Acute ammonia neurotoxicity in vivo involves increase in cytoplasmic protein P53 without alterations in other markers of apoptosis

2007 ◽  
Vol 85 (11) ◽  
pp. 2491-2499 ◽  
Author(s):  
Elena Kosenko ◽  
Yuri Kaminsky ◽  
Ilia Solomadin ◽  
Nikolay Marov ◽  
Natalia Venediktova ◽  
...  
Keyword(s):  
Cytoplasmic Protein ◽  
Protein P53 ◽  
Ammonia Neurotoxicity

Acute ammonia neurotoxicity in vivo involves the increase in cytoplasmic protein P53 without alterations in other markers of apoptosis

Mitochondrion ◽  
2006 ◽  
Vol 6 (5) ◽  
pp. 1-2
Author(s):  
N.I. Venedikotova ◽  
E. Kosenko ◽  
Y. Kaminsky ◽  
C. Montoliu ◽  
V. Felipo
Keyword(s):  
Cytoplasmic Protein ◽  
Protein P53 ◽  
Ammonia Neurotoxicity

FRACTIONAL PROTEIN SYNTHESIS RATES IN VIVO OF CONTRACTILE AND CYTOPLASMIC PROTEIN FRACTIONS OF SKELETAL MUSCLE IN THE SEPTIC RAT.

Shock ◽  
1999 ◽  
Vol 12 (Supplement) ◽  
pp. 54-55
Author(s):  
C. Ferguson ◽  
J. Coakley ◽  
M. Koll ◽  
C. J. Hinds ◽  
M. OʼLeary ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Protein Fractions ◽  
Cytoplasmic Protein

scholarly journals Tyrosine phosphorylation of BCR by FPS/FES protein-tyrosine kinases induces association of BCR with GRB-2/SOS.

1995 ◽  
Vol 15 (2) ◽  
pp. 835-842 ◽  
Author(s):  
Y Maru ◽  
K L Peters ◽  
D E Afar ◽  
M Shibuya ◽  
O N Witte ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Kinase ◽  
Sh2 Domain ◽  
Binding Domain ◽  
Ras Signaling ◽  
Cytoplasmic Protein ◽  
Nucleotide Exchange ◽  
Protein Tyrosine

The human bcr gene encodes a protein with serine/threonine kinase activity, CDC24/dbl homology, a GAP domain, and an SH2-binding region. However, the precise physiological functions of BCR are unknown. Coexpression of BCR with the cytoplasmic protein-tyrosine kinase encoded by the c-fes proto-oncogene in Sf-9 cells resulted in stable BCR-FES protein complex formation and tyrosine phosphorylation of BCR. Association involves the SH2 domain of FES and a novel binding domain localized to the first 347 amino acids of the FES N-terminal region. Deletion of the homologous N-terminal BCR-binding domain from v-fps, a fes-related transforming oncogene, abolished transforming activity and tyrosine phosphorylation of BCR in vivo. Tyrosine phosphorylation of BCR in v-fps-transformed cells induced its association with GRB-2/SOS, the RAS guanine nucleotide exchange factor complex. These data provide evidence that BCR couples the cytoplasmic protein-tyrosine kinase and RAS signaling pathways.

Arabidopsis At2g40730 encodes a cytoplasmic protein involved in nuclear tRNA export

Botany ◽  
2011 ◽  
Vol 89 (3) ◽  
pp. 175-190 ◽  
Author(s):  
Aaron D. Johnstone ◽  
Robert T. Mullen ◽  
Dev Mangroo
Keyword(s):  
Nuclear Export ◽  
Cell Cycle Progression ◽  
Nuclear Pore ◽  
Cytoplasmic Protein ◽  
Cycle Progression ◽  
Cellular Processes ◽  
Gtpase Ran ◽  
Cytoplasmic Side

Nuclear tRNA export plays an essential role in several key cellular processes, such as regulation of protein synthesis, cell cycle progression, response to nutrient availability and DNA damage, and development. While the overall mechanism of nuclear tRNA export is, in general, poorly understood, the details of specific steps are emerging from studies conducted in different organisms aimed at identifying and characterizing components involved in the process. Here, we report that Arabidopsis thaliana (L.) Heynh At2g40730 encodes CTEXP, a cytoplasmic protein component of the nuclear tRNA export process. CTEXP bound tRNA directly and saturably, and like the nuclear tRNA export receptor PAUSED, overexpression of CTEXP restored export of a nuclear export-defective lysine amber suppressor tRNA in tobacco cells. CTEXP was also found to associate with nucleoporins of the nuclear pore complex (NPC), PAUSED, and the GTPase Ran in vivo. CTEXP interacted directly with PAUSED in vitro and RanGTP, but not RanGDP. Furthermore, a portion of CTEXP appeared to associate with the NPC. Taken together, the data suggest that CTEXP assists with unloading of tRNAs from PAUSED at the cytoplasmic side of the NPC in plant cells.

scholarly journals Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

2015 ◽  
Vol 197 (19) ◽  
pp. 3216-3227 ◽  
Author(s):  
Sao-Mai Nguyen-Mau ◽  
So-Young Oh ◽  
Daphne I. Schneewind ◽  
Dominique Missiakas ◽  
Olaf Schneewind
Keyword(s):  
Bacillus Anthracis ◽  
Self Assembly ◽  
Protein Assembly ◽  
Crystalline Lattice ◽  
Cell Wall Polysaccharide ◽  
Cytoplasmic Protein ◽  
Content Type ◽  
Bacterial Surface

ABSTRACTBacillus anthracisvegetative forms assemble an S-layer comprised of two S-layer proteins, Sap and EA1. A hallmark of S-layer proteins are their C-terminal crystallization domains, which assemble into a crystalline lattice once these polypeptides are deposited on the bacterial surface via association between their N-terminal S-layer homology domains and the secondary cell wall polysaccharide. Here we show thatslaQ, encoding a small cytoplasmic protein conserved among pathogenic bacilli elaborating S-layers, is required for the efficient secretion and assembly of Sap and EA1. S-layer protein precursors cosediment with SlaQ, and SlaQ appears to facilitate Sap assembly. Purified SlaQ polymerizes and when mixed with purified Sap promotes thein vitroformation of tubular S-layer structures. A model is discussed whereby SlaQ, in conjunction with S-layer secretion factors SecA2 and SlaP, promotes localized secretion and S-layer assembly inB. anthracis.IMPORTANCES-layer proteins are endowed with the propensity for self-assembly into crystalline arrays. Factors promoting S-layer protein assembly have heretofore not been reported. We identifiedBacillus anthracisSlaQ, a small cytoplasmic protein that facilitates S-layer protein assemblyin vivoandin vitro.

Enzyme induction in rat liver: The effects of Be2+in vivo

1981 ◽  
Vol 1 (3) ◽  
pp. 217-222 ◽  
Author(s):  
Margery G. Ord ◽  
Lloyd A. Stocken
Keyword(s):  
Protein Kinase ◽  
Rat Liver ◽  
Enzyme Induction ◽  
Orotic Acid ◽  
Tyrosine Aminotransferase ◽  
Cytoplasmic Protein ◽  
Ribonucleoprotein Particles ◽  
Liver Nuclei

Rats given an LD50 dose of Be2+ showed reduced activities of ornithine decarboxytase and tyrosine aminotransferase in liver in response to dexamethasone induction. Control fed animals showed ‘superinduction’. Be2+ also inhibited the uptake of [3H]orotic acid into rapidly labelled RNA of ribonucleoprotein particles extracted from liver nuclei in isomolar solutions at pH 8.0. Consistent with inhibition of cytoplasmic protein kinase reported previously (Kaser et at., 1980), the uptake of [32P]Pi into proteins in the ribonucleoprotein particles was also diminished.

Differentiation between mitochondrial and cytoplasmic protein subunits of blowfly flight muscle mitochondria synthesized in vivo

1981 ◽  
Vol 50 (1) ◽  
pp. 377-390
Author(s):  
M.B. Ashour ◽  
M. Tribe
Keyword(s):  
Gel Electrophoresis ◽  
Flight Muscle ◽  
Polyacrylamide Gel Electrophoresis ◽  
Mitochondrial Protein ◽  
Cytoplasmic Protein ◽  
Protein Subunits ◽  
Molecular Weights ◽  
And Function ◽  
Made In

Total adult blowfly flight-muscle mitochondrial protein was labelled in vivo with [14C]leucine. The labelled proteins were enumerated and characterized by their electrophoretic mobility using sodium dodcecyl sulphate/polyacrylamide gel electrophoresis and autoradiography. When different gel concentrations were used to resolve the maximum number of bands and their molecular weights, it was possible to observe at least 35 electrophoretic bands after staining and scanning; their molecular weights ranged between 11 000 and 130 000. When mitochondria were labelled in the presence of cycloheximide, only 6–8 bands could be identified on gradient gels after electrophoresis and autoradiography. By comparison, controls (where cycloheximide was absent), which were run alongside the drug-treated mitochondria, revealed 17–20 radioactively labelled bands from densitometric tracings. Whilst the molecular weights of these bands could be estimated, it was difficult to identify the precise nature and function of the proteins made in these mitochondria.

scholarly journals PENINGKATAN EKSPRESI p53 OLEH EKSTRAK ETANOLIK RUMPUT MUTIARA (Hedyotis corymbosa) PADA SEL HEPAR TIKUS SPRAGUE DAWLEY TERINDUKSI 7,12-DIMETILBENZ[a]ANTRASENA

2015 ◽  
Vol 11 (1) ◽  
pp. 1-6
Author(s):  
Edy Meiyanto
Keyword(s):  
Tunel Assay ◽  
Sprague Dawley ◽  
Protein P53

Asam ursolat dan asam oleanolat yang terdapat dalam Rumput Mutiara (Hedyotis corymbosa) diduga dapat menghambat kanker dengan berbagai mekanisme. Penelitian ini dirancang untuk mengetahui kemampuan ekstrak etanolik rumput mutiara sebagai agen pemacu apoptosis melalui uji in vivo menggunakan tikus galur Sprague Dawley terinduksi 7,12-dimetilbenz[a]antrasena (DMBA). Kelompok hewan uji yang digunakan terdiri dari kontrol ekstrak 1500mg/kgBB, kontrol pelarut CMC-Na, kontrol DMBA, perlakuan DMBA+ekstrak dosis 750mg/kgBB dan perlakuan DMBA+ekstrak 1500mg/kgBB. Hasil percobaan selanjutnya dianalisis menggunakan metode TUNEL (TUNEL assay) dan Imunohistokimia terhadap ekspresi protein p53 untuk mengetahui tingkat pemacuan apoptosis dari sel kanker hepar hewan uji. Hasil analisa menggunakan metode TUNEL menunjukkan hasil bahwa hepar tikus mengalami apoptosis relatif tinggi pada kelompok perlakuan DMBA+ekstrak. Hasil pengamatan menggunakan metode Imunohistokimia diketahui bahwa sel kanker hepar mengalami pemacuan ekspresi protein p53 yang menunjukkan terjadinya apoptosis pada sel hepar tersebut. Hal ini menunjukkan bahwa ekstrak rumput mutiara dapat memacu apoptosis dan dapat digunakan sebagai salah satu alternatif pengobatan penyakit kanker. Kata Kunci: H.corymbosa, DMBA, apoptosis, p53, TUNEL

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