Hamrita Bechr, Chahed Karim, Trimeche Mounir, Guillier Christelle Lemaitre, Hammann Philippe, Chaïeb Anouar, Korbi Sadok, Chouchane Lotfi
Proteomics-based identification of alpha1-antitrypsin and haptoglobin precursors as novel serum markers in infiltrating ductal breast carcinomas. Article de journal
Dans: Clinica chimica acta; international journal of clinical chemistry, vol. 404, no. 2, p. 111–118, 2009, ISSN: 1873-3492 0009-8981, (Place: Netherlands).
Résumé | Liens | BibTeX | Étiquettes: 80 and over, Adult, Aged, alpha 1-Antitrypsin/*blood, Amino Acid Sequence, Biomarkers, Breast Neoplasms/blood/*pathology, Carcinoma, Ductal/blood/*pathology, Electrophoresis, Female, Gel, Haptoglobins/*analysis, Humans, Mass, Matrix-Assisted Laser Desorption-Ionization, Middle Aged, Molecular Sequence Data, PPSE, Protein Isoforms/blood, proteomics, Spectrometry, Tumor/*blood, Two-Dimensional
@article{hamrita_proteomics-based_2009,
title = {Proteomics-based identification of alpha1-antitrypsin and haptoglobin precursors as novel serum markers in infiltrating ductal breast carcinomas.},
author = {Bechr Hamrita and Karim Chahed and Mounir Trimeche and Christelle Lemaitre Guillier and Philippe Hammann and Anouar Chaïeb and Sadok Korbi and Lotfi Chouchane},
doi = {10.1016/j.cca.2009.03.033},
issn = {1873-3492 0009-8981},
year = {2009},
date = {2009-06-01},
journal = {Clinica chimica acta; international journal of clinical chemistry},
volume = {404},
number = {2},
pages = {111--118},
abstract = {BACKGROUND: The identification of pathological markers of breast cancer for either diagnosis, treatment response or for survival is of critical importance. METHODS: Serum protein profiling using 2-DE separations coupled to matrix-assisted laser desorption ionization mass spectrometry has been used to explore protein alterations in patients with infiltrating ductal breast carcinomas (IDCA). Sera from 39 breast cancer patients and 40 healthy controls were selected for screening study using 2-DE combined with MS. The protein expression patterns obtained after the depletion of high abundance proteins was determined by coomassie blue G-250 stain after 2-DE electrophoresis. RESULTS: Six proteins that expressed differentially in the IDCA group were found. The expression levels of four isoforms corresponding to haptoglobin precursor and two isoforms of alpha1-antitrypsin precursor (alpha1-AT) were upregulated in sera from breast cancer patients. There was an increased expression of both proteins in the sera of patients with various tumor stages (I, II, III) in comparison to healthy women. Applying immunohistochemistry, we further validated alpha1-AT immunoreactivity in 51 formalin-fixed paraffin-embedded sections of breast tumors. Enhanced expression of alpha1-AT like activity has been found in IDCA breast tumors, as well as, in different histological types of breast cancer. No significant association has been found with lymph node occurrence, while in high tumor categories a tendency to an increased expression of alpha1-AT has been found, thereby suggesting a possible role of this protein in tumor growth. CONCLUSIONS: These proteins may constitute new and useful markers of breast cancer that offer a clue to a better understanding of inflammatory pathways and carcinogenesis events linked to breast cancer progression.},
note = {Place: Netherlands},
keywords = {80 and over, Adult, Aged, alpha 1-Antitrypsin/*blood, Amino Acid Sequence, Biomarkers, Breast Neoplasms/blood/*pathology, Carcinoma, Ductal/blood/*pathology, Electrophoresis, Female, Gel, Haptoglobins/*analysis, Humans, Mass, Matrix-Assisted Laser Desorption-Ionization, Middle Aged, Molecular Sequence Data, PPSE, Protein Isoforms/blood, proteomics, Spectrometry, Tumor/*blood, Two-Dimensional},
pubstate = {published},
tppubtype = {article}
}
Bringel Françoise, Hammann Philippe, Kugler Valérie, Arsène-Ploetze Florence
Dans: Microbiology (Reading, England), vol. 154, no. Pt 9, p. 2629–2640, 2008, ISSN: 1350-0872 1350-0872, (Place: England).
Résumé | Liens | BibTeX | Étiquettes: Arginine/*biosynthesis, Argininosuccinate Lyase/genetics, Bacterial, Bacterial Proteins/*genetics, Bacterial/genetics, Carbon Compounds, Carbon Dioxide/metabolism, Electrophoresis, Gel, Gene Expression Regulation, Genetic, IMP Dehydrogenase/genetics, Inorganic/*metabolism, Lactobacillus plantarum/enzymology/genetics/*metabolism, Mass, Matrix-Assisted Laser Desorption-Ionization, Nucleotides/*biosynthesis, Pentosyltransferases/*genetics, PPSE, proteomics, Repressor Proteins/*genetics, Reverse Transcriptase Polymerase Chain Reaction, RNA, Spectrometry, Transcription, Two-Dimensional
@article{bringel_lactobacillus_2008,
title = {Lactobacillus plantarum response to inorganic carbon concentrations: PyrR2-dependent and -independent transcription regulation of genes involved in arginine and nucleotide metabolism.},
author = {Françoise Bringel and Philippe Hammann and Valérie Kugler and Florence Arsène-Ploetze},
doi = {10.1099/mic.0.2008/018184-0},
issn = {1350-0872 1350-0872},
year = {2008},
date = {2008-09-01},
journal = {Microbiology (Reading, England)},
volume = {154},
number = {Pt 9},
pages = {2629--2640},
abstract = {Lactobacillus plantarum susbp. plantarum is a capnophilic Gram-positive heterotroph with optimal growth in 4 % CO(2)-enriched air. At low inorganic carbon (C(i)) concentrations, the pyr genes encoding the enzymes of the pyrimidine biosynthetic pathway were overexpressed, in agreement with a previous study showing that these genes are regulated at the transcription level in response to C(i) via a PyrR(2)-mediated mechanism. A previous study of high-CO(2)-requiring (HCR) mutants revealed an unknown genetic link between arginine regulation and C(i)-dependent nutritional needs. To better understand L. plantarum's adaptation to C(i) availability, additional C(i)-responsive genes were sought in the arginine biosynthetic pathway (arg and car genes) using slot-blot hybridization and a proteomic differential 2D gel electrophoresis (DIGE) global approach. Besides the nine pyr-encoded proteins, 16 new Icr (inorganic-carbon-regulated) proteins accumulated differentially in response to C(i) availability, suggesting that the C(i) response involves several metabolic pathways and adaptation processes. Among these Icr proteins only argininosuccinate lyase, encoded by argH, was involved in arginine biosynthesis. Three proteins involved in the purine biosynthetic pathway and nucleotide conversion, adenylate kinase (Adk), GMP synthase (GuaA), and IMP dehydrogenase (GuaB), accumulated differentially in response to changes in C(i) levels. Expression of the Icr protein-encoding genes argH and guaB was regulated at the transcription level or by RNA stability in response to C(i) availability, as previously demonstrated for the pyr genes. However, PyrR(2) was not essential for the C(i)-regulated transcription of argH and guaB, demonstrating that PyrR(2) modulates only a subset of C(i)-regulated genes. These results suggest that the C(i) response may involve at least two regulatory mechanisms in L. plantarum.},
note = {Place: England},
keywords = {Arginine/*biosynthesis, Argininosuccinate Lyase/genetics, Bacterial, Bacterial Proteins/*genetics, Bacterial/genetics, Carbon Compounds, Carbon Dioxide/metabolism, Electrophoresis, Gel, Gene Expression Regulation, Genetic, IMP Dehydrogenase/genetics, Inorganic/*metabolism, Lactobacillus plantarum/enzymology/genetics/*metabolism, Mass, Matrix-Assisted Laser Desorption-Ionization, Nucleotides/*biosynthesis, Pentosyltransferases/*genetics, PPSE, proteomics, Repressor Proteins/*genetics, Reverse Transcriptase Polymerase Chain Reaction, RNA, Spectrometry, Transcription, Two-Dimensional},
pubstate = {published},
tppubtype = {article}
}
Pochart P., Agoutin B., Fix C., Keith G., Heyman T.
A very poorly expressed tRNA(Ser) is highly concentrated together with replication primer initiator tRNA(Met) in the yeast Ty1 virus-like particles Article de journal
Dans: Nucleic Acids Res, vol. 21, no. 7, p. 1517-21, 1993, (0305-1048 Journal Article).
Résumé | BibTeX | Étiquettes: &, Acid, Base, cerevisiae/metabolism, Conformation, Data, development, DNA, Electrophoresis, Elements/*physiology, Gel, Met/metabolism, Molecular, Nucleic, Retroviridae/*growth, RNA, Saccharomyces, Sequence, Ser/*metabolism, Transfer, Transposable, Two-Dimensional, Viral/*metabolism
@article{,
title = {A very poorly expressed tRNA(Ser) is highly concentrated together with replication primer initiator tRNA(Met) in the yeast Ty1 virus-like particles},
author = { P. Pochart and B. Agoutin and C. Fix and G. Keith and T. Heyman},
year = {1993},
date = {1993-01-01},
journal = {Nucleic Acids Res},
volume = {21},
number = {7},
pages = {1517-21},
abstract = {The analysis of the tRNAs associated to the virus-like particles produced by the Ty1 element revealed the specific packaging of three major tRNA species, in about equal amounts: the replication primer initiator tRNA(Met), the tRNA(Ser)AGA and a tRNA undetected until now as an expressed species in yeast. The latter tRNA is coded by the already described tDNA(Ser)GCT. This tRNA is enriched more than 150 fold in the particles as compared to its content in total cellular tRNA where it represents less than 0.1% (initiator tRNA(Met) and tRNA(Ser)AGA being 11 and 4 fold enriched respectively). This tRNA is the only species coded by the tDNA(Ser)GCT gene which is found in three copies per genome since no other corresponding expressed tRNA could be detected. This gene is thus very poorly expressed. The high concentration of tRNA(Ser)GCU in the particles compared to its very low cellular content led us to consider its possible implication in Ty specific processes.},
note = {0305-1048
Journal Article},
keywords = {&, Acid, Base, cerevisiae/metabolism, Conformation, Data, development, DNA, Electrophoresis, Elements/*physiology, Gel, Met/metabolism, Molecular, Nucleic, Retroviridae/*growth, RNA, Saccharomyces, Sequence, Ser/*metabolism, Transfer, Transposable, Two-Dimensional, Viral/*metabolism},
pubstate = {published},
tppubtype = {article}
}
Nothwang H. G., Coux O., Keith G., Silva-Pereira I., Scherrer K.
The major RNA in prosomes of HeLa cells and duck erythroblasts is tRNA(Lys,3) Article de journal
Dans: Nucleic Acids Res, vol. 20, no. 8, p. 1959-65, 1992, (0305-1048 Journal Article).
Résumé | BibTeX | Étiquettes: Animals, Base, Blotting, Cells, Data, Ducks, effects, Electrophoresis, Erythroblasts, Gel, Gov't, Hela, Human, Lys/*analysis/metabolism, Molecular, Non-U.S., Northern, Nucleotidyltransferases/metabolism, Ribonucleoproteins/*chemistry/drug, RNA, Sequence, Support, Transfer, Two-Dimensional, Zinc/pharmacology
@article{,
title = {The major RNA in prosomes of HeLa cells and duck erythroblasts is tRNA(Lys,3)},
author = { H. G. Nothwang and O. Coux and G. Keith and I. Silva-Pereira and K. Scherrer},
year = {1992},
date = {1992-01-01},
journal = {Nucleic Acids Res},
volume = {20},
number = {8},
pages = {1959-65},
abstract = {Two-dimensional gel electrophoresis of HeLa cell prosomal RNAs, 3'-end labeled by RNA ligase, revealed one prominent spot. Determination of a partial sequence at the 3'-end indicated full homology to the 18 nucleotides at the 3'-end of tRNA(Lys,3) from rabbit, the bovine and the human species. An oligonucleotide complementary to the 3'-end of tRNA(Lys,3) hybridized on Northern blots with prosomal RNA from both HeLa cells and duck erythroblasts. In two-dimensional PAGE, the major pRNA of HeLa cells co-migrated with bovine tRNA(Lys,3). Reconstitution of the CCA 3'-end of RNA from both human and duck prosomes, by tRNA-nucleotidyl-transferase, confirmed the tRNA character of this type of RNA. Furthermore, it revealed at least one additional tRNA band about 85 nt long among the prosomal RNA from both species. Finally, confirming an original property of prosomal RNA, we show that in vitro synthesized tRNA(Lys,3) hybridizes stably to duck globin mRNA, and to poly(A)(+)- and poly(A)(-)-RNA from HeLa cells.},
note = {0305-1048
Journal Article},
keywords = {Animals, Base, Blotting, Cells, Data, Ducks, effects, Electrophoresis, Erythroblasts, Gel, Gov't, Hela, Human, Lys/*analysis/metabolism, Molecular, Non-U.S., Northern, Nucleotidyltransferases/metabolism, Ribonucleoproteins/*chemistry/drug, RNA, Sequence, Support, Transfer, Two-Dimensional, Zinc/pharmacology},
pubstate = {published},
tppubtype = {article}
}