0000000000248248

AUTHOR

Tiina Viitasalo

showing 3 related works from this author

The Fibril-associated Collagen IX Provides a Novel Mechanism for Cell Adhesion to Cartilaginous Matrix

2004

Collagen IX is the prototype fibril-associated collagen with interruptions in triple helix. In human cartilage it covers collagen fibrils, but its putative cellular receptors have been unknown. The reverse transcription-PCR analysis of human fetal tissues suggested that based on their distribution all four collagen receptor integrins, namely alpha1beta1, alpha2beta1, alpha10beta1, and alpha11beta1, are possible receptors for collagen IX. Furthermore primary chondrocytes and chondrosarcoma cells express the four integrins simultaneously. Chondrosarcoma cells, as well as Chinese hamster ovary cells transfected to express alpha1beta1, alpha2beta1, or alpha10beta1 integrin as their only collage…

Integrin alpha1Integrin alpha2LigandsPolymerase Chain ReactionBiochemistryCollagen receptorMiceCricetinaeReceptorbiologyReverse Transcriptase Polymerase Chain ReactionChemistryChinese hamster ovary cellRecombinant ProteinsCell biologyBiochemistryCollagenIntegrin alpha ChainsProtein BindingMolecular Sequence DataIntegrinChondrosarcomaCHO CellsFibrilCollagen Type IXCell LineChondrocytesMicroscopy Electron TransmissionCell Line TumorCell AdhesionEscherichia coliAnimalsHumansImmunoprecipitationAmino Acid SequenceRNA MessengerBinding siteCell adhesionMolecular BiologyBinding SitesSequence Homology Amino AcidCell BiologyProtein Structure TertiaryRatsMicroscopy ElectronCollagen type I alpha 1CartilageMutationMutagenesis Site-Directedbiology.proteinRNAPeptidesJournal of Biological Chemistry
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The cell adhesion domain of type XVII collagen promotes integrin-mediated cell spreading by a novel mechanism.

2001

Type XVII collagen (BP180) is a keratinocyte transmembrane protein that exists as the full-length protein in hemidesmosomes and as a 120-kDa shed ectodomain in the extracellular matrix. The largest collagenous domain of type XVII collagen, COL15, has been described previously as a cell adhesion domain (Tasanen, K., Eble, J. A., Aumailley, M., Schumann, H., Baetge, J, Tu, H., Bruckner, P., and Bruckner-Tuderman, L. (2000) J. Biol. Chem. 275, 3093-3099). In the present work, the integrin binding of triple helical, human recombinant COL15 was tested. Solid phase binding assays using recombinant integrin alpha(1)I, alpha(2)I, and alpha(10)I domains and cell spreading assays with alpha(1)beta(1)…

KeratinocytesIntegrinsDNA ComplementaryDystoninIntegrinAmino Acid MotifsNerve Tissue ProteinsCHO CellsBiochemistryAutoantigensCollagen receptorCell LineCell MovementCricetinaeCell AdhesionTumor Cells CulturedAnimalsHumansCloning MolecularCell adhesionMolecular BiologyIntegrin bindingbiologyDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionHemidesmosomeCell BiologyNon-Fibrillar CollagensMolecular biologyRecombinant ProteinsProtein Structure TertiaryFibronectinHaCaTCytoskeletal ProteinsEctodomainbiology.proteinCollagenCarrier ProteinsPeptidesProtein BindingThe Journal of biological chemistry
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Selective Binding of Collagen Subtypes by Integrin α1I, α2I, and α10I Domains

2001

Four integrins, namely alpha(1)beta(1), alpha(2)beta(1), alpha(10)beta(1), and alpha(11)beta(1), form a special subclass of cell adhesion receptors. They are all collagen receptors, and they recognize their ligands with an inserted domain (I domain) in their alpha subunit. We have produced the human integrin alpha(10)I domain as a recombinant protein to reveal its ligand binding specificity. In general, alpha(10)I did recognize collagen types I-VI and laminin-1 in a Mg(2+)-dependent manner, whereas its binding to tenascin was only slightly better than to albumin. When alpha(10)I was tested together with the alpha(1)I and alpha(2)I domains, all three I domains seemed to have their own collag…

Type IV collagenIntegrin alpha2Integrin alpha ChainsAlpha (ethology)Cell BiologyBiologyMolecular BiologyBiochemistryMolecular biologyType I collagenBinding domainCollagen receptorG alpha subunitJournal of Biological Chemistry
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