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4 results on '"Peoch, K."'

1. A novel binding assay for detection of 14-3-3 protein in cerebrospinal fluid from Creutzfeldt-Jakob patients

Author

Leuck J, Peoch K, Jl, Laplanche, Grabar E, Werner E.G. Müller, and Hc, Schröder

Subjects
Brain Chemistry, Immunoassay, Binding Sites, Tyrosine 3-Monooxygenase, Amino Acid Motifs, Immunoblotting, Molecular Sequence Data, Phosphoproteins, Sensitivity and Specificity, Antibodies, Creutzfeldt-Jakob Syndrome, 14-3-3 Proteins, Animals, Humans, Cattle, Amino Acid Sequence, Phosphorylation, Peptides, Aged, Protein Binding
Abstract

Here we describe a simple and fast microplate assay for 14-3-3 protein, which is based on the binding of 14-3-3 protein to a chemically synthesized peptide containing the phosphorylated recognition sequence of this protein. The peptide is covalently bound to maleimide-activated microplates through reaction of the sulfhydryl group of a N-terminal cysteine residue linked to the peptide. The peptide- 14-3-.3 complexes formed are detected using--as a second recognition principle--an anti-14-3-3 protein antibody. This assay was used for measurement of 14-3-3 protein in brain (bovine) and in cerebrospinal fluid from patients with Creutzfeldt-Jakob disease (CJD) and control cases with diseases other than CJD. This novel assay allowed also the detection of low 14-3-3 protein levels present in cerebrospinal fluid, without further concentration, in contrast to conventional immunoblotting or immunoassay procedures.

Published
2000

2. Beyond PrPres type 1/Type 2 dichotomy in Creutzfeldt-Jakob disease

Author

Uro-Coste, E., Cassard, H., Simon, S., Lugan, S., Bilheude, J.M., Perret-Liaudet, A., Ironside, J.E., Haik, S., Basset-Leobon, C., Lacroux, C., Peoch, K., Streichenberger, N., Langeveld, J.P.M., Head, M.W., Grassi, J., Hauw, J.J., Schelcher, F., Delisle, M.B., Andreoletti, O., Uro-Coste, E., Cassard, H., Simon, S., Lugan, S., Bilheude, J.M., Perret-Liaudet, A., Ironside, J.E., Haik, S., Basset-Leobon, C., Lacroux, C., Peoch, K., Streichenberger, N., Langeveld, J.P.M., Head, M.W., Grassi, J., Hauw, J.J., Schelcher, F., Delisle, M.B., and Andreoletti, O.

Abstract

Sporadic Creutzfeldt-Jakob disease (sCJD) cases are currently subclassified according to the methionine/valine polymorphism at codon 129 of the PRNP gene and the proteinase K (PK) digested abnormal prion protein (PrPres) identified on Western blotting (type 1 or type 2). These biochemically distinct PrPres types have been considered to represent potential distinct prion strains. However, since cases of CJD show co-occurrence of type 1 and type 2 PrPres in the brain, the basis of this classification system and its relationship to agent strain are under discussion. Different brain areas from 41 sCJD and 12 iatrogenic CJD (iCJD) cases were investigated, using Western blotting for PrPres and two other biochemical assays reflecting the behaviour of the disease-associated form of the prion protein (PrPSc) under variable PK digestion conditions. In 30% of cases, both type 1 and type 2 PrPres were identified. Despite this, the other two biochemical assays found that PrPSc from an individual patient demonstrated uniform biochemical properties. Moreover, in sCJD, four distinct biochemical PrPSc subgroups were identified that correlated with the current sCJD clinico-pathological classification. In iCJD, four similar biochemical clusters were observed, but these did not correlate to any particular PRNP 129 polymorphism or western blot PrPres pattern. The identification of four different PrPSc biochemical subgroups in sCJD and iCJD, irrespective of the PRNP polymorphism at codon 129 and the PrPres isoform provides an alternative biochemical definition of PrPSc diversity and new insight in the perception of Human TSE agents variability

Published
2008

3. Beyond PrP9res) type 1/type 2 dichotomy in Creutzfeldt-Jakob disease.

Author

Uro-Coste E, Cassard H, Simon S, Lugan S, Bilheude JM, Perret-Liaudet A, Ironside JW, Haik S, Basset-Leobon C, Lacroux C, Peoch' K, Streichenberger N, Langeveld J, Head MW, Grassi J, Hauw JJ, Schelcher F, Delisle MB, and Andréoletti O

Subjects
Blotting, Western, Brain Chemistry, Enzyme-Linked Immunosorbent Assay, Genetic Variation, Humans, PrPSc Proteins genetics, PrPSc Proteins immunology, Protein Conformation, Protein Isoforms, Species Specificity, Brain metabolism, Creutzfeldt-Jakob Syndrome metabolism, PrPSc Proteins metabolism
Abstract

Sporadic Creutzfeldt-Jakob disease (sCJD) cases are currently subclassified according to the methionine/valine polymorphism at codon 129 of the PRNP gene and the proteinase K (PK) digested abnormal prion protein (PrP(res)) identified on Western blotting (type 1 or type 2). These biochemically distinct PrP(res) types have been considered to represent potential distinct prion strains. However, since cases of CJD show co-occurrence of type 1 and type 2 PrP(res) in the brain, the basis of this classification system and its relationship to agent strain are under discussion. Different brain areas from 41 sCJD and 12 iatrogenic CJD (iCJD) cases were investigated, using Western blotting for PrP(res) and two other biochemical assays reflecting the behaviour of the disease-associated form of the prion protein (PrP(Sc)) under variable PK digestion conditions. In 30% of cases, both type 1 and type 2 PrP(res) were identified. Despite this, the other two biochemical assays found that PrP(Sc) from an individual patient demonstrated uniform biochemical properties. Moreover, in sCJD, four distinct biochemical PrP(Sc) subgroups were identified that correlated with the current sCJD clinico-pathological classification. In iCJD, four similar biochemical clusters were observed, but these did not correlate to any particular PRNP 129 polymorphism or western blot PrP(res) pattern. The identification of four different PrP(Sc) biochemical subgroups in sCJD and iCJD, irrespective of the PRNP polymorphism at codon 129 and the PrP(res) isoform provides an alternative biochemical definition of PrP(Sc) diversity and new insight in the perception of Human TSE agents variability.

Published
2008
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4. Beyond PrP res type 1/type 2 dichotomy in Creutzfeldt-Jakob disease.

Author

Uro-Coste E, Cassard H, Simon S, Lugan S, Bilheude JM, Perret-Liaudet A, Ironside JW, Haik S, Basset-Leobon C, Lacroux C, Peoch K, Streichenberger N, Langeveld J, Head MW, Grassi J, Hauw JJ, Schelcher F, Delisle MB, and Andréoletti O

Subjects
Biological Assay, Blotting, Western, Brain pathology, Brain Chemistry, Humans, PrPSc Proteins chemistry, PrPSc Proteins classification, Protein Isoforms chemistry, Protein Isoforms classification, Protein Isoforms metabolism, Species Specificity, Creutzfeldt-Jakob Syndrome classification, Creutzfeldt-Jakob Syndrome metabolism, PrPSc Proteins metabolism
Abstract

Sporadic Creutzfeldt-Jakob disease (sCJD) cases are currently subclassified according to the methionine/valine polymorphism at codon 129 of the PRNP gene and the proteinase K (PK) digested abnormal prion protein (PrPres)identified on Western blotting (type 1 or type 2). These biochemically distinct PrPres types have been considered to represent potential distinct prion strains. However, since cases of CJD show co-occurrence of type 1 and type 2 PrPres in the brain, the basis of this classification system and its relationship to agent strain are under discussion. Different brain are as from 41 sCJD and 12 iatrogenic CJD (iCJD) cases were investigated, using Western blotting for PrPres and two other biochemical assays reflecting the behaviour of the disease-associated form of the prion protein (PrPSc) under variable PK digestion conditions. In 30% of cases, both type 1 and type 2 PrPres were identified. Despite this, the other two biochemical assays found that PrPSc from an individual patient demonstrated uniform biochemical properties. Moreover, in sCJD, four distinct biochemical PrPSc subgroups were identified that correlated with the current sCJD clinico-pathological classification. In iCJD, four similar biochemical clusters were observed, but these did not correlate to any particular PRNP 129 polymorphism or western blot PrPres pattern. The identification of four different PrPSc biochemical subgroups in sCJD and iCJD, irrespective of the PRNP polymorphism at codon 129 and the PrPres isoform provides an alternative biochemical definition of PrPSc diversity and new insight in the perception of Human TSE agents variability.

Published
2008

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