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@ARTICLE{Hartwig:59197,
author = {Hartwig, B. and Borm, B. and Schneider, H. and Arin, M. J.
and Kirfel, G. and Herzog, V.},
title = {{L}aminin-5-deficient human keratinocytes: {D}efective
adhesion results in a saltatory and inefficient mode of
migration},
journal = {Experimental cell research},
volume = {313},
issn = {0014-4827},
address = {Orlando, Fla.},
publisher = {Academic Press},
reportid = {PreJuSER-59197},
pages = {1575 - 1587},
year = {2007},
note = {Record converted from VDB: 12.11.2012},
abstract = {Laminin-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.},
keywords = {Cell Adhesion / Cell Adhesion Molecules: genetics / Cell
Adhesion Molecules: metabolism / Cell Adhesion Molecules:
physiology / Cell Movement / Cell Polarity / Cell Shape /
Cells, Cultured / Epidermolysis Bullosa, Junctional:
metabolism / Epidermolysis Bullosa, Junctional: pathology /
Extracellular Matrix Proteins: metabolism / Humans /
Keratinocytes: physiology / Pseudopodia: physiology / Cell
Adhesion Molecules (NLM Chemicals) / Extracellular Matrix
Proteins (NLM Chemicals) / kalinin (NLM Chemicals) / J
(WoSType)},
cin = {IBN-4},
ddc = {570},
cid = {I:(DE-Juel1)VDB802},
pnm = {Kondensierte Materie},
pid = {G:(DE-Juel1)FUEK414},
shelfmark = {Oncology / Cell Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:17335805},
UT = {WOS:000246128300006},
doi = {10.1016/j.yexcr.2007.02.003},
url = {https://juser.fz-juelich.de/record/59197},
}