in the liver, pancreas, testes, and kidney homogenates of both normal and diabetic rats. Our new results showed that the nucleic fraction has the highest Cr concentration in the liver cell of both normal and diabetic rats. The diabetic rats retain more Cr in the mitochondrial and lysosomal fractions of liver homogenate than the normal. This is likely an indication of chromium participating in the glucose or lipid metabolism to compensate the low level of insulin in the body of diabetic rats. The concentrations of Cr in the subcellular fractions of pancreas, testes, and kidney in the normal rats are higher than those in the diabetic rats, which favor the hypothesis that Cr(III) plays its biological function via interaction with the insulin-sensitive tissues or enhancement of the sensitivity of the insulin receptor.

Animals↗

PubMed1992

Differential coupling of opioid binding sites to guanosine triphosphate binding regulatory proteins in subcellular fractions of rat brain.

In this study, we present evidence for the occurrence of mu, delta, and kappa opioid binding sites in synaptic plasma membranes (SPM) and microsomes of rat brain. Binding to all three opioid classes was inhibited by 5'-guanylylimidodiphosphate (Gpp[NH]p) in SPM, while microsomal sites proved to be insensitive to this GTP analog. Sensitivity was restored upon solubilization of microsomes with digitonin, suggesting that opioid receptors are physically separated from G proteins in this fraction. Modulation of microsomal binding by Na+ and Mn++ was greater than that of SPM. Pertussis toxin-catalyzed adenosine diphosphate (ADP) ribosylation revealed the presence of G proteins with alpha-subunit molecular weights of 40 kDa in both subcellular fractions. Basal low Km GTPase activity in SPM was greater than in microsomes. Etorphine elicited a concentration-dependent stimulation of guanosine triphosphatase (GTPase) activity in SPMs but not in microsomes, indicating functional coupling of opioid receptors to G protein in the former and an uncoupling in the latter. Microsomes from 3-day-old rat brain contained more mu opioid sites and they were more sensitive to Gpp(NH)p inhibition than those in adults. These results are consistent with the hypothesis that opioid binding sites in adult microsomes are internalized and G protein uncoupled, while those in neonates are newly synthesized, coupled receptors.

Adenosine Diphosphate↗

PubMed2006

Comparative proteome analysis of subcellular fractions from Borrelia burgdorferi by NEPHGE and IPG.

Borrelia burgdorferi, the cause of Lyme disease, produces excessive amounts of membrane lipoproteins such as outer surface protein A (OspA) when grown in vitro, and consequently many low or moderately abundant proteins are underrepresented when cell lysates are examined by 2-DE. We analyzed the B. burgdorferi B31 proteome computationally and by IPG or modified NEPHGE after subcellular fractionation into membrane-associated and soluble proteins. The B. burgdorferi B31 theoretical proteome is comprised of 1623 proteins and has a mean pI of 8.36 and a median pI of 9.03 with 68% of the proteome possessing a pI >/=7.5. Separation of soluble proteins by IPG resulted in 205 individual spots and identification of 78 protein spots by MALDI-TOF MS. Separation by modified NEPHGE routinely resulted in approximately 185 soluble and 160 membrane protein spots with the identification of 88 individual protein spots combined by MALDI-TOF MS. Homologues to GroEL and aminopeptidase I were present in greater amounts in the membrane faction, with enolase at nearly equivalent amounts in the soluble and membrane fractions. Identification of proteins isolated and separated by such methods will enable future determination of proteome changes in membrane and soluble protein fractions as spirochetes adapt to their changing environments.

Bacterial Proteins↗

PubMed2003

Mutagenic activation of arylamines by subcellular fractions of Chamaelea gallina clams exposed to environmental pollutants.

Biochemical measurements in the sentinel clam Chamaelea gallina have been used as biomarkers of marine pollution. In this study, S9, cytosolic fractions (CF), and microsomal fractions (MF) prepared from unexposed clams and clams exposed to model pollutants were used to activate 2-aminoanthracene (2-AA) and 2-acetylaminofluorene (AAF) to mutagens in Salmonella typhimurium strain BA149, which overexpresses O-acetyltransferase. Arylamine activation was similar with subcellular fractions from unexposed and Aroclor 1254-exposed clams, but decreased with fractions from As(III)- and Cu(II)-exposed clams. Bioactivation of arylamines by CF was higher than by MF, and higher with NADH than with NADPH as the reducing agent. alpha-Naphthoflavone inhibited AAF activation by CF and MF, but increased 2-AA activation nearly twofold. In contrast to the results with arylamine activation, benzo[a]pyrene hydroxylase (BPH) activity increased twofold in fractions from Aroclor 1254- and Cu(II)-exposed clams. Activation of 2-AA was also evaluated using S9 fractions from clams sampled at littoral sites with different pollutant levels. Compared to a reference site, lower 2-AA bioactivation and higher BPH activity were found in clams containing high levels of copper and organic contaminants, although the differences were not statistically significant. While these findings agree with the results of the model Cu(II) exposure, the effects of other pollutants cannot be ruled out. The results of the study demonstrate that arylamine activation by clams is not preferentially catalyzed by microsomal monooxygenases but by unknown cytosolic system(s), and that bioactivation of 2-AA and AAF appears to occur by different pathways.

2-Acetylaminofluorene↗

PubMed2001

Processing of the insulin-like growth factor-II-mannose 6-phosphate receptor in isolated liver subcellular fractions.

A truncated, soluble form of the insulin-like growth factor-II-mannose 6-phosphate (IGF-II-M6P) receptor has been identified in serum and shown to be released from cultured tissues and cells, liver being the main contributor to serum receptor in adult rats. In the present study, the processing of the IGF-II-M6P receptor has been characterized in isolated liver subcellular fractions using ligand binding, affinity crosslinking, and Western immunoblotting techniques. The receptor in plasma membrane fractions differed from that in Golgi-endosomal fractions by: (i) a lower molecular size upon reducing polyacrylamide gel electrophoresis (245 vs. 255 kDa); (ii) a less tight membrane association as judged upon extractibility by NaCI; and (iii) the inability to recognize antibody anti-22C, directed against the cytoplasmic domain of the receptor. Incubation of cell fractions at 30 degrees C led to a pH- and time-dependent release of the receptor into the medium. The pH optimum for release was 5.5 in the Golgi-endosomal fraction and 7.5 in plasma membrane fractions; at this pH, approximately 2% and 20%-30% of total receptors were released per hour, respectively. Receptor release was inhibited in a dose-dependent manner by aprotinin, benzamidine, and leupeptin in the Golgi-endosomal fraction, and by 1,10 phenanthroline in plasma membrane fractions, although high concentrations were required for inhibition. The receptor released from Golgi-endosomes showed a 5-10 kDa reduction in size and a loss of ability to recognize antibody anti-22C, but that released from plasma membranes showed little or no changes in size. We conclude that soluble, carboxy-terminally truncated forms of the IGF-II-M6P receptor are generated from the intact receptor in isolated Golgi-endosomal and plasma membrane fractions. However, receptor processing in these fractions exhibits different properties, suggesting the involvement of different proteases.

Animals↗

PubMed1982

[Action of the "delta-sleep peptide" on monoamine oxidase and acetylcholinesterase activity in subcellular fractions from different rabbit brain formations in vivo].

Administration of delta-sleep-inducing peptide (DSIP) in vivo in a dose of 30 microgram/kg bw brings about MAO-A (substrate-serotonin) activation in synaptosome subfractions and cellular mitochondria from the brain structures (motor cortex, nucleus caudatus, thalamus). Activity of MAO-B (substrate-p-nitrophenylethylamine) and acetylcholinesterase was inhibited negligibly and specifically in subcellular fractions of the test brain structures. The results suggest that DSIP effects the regulatory or modulation function in the synapse. As one of the elements of sleep mechanisms this peptide induces a number of processes, particularly in serotonin metabolism.

Acetylcholinesterase↗

PubMed2004

Relationship between Alzheimer's disease clinical stage and Gq/11 in subcellular fractions of frontal cortex.

Alzheimer's disease (AD) is associated with impaired coupling of cell surface muscarinic cholinergic receptors to G proteins of the Gq/11 class in brain. This alteration may contribute to progression of cognitive impairment during the course of the disease. We hypothesized that increasing severity of cognitive impairment would be related to decreased levels of Gq/11 detected in key subcellular fractions made from postmortem brain tissue. In this study, we used Western blotting to determine the quantity of Gq/11alpha in P2, synaptic plasma membrane, cytoplasm, microsomal membrane, and lipid raft fractions prepared from superior frontal cortex gray matter of 25 patients with clinical AD confirmed by post-mortem examination. Multiple linear regression analysis that adjusted for age, sex, and education showed a linear relationship between frontal cortex synaptic plasma membrane Gq/11alpha levels and severity of cognitive impairment determined by Mini Mental State score measured proximate to death.

Age Factors↗

PubMed1987

Labeling of phosphatidylcholines of retina subcellular fractions by [1-14C]eicosatetraenoate (20:4(n-6)), docosapentaenoate (22:5(n-3)) and docosahexaenoate (22:6(n-3)).

The labeling of molecular species of phosphatidylcholine (PC) has been studied in bovine retinas incubated for 2 h with (1-14C)-labeled (n-6) eicosatetraenoate (n-3) docosapentaenoate and (n-3) docosahexaenoate (20:4, 22:5 and 22:6, respectively) and in four subcellular fractions isolated after such incubations. Of the total radioactivity incorporated in PC, the following percentages of the above fatty acids, respectively, are found in its dipolyunsaturated species: 58, 56 and 53% in rod outer segments; 29, 41 and 49% in mitochondria; 24, 28 and 39% in microsomes; 12, 14 and 16% in postmicrosomal supernatants; 28, 36 and 58% in entire retinas. The remainder percentages are in tetra-, penta- and hexaenoic species of PC, respectively. The levels of pentaenoic species in the PCs of all fractions are similar, while tetraenes are lowest and hexaenes highest in photoreceptor membranes. Dipolyunsaturated species are highly concentrated in photoreceptor membranes, but are minor components of mitochondrial, microsomal and cytosolic PC. The specific radioactivities of tetraenoic, pentaenoic and hexaenoic PCs are decreasingly lower in the following order: postmicrosomal supernatants, microsomes, mitochondria, photoreceptor membranes. In contrast, the specific radioactivities of dipolyunsaturated PCs are higher in mitochondria and microsomes than in the other fractions, especially with 22:5 and 22:6. It is suggested that mitochondria as well as the endoplasmic reticulum could play a role in the synthesis and further modifications of dipolyunsaturated PCs before being supplied to photoreceptor membranes.

Animals↗

PubMed1990

Metabolism of nitroxide spin labels in subcellular fraction of rat liver. I. Reduction by microsomes.

As part of an ongoing study of the role of subcellular fractions on the metabolism of nitroxides, we studied the metabolism of a set of seven nitroxides in microsomes obtained from rat liver. The nitroxides were chosen to provide information on the effects of the type of charge, lipophilicity and the ring on which the nitroxide group is located. Important variables that were studied included adding NADH, adding NADPH, induction of enzymes by intake of phenobarbital and the effects of oxygen. Reduction to nonparamagnetic derivatives and oxidation back to paramagnetic derivatives were measured by electron-spin resonance spectroscopy. In general, the relative rates of reduction of nitroxides were similar to those observed with intact cells, but the effects of the various variables that were studied often differed from those observed in intact cells. The rates of reduction were very slow in the absence of added NADH or NADPH. The relative effect of these two nucleotides changed when animals were fed phenobarbital, and paralleled the levels of NADPH cytochrome c reductase, cytochrome P-450, cytochrome b5 and NADH cytochrome c reductase; results with purified NADPH-cytochrome c reductase were consistent with these results. In microsomes from uninduced animals the rate of reduction was about 10-fold higher in the absence of oxygen. The products of reduction of nitroxides by microsomes were the corresponding hydroxylamines. We conclude that there are significant NADH- and NADPH-dependent paths for reduction of nitroxides by hepatic microsomes, probably involving cytochrome c reductases and not directly involving cytochrome P-450. From this, and from parallel studies now in progress in our laboratory, it seems likely that metabolism by microsomes is an important site of reduction of nitroxides. However, mitochondrial metabolism seems to play an even more important role in intact cells.

Animals↗