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| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0521447 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0079904 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1442161 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0600210 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1550548 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1555714 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0243067 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C0678227 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1705654 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:15988021 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15988021 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:15988021 | pubmed:dateCreated | 2005-6-30 | lld:pubmed |
| pubmed-article:15988021 | pubmed:abstractText | The alpha6beta4 integrin-a laminin-5 receptor-mediates assembly of hemidesmosomes and recruitment of Shc and phosphoinositide 3-kinase through the unique cytoplasmic extension of beta4. Mice carrying a targeted deletion of the signaling domain of beta4 develop normally and do not display signs of skin fragility. The epidermis of these mice contains well-structured hemidesmosomes and adheres stably to the basement membrane. However, it is hypoplastic due to reduced proliferation of basal keratinocytes and undergoes wound repair at a reduced rate. Keratinocytes from beta4 mutant mice undergo extensive spreading but fail to proliferate and migrate in response to epidermal growth factor (EGF) on laminin-5. EGF causes significant phosphorylation of extracellular signal-regulated kinase (ERK) and Jun N-terminal protein kinase (JNK) and phosphorylation and degradation of IkappaB in beta4 mutant cells adhering to laminin-5. Unexpectedly, however, ERK, JNK, and NF-kappaB remain in the cytoplasm in beta4 mutant cells on laminin-5, whereas they enter effectively into the nucleus in the same cells on fibronectin or in wild-type cells on both matrix proteins. Inhibitor studies indicate that alpha6beta4 promotes keratinocyte proliferation and migration through its effect on NF-kappaB and P-JNK. These findings provide evidence that beta4 signaling promotes epidermal growth and wound healing through a previously unrecognized effect on nuclear translocation of NF-kappaB and mitogen-activated protein kinases. | lld:pubmed |
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| pubmed-article:15988021 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15988021 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15988021 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15988021 | pubmed:month | Jul | lld:pubmed |
