michel soulard - Academia.edu (original) (raw)

Papers by michel soulard

Research paper thumbnail of Evaluation of the analytical performances of the Cobas c513 analyser for HbA1c assay

Biochemia Medica, Oct 15, 2018

Introduction: Haemoglobin A 1c (HbA 1c) is considered to be the gold standard for the follow-up o... more Introduction: Haemoglobin A 1c (HbA 1c) is considered to be the gold standard for the follow-up of glycaemic control in patients with diabetes mellitus and is also a diagnostic tool. Accordingly, reliable and efficient methods must be used for its quantification. Roche Diagnostics have recently adapted the Tina-quant® HbA 1c Third Generation immunoassay on a fully dedicated analyser, the Cobas c513, which allows a high throughput of up to 400 samples per hour. The present article deals with the evaluation of the analytical performances of this system which has been recently introduced to the market. Materials and methods: Precision, comparison with two ion-exchange high-performance liquid chromatography (HPLC) methods (Variant II and D-100 systems, BioRad Laboratories) using Passing Bablok and Bland-Altman analyses, accuracy and interference of the most frequent haemoglobin (Hb) variants on HbA 1c measurement were evaluated. Results: Precision was high, with coefficients of variation lower than 1.1% (HbA 1c values expressed in National Glycohemoglobin Standardization Program units, 1.7% for values expressed in International Federation of Clinical Chemistry and Laboratory Medicine [IFCC] units). The comparison study showed similar results with the two HPLC systems. The analysis of samples with IFCC-assigned values showed high methodological accuracy. Finally, no interference of bilirubin, triglycerides and common Hb variants (Hb AC, AD, AE, AS) was observed. Conclusions: This evaluation showed that the analytical performance of the Cobas c513 analyser for HbA 1c assay makes it suitable for a routine use in clinical chemistry laboratories.

Research paper thumbnail of Platelet Counting: Ugly Traps and Good Advice. Proposals from the French-Speaking Cellular Hematology Group (GFHC)

Journal of Clinical Medicine, 2020

Despite the ongoing development of automated hematology analyzers to optimize complete blood coun... more Despite the ongoing development of automated hematology analyzers to optimize complete blood count results, platelet count still suffers from pre-analytical or analytical pitfalls, including EDTA-induced pseudothrombocytopenia. Although most of these interferences are widely known, laboratory practices remain highly heterogeneous. In order to harmonize and standardize cellular hematology practices, the French-speaking Cellular Hematology Group (GFHC) wants to focus on interferences that could affect the platelet count and to detail the verification steps with minimal recommendations, taking into account the different technologies employed nowadays. The conclusions of the GFHC presented here met with a "strong professional agreement" and are explained with their rationale to define the course of actions, in case thrombocytopenia or thrombocytosis is detected. They are proposed as minimum recommendations to be used by each specialist in laboratory medicine who remains free t...

Research paper thumbnail of hnRNP G: sequence and characterization of a glycosylated RNA-binding protein

Nucleic Acids Research, 1993

The autoantlgen p43 is a nuclear protein initially identified with autoantibodles from dogs with ... more The autoantlgen p43 is a nuclear protein initially identified with autoantibodles from dogs with a lupuslike syndrome. Here we show that p43 Is an RNAblnding protein, and identify it as hnRNP G, a previously described component of heterogeneous nuclear ribonucleoproteln complexes. We demonstrate that p43/hnRNP G Is glycosylated, and identify the modification as O-linked N-acetylglucosamine. A fulllength cDNA clone for hnRNP G has been isolated and sequenced, and the predicted amlno acid sequence for hnRNP G shows that It contains one RNP-consensus RNA binding domain (RBD) at the amlno terminus and a carboxyl domain rich In serines, arglnines and glyclnes. The RBD of human hnRNP G shows striking similarities with the RBDs of several plant RNA-blndlng proteins. MATERIALS AND METHODS Cell cultures, labeling and cell fractionation HeLa S3 cells were grown in agitated suspension as previously described (38). They were labeled for 48 hrs with 11/ic/ml of 6-[ 3 H]glucosamine (specific activity: 0.37-l.llTBl/mM; Centre Energie Atomique, Saclay, France). HeLa cells were labeled with 20/xCi of [ 35 S]methionine per ml for 20hrs in Dulbecco's modified Eagle's medium (DMEM) containing '/ 10 the normal methionine levels and 5% calf thymus. Preparation of cell extracts and immunoprecipitation procedure Cell fractionation, immunoprecipitation and Western blotting of nuclear extracts were as previously reported (38). Immunopurification of hnRNP complexes with the anti-C proteins monoclonal

Research paper thumbnail of Localization of the human gene encoding heterogeneous nuclear RNA ribonucleoprotein G (hnRNP-G) to chromosome 6p12

Human Genetics, 1992

The gene encoding nuclear RNA ribonucleoprotein G (hnRNP-G), a p43 glycoprotein, has been mapped ... more The gene encoding nuclear RNA ribonucleoprotein G (hnRNP-G), a p43 glycoprotein, has been mapped to human chromosome 6, band p12, by radioactive in situ hybridization.

Research paper thumbnail of Dual localization of the human gene encoding hnRNP I/PTB protein to chromosomes 19p13.3 and 14q23

Human Genetics, 1996

A cDNA probe representative of the human hnRNP I/PTB gene was used to perform fluorescence in sit... more A cDNA probe representative of the human hnRNP I/PTB gene was used to perform fluorescence in situ hybridization (FISH) on metaphases of human chromosomes. A new localization was found on band 19p13.3 in addition to the previously reported localization to band 14q23. Identical results were obtained when FISH analysis was repeated with probes covering different parts of the hnRNP I cDNA clone. This supported the notion that most, if not all, of the sequences of the different parts of this clone are present on both chromosomes. Moreover, Southern blot analysis of DNAs from interspecies somatic hybrids containing chromosomes 19 and 14 revealed that the whole hnRNP I cDNA probe generated very similar patterns in each hybrid DNA. These data suggest that two closely related copies of the hnRNP I gene exist in the human genome.

Research paper thumbnail of Nucleolar proteins identified in human cells as antigens by sera from dogs with autoimmune disorders

Experimental Cell Research, 1989

In the course of a systematic screening of sera from dogs suffering from autoimmune disorders, th... more In the course of a systematic screening of sera from dogs suffering from autoimmune disorders, three sera were shown by indirect immunofluorescence to characteristically label the nucleoli and nucleoplasm of human cell lines (Hep-2 and HeLa). This pattern of staining persisted throughout the cell cycle, except for mitosis when the fluorescence was localized in extrachromosomal areas. By immunoblotting nuclear and subnuclear fractions, three polypeptides of 110,000, 95,000, and 45,000 Da apparent molecular weight were identified, which reacted with all three sera. By means of aftinity purification, it was shown that an antibody specific for any one of the three proteins also reacts with the two others. This antigenic cross-reactivity suggested regions of structural homology shared by the three proteins. Indeed, treatment of nucleoli with high concentrations of DNase I containing residual proteolytic activity resulted in the disappearance of the llO-and 95-kDa proteins and the concomitant appearance of a doublet of 45-kDa proteins. Subnuclear localization studies indicated that all three polypeptides were located in both nucleoli and nucleoplasm. Significantly, the llO-kDa protein differs from the major nucleolar protein, nucleolin, by its electrophoretic mobility in two-dimensional gels, its location in nucleoli and in nucleoplasm, its absence in nucleolar organizer regions of chromosomes, and its differential solubihty of DNase I. Therefore, the three antigenically related species reported in this study constitute a new class of nucleolar proteins. @ 1989 Academic press, IN.

Research paper thumbnail of Evaluation of the analytical performances of the Cobas c513 analyser for HbA1c assay

Biochemia Medica, Oct 15, 2018

Introduction: Haemoglobin A 1c (HbA 1c) is considered to be the gold standard for the follow-up o... more Introduction: Haemoglobin A 1c (HbA 1c) is considered to be the gold standard for the follow-up of glycaemic control in patients with diabetes mellitus and is also a diagnostic tool. Accordingly, reliable and efficient methods must be used for its quantification. Roche Diagnostics have recently adapted the Tina-quant® HbA 1c Third Generation immunoassay on a fully dedicated analyser, the Cobas c513, which allows a high throughput of up to 400 samples per hour. The present article deals with the evaluation of the analytical performances of this system which has been recently introduced to the market. Materials and methods: Precision, comparison with two ion-exchange high-performance liquid chromatography (HPLC) methods (Variant II and D-100 systems, BioRad Laboratories) using Passing Bablok and Bland-Altman analyses, accuracy and interference of the most frequent haemoglobin (Hb) variants on HbA 1c measurement were evaluated. Results: Precision was high, with coefficients of variation lower than 1.1% (HbA 1c values expressed in National Glycohemoglobin Standardization Program units, 1.7% for values expressed in International Federation of Clinical Chemistry and Laboratory Medicine [IFCC] units). The comparison study showed similar results with the two HPLC systems. The analysis of samples with IFCC-assigned values showed high methodological accuracy. Finally, no interference of bilirubin, triglycerides and common Hb variants (Hb AC, AD, AE, AS) was observed. Conclusions: This evaluation showed that the analytical performance of the Cobas c513 analyser for HbA 1c assay makes it suitable for a routine use in clinical chemistry laboratories.

Research paper thumbnail of Platelet Counting: Ugly Traps and Good Advice. Proposals from the French-Speaking Cellular Hematology Group (GFHC)

Journal of Clinical Medicine, 2020

Despite the ongoing development of automated hematology analyzers to optimize complete blood coun... more Despite the ongoing development of automated hematology analyzers to optimize complete blood count results, platelet count still suffers from pre-analytical or analytical pitfalls, including EDTA-induced pseudothrombocytopenia. Although most of these interferences are widely known, laboratory practices remain highly heterogeneous. In order to harmonize and standardize cellular hematology practices, the French-speaking Cellular Hematology Group (GFHC) wants to focus on interferences that could affect the platelet count and to detail the verification steps with minimal recommendations, taking into account the different technologies employed nowadays. The conclusions of the GFHC presented here met with a "strong professional agreement" and are explained with their rationale to define the course of actions, in case thrombocytopenia or thrombocytosis is detected. They are proposed as minimum recommendations to be used by each specialist in laboratory medicine who remains free t...

Research paper thumbnail of hnRNP G: sequence and characterization of a glycosylated RNA-binding protein

Nucleic Acids Research, 1993

The autoantlgen p43 is a nuclear protein initially identified with autoantibodles from dogs with ... more The autoantlgen p43 is a nuclear protein initially identified with autoantibodles from dogs with a lupuslike syndrome. Here we show that p43 Is an RNAblnding protein, and identify it as hnRNP G, a previously described component of heterogeneous nuclear ribonucleoproteln complexes. We demonstrate that p43/hnRNP G Is glycosylated, and identify the modification as O-linked N-acetylglucosamine. A fulllength cDNA clone for hnRNP G has been isolated and sequenced, and the predicted amlno acid sequence for hnRNP G shows that It contains one RNP-consensus RNA binding domain (RBD) at the amlno terminus and a carboxyl domain rich In serines, arglnines and glyclnes. The RBD of human hnRNP G shows striking similarities with the RBDs of several plant RNA-blndlng proteins. MATERIALS AND METHODS Cell cultures, labeling and cell fractionation HeLa S3 cells were grown in agitated suspension as previously described (38). They were labeled for 48 hrs with 11/ic/ml of 6-[ 3 H]glucosamine (specific activity: 0.37-l.llTBl/mM; Centre Energie Atomique, Saclay, France). HeLa cells were labeled with 20/xCi of [ 35 S]methionine per ml for 20hrs in Dulbecco's modified Eagle's medium (DMEM) containing '/ 10 the normal methionine levels and 5% calf thymus. Preparation of cell extracts and immunoprecipitation procedure Cell fractionation, immunoprecipitation and Western blotting of nuclear extracts were as previously reported (38). Immunopurification of hnRNP complexes with the anti-C proteins monoclonal

Research paper thumbnail of Localization of the human gene encoding heterogeneous nuclear RNA ribonucleoprotein G (hnRNP-G) to chromosome 6p12

Human Genetics, 1992

The gene encoding nuclear RNA ribonucleoprotein G (hnRNP-G), a p43 glycoprotein, has been mapped ... more The gene encoding nuclear RNA ribonucleoprotein G (hnRNP-G), a p43 glycoprotein, has been mapped to human chromosome 6, band p12, by radioactive in situ hybridization.

Research paper thumbnail of Dual localization of the human gene encoding hnRNP I/PTB protein to chromosomes 19p13.3 and 14q23

Human Genetics, 1996

A cDNA probe representative of the human hnRNP I/PTB gene was used to perform fluorescence in sit... more A cDNA probe representative of the human hnRNP I/PTB gene was used to perform fluorescence in situ hybridization (FISH) on metaphases of human chromosomes. A new localization was found on band 19p13.3 in addition to the previously reported localization to band 14q23. Identical results were obtained when FISH analysis was repeated with probes covering different parts of the hnRNP I cDNA clone. This supported the notion that most, if not all, of the sequences of the different parts of this clone are present on both chromosomes. Moreover, Southern blot analysis of DNAs from interspecies somatic hybrids containing chromosomes 19 and 14 revealed that the whole hnRNP I cDNA probe generated very similar patterns in each hybrid DNA. These data suggest that two closely related copies of the hnRNP I gene exist in the human genome.

Research paper thumbnail of Nucleolar proteins identified in human cells as antigens by sera from dogs with autoimmune disorders

Experimental Cell Research, 1989

In the course of a systematic screening of sera from dogs suffering from autoimmune disorders, th... more In the course of a systematic screening of sera from dogs suffering from autoimmune disorders, three sera were shown by indirect immunofluorescence to characteristically label the nucleoli and nucleoplasm of human cell lines (Hep-2 and HeLa). This pattern of staining persisted throughout the cell cycle, except for mitosis when the fluorescence was localized in extrachromosomal areas. By immunoblotting nuclear and subnuclear fractions, three polypeptides of 110,000, 95,000, and 45,000 Da apparent molecular weight were identified, which reacted with all three sera. By means of aftinity purification, it was shown that an antibody specific for any one of the three proteins also reacts with the two others. This antigenic cross-reactivity suggested regions of structural homology shared by the three proteins. Indeed, treatment of nucleoli with high concentrations of DNase I containing residual proteolytic activity resulted in the disappearance of the llO-and 95-kDa proteins and the concomitant appearance of a doublet of 45-kDa proteins. Subnuclear localization studies indicated that all three polypeptides were located in both nucleoli and nucleoplasm. Significantly, the llO-kDa protein differs from the major nucleolar protein, nucleolin, by its electrophoretic mobility in two-dimensional gels, its location in nucleoli and in nucleoplasm, its absence in nucleolar organizer regions of chromosomes, and its differential solubihty of DNase I. Therefore, the three antigenically related species reported in this study constitute a new class of nucleolar proteins. @ 1989 Academic press, IN.