0000000000610467

AUTHOR

Matthias Conrad

showing 3 related works from this author

Zebrafish vimentin: molecular characterization, assembly properties and developmental expression

1998

To provide a basis for the investigation of the intermediate filament (IF) protein vimentin in one of the most promising experimental vertebrate systems, the zebrafish (Danio rerio), we have isolated a cDNA clone of high sequence identity to and with the characteristic features of human vimentin. Using this clone we produced recombinant zebrafish vimentin and studied its assembly behaviour. Unlike other vimentins, zebrafish vimentin formed unusually thick filaments when assembled at temperatures below 21 degrees C. At 37 degrees C few filaments were observed, which often also terminated in aggregated masses, indicating that its assembly was severely disturbed at this temperature. Between 21…

HistologyTroutMolecular Sequence DataCellDanioClone (cell biology)Vimentinmacromolecular substancesPathology and Forensic MedicineMyosinmedicineAnimalsHumansVimentinTissue DistributionAmino Acid SequenceRNA MessengerCloning MolecularIntermediate filamentPeptide sequenceZebrafishZebrafishSequence Homology Amino AcidbiologyTemperatureGene Expression Regulation DevelopmentalCell BiologyGeneral Medicinebiology.organism_classificationImmunohistochemistryMolecular biologyCell biologyMicroscopy Electronmedicine.anatomical_structurebiology.protein
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Biochemical identification and tissue-specific expression patterns of keratins in the zebrafish Danio rerio

1998

We have identified a number of type I and type II keratins in the zebrafish Danio rerio by two-dimensional polyacrylamide gel electrophoresis, complementary keratin blot-binding assay and immunoblotting. These keratins range from 56 kDa to 46 kDa in molecular mass and from pH 6.6 to pH 5.2 in isoelectric point. Type II zebrafish keratins exhibit significantly higher molecular masses (56-52 kDa) compared with the type I keratins (50-48 kDa), but the isoelectric points show no significant difference between the two keratin subclasses (type II: pH 6.0-5.5; type I: pH 6.1-5.2). According to their occurrence in various zebrafish tissues, the identified keratins can be classified into "E" (epider…

chemistry.chemical_classificationanimal structuresHistologyintegumentary systembiologyMolecular massCellular differentiationDanioCell Biologybiology.organism_classificationMolecular biologyPathology and Forensic MedicineIsoelectric pointMicroscopy FluorescenceBiochemistrychemistryGenetic modelKeratinAnimalsKeratinsTissue DistributionPolyacrylamide gel electrophoresisZebrafishCytoskeletonZebrafishCell and Tissue Research
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Type I keratin cDNAs from the rainbow trout: independent radiation of keratins in fish

2002

Five different type I keratins from a teleost fish, the rainbow trout Oncorhynchus mykiss, have been sequenced by cDNA cloning and identified at the protein level by peptide mass mapping using MALDI-MS. This showed that the entire range of type I keratins detected biochemically in this fish has now been sequenced. Three of the keratins are expressed in the epidermis (subtype Ie), whereas the other two occur in simple epithelia and mesenchymal cells (subtype Is). Among the Is keratins is an ortholog of human K18; the second Is polypeptide is clearly distinct from K18. We raised a new monoclonal antibody (F1F2, subclass IgG1) that specifically recognizes trout Is keratins, with negative react…

Cancer ResearchDNA Complementaryanimal structuresType I keratinMolecular Sequence Datamacromolecular substancesBiologyPeptide MappingEvolution MolecularMesodermSpecies SpecificityAntibody SpecificityKeratinAnimalsHumansProtein IsoformsAmino Acid SequenceCloning MolecularMolecular BiologyZebrafishPhylogenyZebrafishMammalschemistry.chemical_classificationGeneticsMultiple sequence alignmentSequence Homology Amino Acidintegumentary systemPhylogenetic treeLampreyAntibodies MonoclonalLampreysEpithelial CellsCell Biologybiology.organism_classificationProtein Structure TertiaryTroutchemistryOrgan SpecificityOncorhynchus mykissSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationSharksKeratinsRainbow troutEpidermisSequence AlignmentDevelopmental BiologyDifferentiation
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