Search results for "isoforms"

showing 5 items of 185 documents

Characterization of lacrimal proline-rich protein 4 (PRR4) in human tear proteome

2014

This study was initiated considering the lack of comprehensive characteristics profile of PRR4 in tears of healthy subjects. Therefore, detailed characterizations of PRR4 from basal tears employing in-gel and in-solution digestions for MS systems are presented herein. First, pooled tear samples (n = 10) were utilized to identify PRR4-rich region/spots in 1DE/2DE gels employing LC-MALDI-MS and 1DE-LC-ESI-LTQ-Orbitrap-MS systems. PRR4-rich region and ten spots with vast polymorphisms (Mr : 17-30 kDa, pI: 3.0-6.6) were identified in 1DE and 2DE gels, respectively. In addition, combinations of four types of PTMs, which are methylation, acetylation, oxidation, and pyroglutamate formation, were i…

AdultMaleGene isoformProteomeMolecular Sequence DataBiologyBiochemistryYoung AdultHumansProtein IsoformsElectrophoresis Gel Two-DimensionalAmino Acid SequenceLACRIMAL PROLINE-RICH PROTEINMolecular BiologyGel electrophoresisChromatographyHealthy subjectsProteinsMethylationBiochemistryAcetylationSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationTearsProteomeTearsFemalePROTEOMICS
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Plasma membrane Ca2+ ATPase 4 is required for sperm motility and male fertility.

2004

Calcium and Ca(2+)-dependent signals play a crucial role in sperm motility and mammalian fertilization, but the molecules and mechanisms underlying these Ca(2+)-dependent pathways are incompletely understood. Here we show that homozygous male mice with a targeted gene deletion of isoform 4 of the plasma membrane calcium/calmodulin-dependent calcium ATPase (PMCA), which is highly enriched in the sperm tail, are infertile due to severely impaired sperm motility. Furthermore, the PMCA inhibitor 5-(and-6)-carboxyeosin diacetate succinimidyl ester reduced sperm motility in wild-type animals, thus mimicking the effects of PMCA4 deficiency on sperm motility and supporting the hypothesis of a pivot…

MaleTime FactorsBiochemistryMiceTestisProtein IsoformsCloning MolecularCation Transport Proteinsreproductive and urinary physiologySperm motilityMice KnockoutRecombination GeneticReverse Transcriptase Polymerase Chain ReactionPlasma Membrane Calcium-Transporting ATPasesFluoresceinsTransport proteinCell biologyBlotting SouthernBiochemistrySperm Motilityendocrine systemDNA ComplementaryGenotypeBlotting WesternMolecular Sequence Datachemistry.chemical_elementSuccinimidesCalcium-Transporting ATPasesFertilization in VitroCalciumBiologyPlasma Membrane Calcium-Transporting ATPasesAnimalsHumansMolecular BiologyFluorescent DyesCalcium metabolismModels Geneticurogenital systemCell BiologyBlotting NorthernSpermProtein Structure TertiaryRatsCalcium ATPaseAlternative SplicingFertilitychemistryMicroscopy FluorescencePlasma membrane Ca2+ ATPaseCalciumThe Journal of biological chemistry
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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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SNAP-25a and -25b isoforms are both expressed in insulin-secreting cells and can function in insulin secretion

1999

The tSNARE (the target-membrane soluble NSF-attachment protein receptor, where NSF is N-ethylmaleimide-sensitive fusion protein) synaptosomal-associated protein of 25 kDa (SNAP-25) is expressed in pancreatic B-cells and its cleavage by botulinum neurotoxin E (BoNT/E) abolishes stimulated secretion of insulin. In the nervous system, two SNAP-25 isoforms (a and b) have been described that are produced by alternative splicing. Here it is shown, using reverse transcriptase PCR, that messages for both SNAP-25 isoforms are expressed in primary pancreatic B and non-B cells as well as in insulin-secreting cell lines. After transfection, both isoforms can be detected at the plasma membrane as well a…

Gene isoformProtein Isoforms/genetics/ metabolismBotulinum ToxinsSynaptosomal-Associated Protein 25RNA Messenger/genetics/metabolismmedicine.medical_treatmentMutantNerve Tissue ProteinsBiologyBiochemistryCell LineIslets of LangerhansInsulin SecretionmedicineBotulinum Toxins/pharmacologyInsulinProtein IsoformsAnimalsHumansSecretionRNA MessengerReceptorMolecular BiologyDNA Primersddc:616Base SequenceInsulinMembrane ProteinsCell BiologyTransfectionNerve Tissue Proteins/genetics/ metabolismFusion proteinMolecular biologyRatsCell cultureMutagenesis Site-DirectedIslets of Langerhans/cytology/drug effects/ secretionInsulin/ secretionResearch Article
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Type II keratin cDNAs from the rainbow trout: implications for keratin evolution.

2002

From a teleost fish, the rainbow trout Oncorhynchus mykiss, we have cloned and sequenced cDNAs encoding five different type II keratins. The corresponding protein spots, as separated by 2D-PAGE of trout cytoskeletal preparations, have been identified by peptide mass mapping using MALDI mass spectrometry. Three of the sequenced keratins are expressed in the epidermis (subtype IIe), and two in simple epithelia and mesenchymal cells (subtype IIs). The IIs keratins are both orthologs of human K8. This leaves unsequenced only the trace component S3 of the biochemically established trout keratin catalog. A phylogenetic tree has been constructed from a multiple alignment of the rod domains of the …

endocrine systemCancer Researchanimal structuresDNA ComplementaryMolecular Sequence Datamacromolecular substancesPeptide MappingType II keratinEvolution MolecularMesodermSpecies SpecificityAntibody SpecificityKeratinAnimalsHumansProtein IsoformsAmino Acid SequenceCloning MolecularMolecular BiologyZebrafishPhylogenyZebrafishchemistry.chemical_classificationGeneticsMammalsMultiple sequence alignmentintegumentary systembiologyPhylogenetic treeSequence Homology Amino AcidLampreyAntibodies MonoclonalLampreysEpithelial CellsCell Biologybiology.organism_classificationProtein Structure TertiaryTroutchemistryOrgan SpecificityOncorhynchus mykissSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationSharksKeratinsRainbow troutEpidermisSequence AlignmentDevelopmental BiologyDifferentiation; research in biological diversity
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