26 documentos corresponden a la consulta.
Palabras contadas: cytoplasm: 47
Gholipour, Y. - Nonami, H. - Erra-Balsells, R.
J. Am. Soc. Mass Spectrom. 2008;19(12):1841-1848
2008
Temas: Carbohydrates - Carbon nanotubes - Cells - Cytology - Glucose - Military engineering - Organic compounds - Polysaccharides - Positive ions - Potential flow
Descripción: Single-cell cytoplasm sap (1-10 pL) was extracted by using a pressure probe glass microcapillary tip from tulip leaf and bulb and analyzed by UV-MALDI-TOF MS for free underivatized carbohydrate content. Three matrices including 2,5-dihydroxybenzoic acid (DHB), 2,4,6-trihydroxyacetophenone (THAP), and carbon nanotubes (CNTs) in positive ion mode were selected for analysis because of acceptable carbohydrate-related signal reproducibility. Disaccharide and oligosaccharide (up to 15 Hex when THAP was used, 11 Hex with DHB, and 7 Hex with CNTs) were detected in tulip bulb cell cytoplasm sample. When DHB was used as matrix, neutral carbohydrates were more abundantly detected as sodiated cations; the sugar-related signals, however, appeared as dominant potassiated cations when THAP and CNTs were used. Small amount of monosaccharide was also detected in bulb cell cytoplasm with CNTs as matrix. UV-MALDI-TOF MS of leaf cell extract resulted in high-resolution detection of hexose and disaccharide with DHB, THAP, and CNTs. © 2008 American Society for Mass Spectrometry.
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Harrell, J.M. - Murphy, P.J.M. - Morishima, Y. - Chen, H. - Mansfield, J.F. - Galigniana, M.D. - Pratt, W.B.
J. Biol. Chem. 2004;279(52):54647-54654
2004
Temas: Binding energy - Biochemistry - Immunology - Cytoplasm - Glucocorticoid receptors (GR) - Immunophilins - Steroids - Cells - cell protein - dynactin
Descripción: Rapid, ligand-dependent movement of glucocorticoid receptors (GR) from cytoplasm to the nucleus is hsp90-dependent, and much of the movement system has been defined. GR-hsp90 heterocomplexes isolated from cells contain one of several hsp90-binding immunophilins that link the complex to cytoplasmic dynein, a molecular motor that processes along microtubular tracks to the nucleus. The immunophilins link to dynein indirectly via the dynamitin component of the dynein-associated dynactin complex (Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) J. Biol. Chem. 279, 22483-22489). Although it is known that rapid, hsp90-dependent GR movement requires intact microtubules, it has not been shown that the movement is dynein-dependent. Here, we show that overexpression of dynamitin, which blocks movement by dissociating the dynein motor from its cargo, inhibits ligand-dependent movement of the GR to the nucleus. We show that native GR·hsp90·immnunophilin complexes contain dynamitin as well as dynein and that GR heterocomplexes isolated from cytosol containing paclitaxel and GTP to stabilize microtubules also contain tubulin. The complete movement system, including the dynein motor complex and tubulin, can be assembled under cell-free conditions by incubating GR immune pellets with paclitaxel/GTP-stabilized cytosol prepared from GR - L cells. This is the first evidence that the movement of a steroid receptor is dynein-dependent, and it is the first isolation of a steroid receptor bound to the entire system that determines its retrograde movement.
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Galigniana, M.D. - Morishima, Y. - Gallay, P.A. - Pratt, W.B.
J. Biol. Chem. 2004;279(53):55754-55759
2004
Temas: Cells - Cytology - Drug products - Immunology - Living systems studies - Molecular weight - Immunophilins - Microtubules - Prolyl isomerase - Protein trafficking
Descripción: Although cyclophilin A (CyP-A) is a relatively abundant small immunophilin present in the cytoplasm of all mammalian cells, its general function(s) in the absence of the immunosuppressant drug cyclosporin A is not known. In contrast, the high molecular weight hsp90-binding immunophilins appear to play a role in protein trafficking in that they have been shown to link glucocorticoid receptor-hsp90 and p53-hsp90 complexes to the dynein motor protein for retrograde movement along microtubules. These immunophilins link to cytoplasmic dynein indirectly through the association of the immunophilin peptidylprolyl isomerase (PPIase) domain with dynamitin, a component of the dynein-associated dynactin complex (Galigniana, M. D., Harrell, J. M., O'Hagen, H. M., Ljungman, M., and Pratt, W. B. (2004) J. Biol. Chem. 279, 22483-22489). Here, we show that CyP-A exists in native heterocomplexes containing cytoplasmic dynein that can be formed in cell-free systems. Prolyl isomerase activity is not required for forming the dynein complex, but the PPIase domain fragment of FKBP52 blocks complex formation and CyP-A binds to dynamitin in a PPIase domain-dependent manner. CyP-A heterocomplexes containing tubulin and dynein can be formed in cytosol prepared under microtubule-stabilizing conditions, and CyP-A colocalizes in mouse fibroblasts with microtubules. Colocalization with microtubules is disrupted by overexpression of the PPIase domain fragment. Thus, we conclude that CyP-A associates in vitro and in vivo with the dynein/dynactin motor protein complex and we suggest that CyP-A may perform a general function related to the binding of cargo for retrograde movement along microtubules.
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Thomas, M.G. - Luchelli, L. - Pascual, M. - Gottifredi, V. - Boccaccio, G.L.
PLoS ONE 2012;7(5)
2012
Temas: cell marker - cycloheximide - decapping enzyme 1a - decapping enzyme 1b - decapping enzyme 2 - epitope - exoribonuclease - exoribonuclease 1 - messenger RNA - monoclonal antibody
Descripción: The p53 tumor suppressor protein is an important regulator of cell proliferation and apoptosis. p53 can be found in the nucleus and in the cytosol, and the subcellular location is key to control p53 function. In this work, we found that a widely used monoclonal antibody against p53, termed Pab 1801 (Pan antibody 1801) yields a remarkable punctate signal in the cytoplasm of several cell lines of human origin. Surprisingly, these puncta were also observed in two independent p53-null cell lines. Moreover, the foci stained with the Pab 1801 were present in rat cells, although Pab 1801 recognizes an epitope that is not conserved in rodent p53. In contrast, the Pab 1801 nuclear staining corresponded to genuine p53, as it was upregulated by p53-stimulating drugs and absent in p53-null cells. We identified the Pab 1801 cytoplasmic puncta as P Bodies (PBs), which are involved in mRNA regulation. We found that, in several cell lines, including U2OS, WI38, SK-N-SH and HCT116, the Pab 1801 puncta strictly colocalize with PBs identified with specific antibodies against the PB components Hedls, Dcp1a, Xrn1 or Rck/p54. PBs are highly dynamic and accordingly, the Pab 1801 puncta vanished when PBs dissolved upon treatment with cycloheximide, a drug that causes polysome stabilization and PB disruption. In addition, the knockdown of specific PB components that affect PB integrity simultaneously caused PB dissolution and the disappearance of the Pab 1801 puncta. Our results reveal a strong cross-reactivity of the Pab 1801 with unknown PB component(s). This was observed upon distinct immunostaining protocols, thus meaning a major limitation on the use of this antibody for p53 imaging in the cytoplasm of most cell types of human or rodent origin. © 2012 Thomas et al.
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Panza, V. - Láinez, V. - Maldonado, S.
Bot. J. Linn. Soc. 2004;145(4):445-453
2004
Temas: Embryo - Minerals - Mitochondria - Palmito - Phytoferritin - Proteinbodies - Recalcitrance - Vacuole - cell organelle - embryo
Descripción: The Euterpe edulis embryo consists of a prominent single cotyledon, a very short radicle-hypocotyl axis and an epicotyl. The epicotyl is obliquely angled with respect to the cotyledon; consequently it corresponds to one of the two categories recognized for palm seeds by DeMason (1988). Parenchyma, protoderm and procambium can be distinguished on the basis of position and shape of their cells, which are highly vacuolated with one central vacuole and the cytoplasm restricted to a thin parietal layer. Initial cells from both apical meristems are also vacuolated but they have small vacuoles distributed around the nuclei. Silica occurs in cell walls of some protodermal cells. Raphides, silica bodies and tannins all occur occasionally in vacuoles, especially in the basal cotyledon region. Most embryo cells lack storage reserves and exhibit an active state, with numerous mitochondria, RER cisternae and Golgi apparatus, indicating a strategy of continuous development without the interposition, at maturity, of a dry state. The endosperm consists of living cells with very large nuclei and thickened cell walls. Similar to the endosperm of other studied palm species, their cells exhibit a quiescent appearance with lipid, protein, minerals (in the cytoplasm) and mannans (in the cell walls) as the insoluble storage reserves. © 2004 The Linnean Society of London.
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Acosta, E.G. - Castilla, V. - Damonte, E.B.
PLoS ONE 2012;7(9)
2012
Temas: ammonium chloride - chlorpromazine - clathrin - Rab protein - Rab7 protein - virus RNA - animal cell - article - cell migration - cellular distribution
Descripción: The entry of DENV into the host cell appears to be a very complex process which has been started to be studied in detail. In this report, the route of functional intracellular trafficking after endocytic uptake of dengue virus serotype 1 (DENV-1) strain HW, DENV-2 strain NGC and DENV-2 strain 16681 into Vero cells was studied by using a susceptibility to ammonium chloride assay, dominant negative mutants of several members of the family of cellular Rab GTPases that participate in regulation of transport through endosome vesicles and immunofluorescence colocalization. Together, the results presented demonstrate that in spite of the different internalization route among viral serotypes in Vero cells and regardless of the viral strain, DENV particles are first transported to early endosomes in a Rab5-dependent manner. Then a Rab7-dependent pathway guides DENV-2 16681 to late endosomes, whereas a yet unknown sorting event controls the transport of DENV-2 NGC, and most probably DENV-1 HW, to the perinuclear recycling compartments where fusion membrane would take place releasing nucleocapsid into the cytoplasm. Besides the demonstration of a different intracellular trafficking for two DENV-2 strains that shared the initial clathrin-independent internalization route, these studies proved for the first time the involvement of the slow recycling pathway for DENV-2 productive infection. © 2012 Acosta et al.
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Pallavicini, C. - Despósito, M.A. - Levi, V. - Bruno, L.
J. Phys. Conf. Ser. 2010;246
2010
Temas: Cytology - Anomalous diffusion - Cell cytoplasm - Function of time - Molecular motors - Spatio-temporal resolution - Tracking techniques - Turning angles - Xenopus laevis - Proteins
Descripción: The displacement of particles or probes in the cell cytoplasm as a function of time is characterized by different anomalous diffusion regimes. The transport of large cargoes, such as organelles, vesicles or large proteins, involves the action of ATP-consuming molecular motors. We investigate the motion of pigment organelles driven by myosin-V motors in Xenopus laevis melanocytes using a high spatio-temporal resolution tracking technique. By analyzing the turning angles (φ) of the obtained 2D trajectories as a function of the time lag, we determine the critical time of the transition between anticorrelated and directed motion as the time when the turning angles begin to concentrate around φ 0. We relate this transition with the crossover from subdiffusive to superdiffusive behavior observed in a previous work [5]. We also assayed the properties of the trajectories in cells with inhibited myosin activity, and we can compare the results in the presence and absence of active motors. © 2010 IOP Publishing Ltd.
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Brunstein, M. - Bruno, L. - Desposito, M. - Levi, V.
Biophys. J. 2009;97(6):1548-1557
2009
Temas: actin - molecular motor - myosin V - actin filament - active transport - animal cell - article - cell organelle - controlled study - diffusion
Descripción: The organization of the cytoplasm is regulated by molecular motors, which transport organelles and other cargoes along cytoskeleton tracks. In this work, we use single particle tracking to study the in vivo regulation of the transport driven by myosin-V along actin filaments in Xenopus laevis melanophores. Melanophores have pigment organelles or melanosomes, which, in response to hormones, disperse in the cytoplasm or aggregate in the perinuclear region. We followed the motion of melanosomes in cells treated to depolymerize microtubules during aggregation and dispersion, focusing the analysis on the dynamics of these organelles in a time window not explored before to our knowledge. These data could not be explained by previous models that only consider active transport. We proposed a transport-diffusion model in which melanosomes may detach from actin tracks and reattach to nearby filaments to resume the active motion after a given time of diffusion. This model predicts that organelles spend -70% and 10% of the total time in active transport during dispersion and aggregation, respectively. Our results suggest that the transport along actin filaments and the switching from actin to microtubule networks are regulated by changes in the diffusion time between periods of active motion driven by myosin-V. © 2009 by the Biophysical Society.
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Schwede, A. - Manful, T. - Jha, B.A. - Helbig, C. - Bercovich, N. - Stewart, M. - Clayton, C.
Nucleic Acids Res. 2009;37(16):5511-5528
2009
Temas: chromatin assembly factor 1 - gene product - messenger RNA - protein EP - ribosome protein - unclassified drug - EP procyclin protein, Trypanosoma brucei - membrane protein - mRNA deadenylase - phosphoglycerate kinase
Descripción: Removal of the poly(A) tail is the first step in the degradation of many eukaryotic mRNAs. In metazoans and yeast, the Ccr4/Caf1/Not complex has the predominant deadenylase activity, while the Pan2/Pan3 complex may trim poly(A) tails to the correct size, or initiate deadenylation. In trypanosomes, turnover of several constitutively-expressed or long-lived mRNAs is not affected by depletion of the 5'-3' exoribonuclease XRNA, but is almost completely inhibited by depletion of the deadenylase CAF1. In contrast, two highly unstable mRNAs, encoding EP procyclin and a phosphoglycerate kinase, PGKB, accumulate when XRNA levels are reduced. We here show that degradation of EP mRNA was partially inhibited after CAF1 depletion. RNAi-targeting trypanosome PAN2 had a mild effect on global deadenylation, and on degradation of a few mRNAs including EP. By amplifying and sequencing degradation intermediates, we demonstrated that a reduction in XRNA had no effect on degradation of a stable mRNA encoding a ribosomal protein, but caused accumulation of EP mRNA fragments that had lost substantial portions of the 5' and 3' ends. The results support a model in which trypanosome mRNAs can be degraded by at least two different, partially independent, cytoplasmic degradation pathways attacking both ends of the mRNA. © 2009 The Author(s).
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Landau, A.M. - Lokstein, H. - Scheller, H.V. - Lainez, V. - Maldonado, S. - Prina, A.R.
Plant Physiol. 2009;151(4):1802-1811
2009
Temas: messenger RNA - pigment - plant extract - vegetable protein - article - barley - chloroplast - cytoplasm - gene expression regulation - genetics
Descripción: A cytoplasmically inherited chlorophyll-deficient mutant of barley (Hordeum vulgare) termed cytoplasmic line 3 (CL3), displaying a viridis (homogeneously light-green colored) phenotype, has been previously shown to be affected by elevated temperatures. In this article, biochemical, biophysical, and molecular approaches were used to study the CL3 mutant under different temperature and light conditions. The results lead to the conclusion that an impaired assembly of photosystem I (PSI) under higher temperatures and certain light conditions is the primary cause of the CL3 phenotype. Compromised splicing of ycf3 transcripts, particularly at elevated temperature, resulting from a mutation in a noncoding region (intron 1) in the mutant ycf3 gene results in a defective synthesis of Ycf3, which is a chaperone involved in PSI assembly. The defective PSI assembly causes severe photoinhibition and degradation of PSII. © 2009 American Society of Plant Biologists.
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Quintá, H.R. - Maschi, D. - Gomez-Sanchez, C. - Piwien-Pilipuk, G. - Galigniana, M.D.
J. Neurochem. 2010;115(3):716-734
2010
Temas: Chaperones - FKBP - Hippocampus - P23 - Tau - Tetratricopeptide proteins - beta tubulin - beta3 tubulin - fk 506 binding protein - fk 506 binding protein 51
Descripción: FKBP51 and FKBP52 (FK506-binding protein 51 and 52) are tetratricopeptide repeat-domain immunophilins belonging to the tetratricopeptide- protein•hsp90•hsp70•p23 heterocomplex bound to steroid receptors. Immunophilins are related to receptor folding, subcellular localization, and hormonedependent transcription. Also, they bind the immunosuppressant macrolide FK506, which shows neuroregenerative and neuroprotective actions by a still unknown mechanism. In this study, we demonstrate that in both, undifferentiated neuroblastoma cells and embryonic hippocampal neurons, the FKBP52• hsp90•p23 heterocomplex concentrates in a perinuclear structure. Upon cell stimulation with FK506, this structure disassembles and this perinuclear area becomes transcriptionally active. The acquisition of a neuronal phenotype is accompanied by increased expression of bIII-tubulin, Map-2, Tau-1, but also hsp90, hsp70, p23, and FKBP52. During the early differentiation steps, the perinuclear heterocomplex redistributes along the cytoplasm and nascent neurites, p23 binds to intermediate filaments and microtubules acquired higher filamentary organization. While FKBP52 moves towards neurites and concentrates in arborization bodies and terminal axons, FKBP51, whose expression remains constant, replaces FKBP52 in the perinuclear structure. Importantly, neurite outgrowth is favored by FKBP52 over-expression or FKBP51 knock-down, and is impaired by FKBP52 knock-down or FKBP51 over-expression, indicating that the balance between these FK506-binding proteins plays a key role during the early mechanism of neuronal differentiation. © 2010 The Authors.
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Baez, M.V. - Boccaccio, G.L.
J. Biol. Chem. 2005;280(52):43131-43140
2005
Temas: Degradation - Genes - Proteins - RNA - Deadenylation - Gene expression - RNA-binding proteins - Cytology - messenger RNA - protein mSmaug 1
Descripción: Cytoplasmic events depending on RNA-binding proteins contribute to the fine-tuning of gene expression. Sterile α motif-containing RNA-binding proteins constitute a novel family of post-transcriptional regulators that recognize a specific RNA sequence motif known as Smaug recognition element (SRE). The Drosophila member of this family, dSmaug, triggers the translational repression and deadenylation of maternal mRNAs by independent mechanisms, and the yeast homologue Vts1 stimulates degradation of SRE-containing messengers. Two homologous genes are present in the mammalian genome. Here we showed that hSmaug 1, encoded in human chromosome 14, represses the translation of reporter transcripts carrying SRE motifs. When expressed in fibroblasts, hSmaug 1 forms cytoplasmic granules that contain polyadenylated mRNA and the RNA-binding proteins Staufen, TIAR, TIA-1, and HuR. Smaug 1 foci are distinct from degradation foci. The murine protein mSmaug 1 is expressed in the central nervous system and is abundant in post-synaptic densities, a subcellular region where translation is tightly regulated by synaptic stimulation. Biochemical analysis indicated that mSmaug 1 is present in synaptoneurosomal 20 S particles. These results suggest a role for mammalian Smaug 1 in RNA granule formation and translation regulation in neurons. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
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Vallejo, G. - Ballaré, C. - Barañao, J.L. - Beato, M. - Saragüeta, P.
Mol. Endocrinol. 2005;19(12):3023-3037
2005
Temas: estradiol - estrogen receptor beta - fulvestrant - gestagen - mifepristone - mitogen activated protein kinase 1 - mitogen activated protein kinase 3 - progesterone receptor - promegestone - animal cell
Descripción: Uterine decidualization is characterized by stromal cell proliferation and differentiation, which are controlled by ovarian hormones estradiol and progesterone. Here we report that the proliferative response of UIII rat uterine stromal cells to a short treatment with progestins requires active progesterone receptor (PR) and estrogen receptor β (ERβ) as well as a rapid and transient activation of Erk1-2 and Akt signaling. The optimal R5020 concentration for the proliferative response as well as for activation of the signaling cascades was between 10 and 100 pM. UIII cells are negative for ERα and have low levels of ERβ and PR located mainly in the cytoplasm. Upon progestin treatment PR translocated to the cell nucleus where it colocalized with activated Erk1-2. Neither progestins nor estradiol transactivated the corresponding transfected reporter genes, suggesting that endogenous PR and ERβ are transcriptionally incompetent. A fraction of endogenous PR and ERβ form a complex as demonstrated by coimmunoprecipitation. Taken together, our results suggest that the proliferative response of uterine stromal cells to picomolar concentrations of progestins does not require direct transcriptional effects and is mediated by activation of the Erk1-2 and Akt signaling pathways via cross talk between PR and ERβ. Copyright © 2005 by The Endocrine Society.
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Galigniana, M.D. - Erlejman, A.G. - Monte, M. - Gomez-Sanchez, C. - Piwien-Pilipuk, G.
Mol. Cell. Biol. 2010;30(5):1285-1298
2010
Temas: aldosterone - dynein adenosine triphosphatase - fk 506 binding protein - heat shock protein 90 - immunophilin - mineralocorticoid receptor - molecular motor - protein fkbp52 - tubulin - unclassified drug
Descripción: In this study, we demonstrate that the subcellular localization of the mineralocorticoid receptor (MR) is regulated by tetratricopeptide domain (TPR) proteins. The high-molecular-weight immunophilin (IMM) FKBP52 links the MR-hsp90 complex to dynein/dynactin motors favoring the cytoplasmic transport of MR to the nucleus. Replacement of this hsp90-binding IMM by FKBP51 or the TPR peptide favored the cytoplasmic localization of MR. The complete movement machinery, including dynein and tubulin, could be recovered from paclitaxel/GTP-stabilized cytosol and was fully reassembled on stripped MR immune pellets. The whole MR-hsp90-based heterocomplex was transiently recovered in the soluble fraction of the nucleus after 10 min of incubation with aldosterone. Moreover, cross-linked MR-hsp90 heterocomplexes accumulated in the nucleus in a hormone-dependent manner, demonstrating that the heterocomplex can pass undissociated through the nuclear pore. On the other hand, a peptide that comprises the DNA-binding domain of MR impaired the nuclear export of MR, suggesting the involvement of this domain in the process. This study represents the first report describing the entire molecular system that commands MR nucleocytoplasmic trafficking and proposes that the MR-hsp90-TPR protein heterocomplex is dissociated in the nucleus rather than in the cytoplasm. Copyright © 2010, American Society for Microbiology. All Rights Reserved.
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Dominguez, P.G. - Frankel, N. - Mazuch, J. - Balbo, I. - Iusem, N. - Fernie, A.R. - Carrari, F.
Plant Physiol. 2013;161(3):1486-1500
2013
Temas: abscisic acid - carbon - carrier protein - gibberellic acid - gibberellin - glucose - messenger RNA - phytohormone - vegetable protein - article
Descripción: Asr (for ABA, stress, ripening) genes are exclusively found in the genomes of higher plants, and the encoded proteins have been found localized both to the nucleus and cytoplasm. However, before the mechanisms underlying the activity of ASR proteins can be determined, the role of these proteins in planta should be deciphered. Results from this study suggest that ASR is positioned within the signaling cascade of interactions among glucose, abscisic acid, and gibberellins. Tobacco (Nicotiana tabacum) transgenic lines with reduced levels of ASR protein showed impaired glucose metabolism and altered abscisic acid and gibberellin levels. These changes were associated with dwarfism, reduced carbon dioxide assimilation, and accelerated leaf senescence as a consequence of a fine regulation exerted by ASR to the glucose metabolism. This regulation resulted in an impact on glucose signaling mediated by Hexokinase1 and Snf1-related kinase, which would subsequently have been responsible for photosynthesis, leaf senescence, and hormone level alterations. It thus can be postulated that ASR is not only involved in the control of hexose uptake in heterotrophic organs, as we have previously reported, but also in the control of carbon fixation by the leaves mediated by a similar mechanism. © 2013 American Society of Plant Biologists. All Rights Reserved.
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Boltovskoy, D. - Kogan, M. - Alder, V.A. - Mianzan, H.
J. Plankton Res. 2003;25(12):1551-1559
2003
Temas: estuary - geographical distribution - new record - new species - radiolaria - taxonomy - Rio de la Plata - South America - Nassellaria - Polycystinea
Descripción: Vertically stratified bottle plankton samples collected in the Río de La Plata estuary (Atlantic coast of South America at ∼35° S) and in coastal waters off Mar del Plata (∼38° S) in December 1999 and November 2001 yielded up to 394 live cells l-1 of a single new nassellarian species: Lophophaena rioplatensis n. sp. (family Plagoniidae). In estuarine waters, the species was recorded at salinities as low as 15.4 p.s.u.; densities in excess of 100 cells l-1 were found at salinities ranging from 16. 9 p.s.u. These extremely high concentrations (the highest ever reported in the literature), as well as the fact that >90% of the individuals recorded contain cytoplasm, indicate that these are self-sustaining populations which thrive in the estuary (and in nearshore coastal waters), probably due to plentiful dissolved silica and an abundant food supply. Lophophaena rioplatensis is the first polycystine brackish-water species described. This finding shows that radiolarian fossils are not unequivocally associated with open-ocean conditions, but may also be useful indicators of coastal and brackish estuarine paleoenvironments.
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Galati, B.G. - Monacci, F. - Gotelli, M.M. - Rosenfeldt, S.
Ann. Bot. 2007;99(4):755-763
2007
Temas: Invasive non-syncytial tapetum - Modiolastrum malvifolium - Orbicules - Peritapetal membrane - angiosperm - cytoplasm - developmental stage - invasive species - pollen - spore
Descripción: • Background and Aims: Although orbicular functions are still a matter of debate, they are considered by most authors to be exclusively formed by a secretory tapetum. However, the presence of orbicules on a peritapetal membrane associated with a plasmodial tapetum has been described for Abutilon pictum (Malvaceae) in a previous study. Thus, studies on other species of Malvaceae are necessary to corroborate the presence of such bodies in other members of the family. Pollen and microsporangium development of Modiolastrum malvifolium has been studied in this work. • Methods: Anthers at different stages of development were processed for transmission electron microscopy and light microscopy. Membranes and pollen walls resistant to acetolysis were isolated from whole anthers. • Key Results: Microspore tetrads have a tetrahedral arrangement. Pollen grains are shed at the bicellular stage. The tapetum is invasive, non-syncytial and a peritapetal membrane with orbicules is formed. • Conclusions: This is the first report of the presence of orbicules on a peritapetal membrane in a species with a tapetum of an invasive, non-syncytial type. Taking into consideration all the information on the subject, it can be concluded that the presence of orbicules is not a stable criterion to differentiate between a secretory or plasmodial, or intermediate invasive, non-syncytial tapetum. © The Author 2007. Published by Oxford University Press on behalf of the Annals of Botany Company. All rights reserved.
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Galigniana, M.D. - Harrell, J.M. - O'Hagen, H.M. - Ljungman, M. - Pratt, W.B.
J. Biol. Chem. 2004;279(21):22483-22489
2004
Temas: Dissociation - Mutagenesis - Polypeptides - Proteins - Sensitivity analysis - Thermal effects - Tumors - Microtubular tracks - Motor proteins - Immunology
Descripción: The tumor suppressor protein p53 is known to be transported to the nucleus along microtubular tracks by cytoplasmic dynein. However, the connection between p53 and the dynein motor protein complex has not been established. Here, we show that hsp90·binding immunophilins link p53·hsp90 complexes to dynein and that prevention of that linkage in vivo inhibits the nuclear movement of p53. First, we show that p53·hsp90 heterocomplexes from DLD-1 human colon cancer cells contain an immunophilin (FKBP52, CyP-40, or PP5) as well as dynein. p53·hsp90·immunophilin·dynein complexes can be formed by incubating immunopurified p53 with rabbit reticulocyte lysate, and we show by peptide competition that the immunophilins link via their tetratricopeptide repeat domains to p53-bound hsp90 and by means of their PPIase domains to the dynein complex. The linkage of immunophilins to the dynein motor is indirect by means of the dynamitin component of the dynein-associated dynactin complex, and we show that purified FKBP52 binds directly by means of its PPIase domain to purified dynamitin. By using a temperature-sensitive mutant of p53 where cytoplasmic-nuclear movement occurs by shift to permissive temperature, we show that p53 movement is impeded when p53 binding to hsp90 is inhibited by the hsp90 inhibitor radicicol. Also, nuclear movement of p53 is inhibited when immunophilin binding to dynein is competed for by expression of a PPIase domain fragment in the same manner as when dynein linkage to cargo is dissociated by expression of dynamitin. This is the first demonstration of the linkage between an hsp90-chaperoned transcription factor and the system for its retrograde movement to the nucleus both in vitro and in vivo.
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Abrahamyan, L.G. - Chatel-Chaix, L. - Ajamian, L. - Milev, M.P. - Monette, A. - Clément, J.-F. - Song, R. - Lehmann, M. - DesGroseillers, L. - Laughrea, M. - Boccaccio, G. - Mouland, A.J.
J. Cell Sci. 2010;123(3):369-383
2010
Temas: AIDS - HIV-1 - Intracellular traffic - Ribonucleoprotein - RNA encapsidation - SHRNP - sIRNA - Staufen1 - Staufen1 HIV-1-dependent RNP - Virus-host interaction
Descripción: Human immunodeficiency virus type 1 (HIV-1) Gag selects for and mediates genomic RNA (vRNA) encapsidation into progeny virus particles. The host protein, Staufen1 interacts directly with Gag and is found in ribonucleoprotein (RNP) complexes containing vRNA, which provides evidence that Staufen1 plays a role in vRNA selection and encapsidation. In this work, we show that Staufen1, vRNA and Gag are found in the same RNP complex. These cellular and viral factors also colocalize in cells and constitute novel Staufen1 RNPs (SHRNPs) whose assembly is strictly dependent on HIV-1 expression. SHRNPs are distinct from stress granules and processing bodies, are preferentially formed during oxidative stress and are found to be in equilibrium with translating polysomes. Moreover, SHRNPs are stable, and the association between Staufen1 and vRNA was found to be evident in these and other types of RNPs. We demonstrate that following Staufen1 depletion, apparent supraphysiologic-sized SHRNP foci are formed in the cytoplasm and in which Gag, vRNA and the residual Staufen1 accumulate. The depletion of Staufen1 resulted in reduced Gag levels and deregulated the assembly of newly synthesized virions, which were found to contain several-fold increases in vRNA, Staufen1 and other cellular proteins. This work provides new evidence that Staufen1-containing HIV-1 RNPs preferentially form over other cellular silencing foci and are involved in assembly, localization and encapsidation of vRNA.
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Ferrari, C.C. - Aldana Marcos, H.J. - Carmanchahi, P.D. - Affanni, J.M.
Anat. Rec. 1998;252(3):325-339
1998
Temas: Apocrine secretion - Apoptosis - Armadillo - Electron microscopy - Olfactory mucosa - Supporting cells - Xenarthra - animal tissue - armadillo - article
Descripción: The sense of olfaction in armadillos plays an important role, suggested by the great development of the nasal structures, olfactory bulbs, and related brain regions. The mammalian olfactory mucosa is a privileged site of neuronal death and regeneration during the whole life span. A detailed knowledge of its ultrastructure is convenient for gaining insight into the factors controlling those phenomena. We performed this work in species not previously studied in order to provide a firm basis for further research on those factors. No information is available on the histology and ultrastructure of the olfactory mucosa in the order Xenarthra to which armadillos belong. Samples from the endoturbinals of the armadillo Chaetophractus villosus were prepared for light and electron microscopic examination by the usual conventional means. The olfactory epithelium of Chaetophractus villosus shows the classical three types of cells: supporting cells, olfactory receptor neurons, and basal cells. The olfactory neurons and the basal cells were similar to that described in other species. Two different types of supporting cells are described. An outstanding characteristic of the supporting cells is the normal presence of abundant phagosomes, apical secretory granules, apocrine-like protrusions, and highly developed smooth endoplasmic reticulum. Apoptotic bodies are frequently found in the infranuclear cytoplasm of supporting cells. The ductular epithelium of Bowman's glands reveals secretory activity. The lamina propria shows mixed Bowman's glands. Great development of smooth endoplasmic reticulum is observed in the mucous acinar cells. Evidence for merocrine and apocrine mechanisms in the Bowman's glands is presented. The presence of apoptotic bodies and phagosomes in supporting cells suggests a participation in the cellular events induced by cell death and proliferation of the olfactory epithelium. The variety of characteristics exhibited by the supporting cells of the olfactory mucosa may contribute to a deeper understanding of their scarcely known functions.
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