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000059197 0247_ $$2DOI$$a10.1016/j.yexcr.2007.02.003
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000059197 041__ $$aeng
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000059197 084__ $$2WoS$$aOncology
000059197 084__ $$2WoS$$aCell Biology
000059197 1001_ $$0P:(DE-HGF)0$$aHartwig, B.$$b0
000059197 245__ $$aLaminin-5-deficient human keratinocytes: Defective adhesion results in a saltatory and inefficient mode of migration
000059197 260__ $$aOrlando, Fla.$$bAcademic Press$$c2007
000059197 300__ $$a1575 - 1587
000059197 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000059197 440_0 $$013781$$aExperimental Cell Research$$v313$$x0014-4827$$y8
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000059197 520__ $$aLaminin-5 is a major adhesion protein of the skin basement membrane and crucially involved in integrin-mediated cell substrate attachment of keratinocytes, which is important for hemidesmosomal anchorage as well as for keratinocyte migration during epidermal wound healing. To investigate its role in keratinocyte migration, we analyzed laminin-5-deficient cells of patients with a lethal variant of junctional epidermolysis bullosa. Normal migrating keratinocytes adopted monopolar morphology with a distinct front lamella and employed a continuous mode of translocation. In contrast, laminin-5-deficient cells assumed a stretched bipolar shape with two lamella regions and migrated in a discontinuous, saltatory manner characterized by significantly decreased directional persistence and reduced migration velocity. The distinct morphology as well as the migratory phenotype apparently resulted from a defect in the formation of cell substrate adhesions that were completely missing in the cell body and less stable in the lamella regions. Accordingly in normal keratinocytes, a bipolar shape and a saltatory migration mode were inducible by blocking laminin-5-mediated substrate adhesion. Our findings clearly point to an essential role of laminin-5 in forming dynamic cell substrate adhesion during migration of epidermal keratinocytes and provide an explanation for the cellular mechanisms that underlie the lethal form of junctional epidermolysis bullosa.
000059197 536__ $$0G:(DE-Juel1)FUEK414$$2G:(DE-HGF)$$aKondensierte Materie$$cP54$$x0
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000059197 650_2 $$2MeSH$$aCell Adhesion
000059197 650_2 $$2MeSH$$aCell Adhesion Molecules: genetics
000059197 650_2 $$2MeSH$$aCell Adhesion Molecules: metabolism
000059197 650_2 $$2MeSH$$aCell Adhesion Molecules: physiology
000059197 650_2 $$2MeSH$$aCell Movement
000059197 650_2 $$2MeSH$$aCell Polarity
000059197 650_2 $$2MeSH$$aCell Shape
000059197 650_2 $$2MeSH$$aCells, Cultured
000059197 650_2 $$2MeSH$$aEpidermolysis Bullosa, Junctional: metabolism
000059197 650_2 $$2MeSH$$aEpidermolysis Bullosa, Junctional: pathology
000059197 650_2 $$2MeSH$$aExtracellular Matrix Proteins: metabolism
000059197 650_2 $$2MeSH$$aHumans
000059197 650_2 $$2MeSH$$aKeratinocytes: physiology
000059197 650_2 $$2MeSH$$aPseudopodia: physiology
000059197 650_7 $$00$$2NLM Chemicals$$aCell Adhesion Molecules
000059197 650_7 $$00$$2NLM Chemicals$$aExtracellular Matrix Proteins
000059197 650_7 $$00$$2NLM Chemicals$$akalinin
000059197 650_7 $$2WoSType$$aJ
000059197 65320 $$2Author$$akeratinocytes
000059197 65320 $$2Author$$alaminin-5-deficiency
000059197 65320 $$2Author$$ajunctional epidermolysis bullosa
000059197 65320 $$2Author$$acell adhesion
000059197 65320 $$2Author$$acell migration
000059197 65320 $$2Author$$asaltatory migration
000059197 7001_ $$0P:(DE-Juel1)VDB57504$$aBorm, B.$$b1$$uFZJ
000059197 7001_ $$0P:(DE-HGF)0$$aSchneider, H.$$b2
000059197 7001_ $$0P:(DE-HGF)0$$aArin, M. J.$$b3
000059197 7001_ $$0P:(DE-HGF)0$$aKirfel, G.$$b4
000059197 7001_ $$0P:(DE-HGF)0$$aHerzog, V.$$b5
000059197 773__ $$0PERI:(DE-600)1466780-0$$a10.1016/j.yexcr.2007.02.003$$gVol. 313, p. 1575 - 1587$$p1575 - 1587$$q313<1575 - 1587$$tExperimental cell research$$v313$$x0014-4827$$y2007
000059197 8567_ $$uhttp://dx.doi.org/10.1016/j.yexcr.2007.02.003
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000059197 9141_ $$y2007
000059197 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
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