0000000000175622

AUTHOR

Thomas M. Magin

showing 4 related works from this author

Ectopic expression of desmin in the epidermis of transgenic mice permits development of a normal epidermis.

2002

Cell architecture is largely based on the interaction of cytoskeletal proteins, which include intermediate filaments (IF), microfilaments, microtubules, as well as their type-specific membrane-attachment structures and associated proteins. In order to further our understanding of IF proteins and to address the fundamental issue whether different IF perform unique functions in different tissues, we expressed a desmin transgene in the basal epidermis of mice. Ectopic expression of desmin led to the formation of an additional, keratin-independent IF cytoskeleton and did not interfere with the keratin-desmosome interaction. We show that ectopic expression of a type III IF protein in basal kerat…

KeratinocytesCancer ResearchCellular differentiationMice Transgenicmacromolecular substancesBiologyDesminMiceKeratinmedicineAnimalsHumansIntermediate filamentCytoskeletonMolecular Biologychemistry.chemical_classificationEpidermis (botany)Keratin-14Cell BiologyImmunohistochemistryCell biologyDisease Models Animalmedicine.anatomical_structurePhenotypechemistryEpidermolysis Bullosa SimplexImmunologyKeratinsEctopic expressionDesminEpidermisKeratinocyteDevelopmental BiologyDifferentiation; research in biological diversity
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Epidermolysis Bullosa Simplex-Type Mutations Alter the Dynamics of the Keratin Cytoskeleton and Reveal a Contribution of Actin to the Transport of Ke…

2003

Dominant keratin mutations cause epidermolysis bullosa simplex by transforming keratin (K) filaments into aggregates. As a first step toward understanding the properties of mutant keratins in vivo, we stably transfected epithelial cells with an enhanced yellow fluorescent protein-tagged K14R125C mutant. K14R125C became localized as aggregates in the cell periphery and incorporated into perinuclear keratin filaments. Unexpectedly, keratin aggregates were in dynamic equilibrium with soluble subunits at a half-life time of <15 min, whereas filaments were extremely static. Therefore, this dominant-negative mutation acts by altering cytoskeletal dynamics and solubility. Unlike previously post…

KeratinocytesMutantmacromolecular substancesBiologyEpidermolysis bullosa simplexMicrotubuleKeratinmedicineHumansRNA Small InterferingCytoskeletonMolecular BiologyCells CulturedCytoskeletonActinchemistry.chemical_classificationintegumentary systemBiological TransportArticlesCell BiologyKeratin 6Amedicine.diseaseMolecular biologyActinsRecombinant ProteinsCell biologyKeratin 5chemistryEpidermolysis Bullosa SimplexMutationKeratinsMolecular Biology of the Cell
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Patterns of Expression and Organization of Cytokeratin Intermediate Filaments

1985

Cytokeratins are a large multigene family comprising two polypeptide types, i.e. acidic (type I) and basic (type II) ones, which are distinguished on the basis of immunological, peptide mapping, mRNA hybridization, and primary amino acid sequence data. The acidic (type I) cytokeratins can be subdivided into at least two different subtypes on the basis of their carboxy-terminal sequences. Considerable interspecies conservation of sequences exists, even extending to the 3'-non-coding mRNA regions. Different pairs of type I and II cytokeratins show different resistance to dissociation in urea. Sequence differences of the type I cytokeratins containing functional domains may be an explanation o…

Messenger RNANeurofilamentBase SequenceProtein ConformationChemistryGeneral NeuroscienceIntermediate FilamentsRNAMolecular biologyGeneral Biochemistry Genetics and Molecular BiologyMolecular WeightCytokeratinProtein structureHistory and Philosophy of ScienceTetramerAnimalsHumansKeratinsAmino Acid SequenceRNA MessengerIntermediate filamentPeptide sequenceCytoskeletonAnnals of the New York Academy of Sciences
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Structural and regulatory functions of keratins.

2007

The diversity of epithelial functions is reflected by the expression of distinct keratin pairs that are responsible to protect epithelial cells against mechanical stress and to act as signaling platforms. The keratin cytoskeleton integrates these functions by forming a supracellular scaffold that connects at desmosomal cell-cell adhesions. Multiple human diseases and murine knockouts in which the integrity of this system is destroyed testify to its importance as a mechanical stabilizer in certain epithelia. Yet, surprisingly little is known about the precise mechanisms responsible for assembly and disease pathology. In addition to these structural aspects of keratin function, experimental e…

CellIntermediate Filamentsmacromolecular substancesBiologyFocal adhesionEpidermolysis bullosa simplexMicrotubuleOrganelleKeratinmedicineAnimalsHumansCytoskeletonCytoskeletonchemistry.chemical_classificationCell PolarityEpithelial CellsCell BiologyDesmosomesmedicine.diseaseCell biologymedicine.anatomical_structureCell Transformation NeoplasticchemistryKeratinsStress MechanicalFunction (biology)Signal TransductionExperimental cell research
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