Linked Life Data

10906782

Source:http://linkedlifedata.com/resource/pubmed/id/10906782

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-10-5
pubmed:abstractText
HOX homeodomain proteins are master developmental regulators, which are now thought to function as transcription factors by forming cooperative DNA binding complexes with PBX or other protein partners. Although PBX proteins exhibit regulated subcellular localization and function in the nucleus in other tissues, little data exists on HOX and PBX protein localization during skin development. We now show that the HOXB6 protein is expressed in the suprabasal layer of the early developing epidermis and throughout the upper layers of late fetal and adult human skin. HOXB6 signal is cytoplasmic throughout fetal epidermal development, but substantially nuclear in normal adult skin. HOXB6 protein is also partially nuclear in hyperproliferative skin conditions, but appears to be cytoplasmic in basal and squamous cell carcinomas. Although all three PBX genes are expressed in fetal epidermis, none of the three PBX proteins exhibit nuclear co-localization with HOXB6 in either fetal or adult epidermis. RNA and protein data suggest that a truncated HOXB6 protein, lacking the homeodomain, is expressed in undifferentiated keratinocytes and that the full-length protein is induced by differentiation. GFP-fusion proteins were used to demonstrate that the full-length HOXB6 protein is localized to the nucleus while the truncated protein is largely cytoplasmic. Taken together, these data suggest that during epidermal development the truncated HOXB6 isoform may function by a mechanism other than as DNA binding protein, and that most of the nuclear, homeodomain-containing HOXB6 protein does not utilize PBX proteins as DNA binding partners in the skin. Published 2000 Wiley-Liss, Inc.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1058-8388
pubmed:author
pubmed:issnType
Print
pubmed:volume
218
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
636-47
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10906782-Adult, pubmed-meshheading:10906782-Calcium, pubmed-meshheading:10906782-Cell Differentiation, pubmed-meshheading:10906782-Cell Nucleus, pubmed-meshheading:10906782-Cells, Cultured, pubmed-meshheading:10906782-Cytoplasm, pubmed-meshheading:10906782-DNA-Binding Proteins, pubmed-meshheading:10906782-Dose-Response Relationship, Drug, pubmed-meshheading:10906782-Epidermis, pubmed-meshheading:10906782-Homeodomain Proteins, pubmed-meshheading:10906782-Humans, pubmed-meshheading:10906782-Immunohistochemistry, pubmed-meshheading:10906782-In Situ Hybridization, pubmed-meshheading:10906782-Keratinocytes, pubmed-meshheading:10906782-Proto-Oncogene Proteins, pubmed-meshheading:10906782-RNA, Messenger, pubmed-meshheading:10906782-Recombinant Fusion Proteins, pubmed-meshheading:10906782-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:10906782-Time Factors, pubmed-meshheading:10906782-Transcription, Genetic, pubmed-meshheading:10906782-Transfection
pubmed:year
2000
pubmed:articleTitle
Changes in HOXB6 homeodomain protein structure and localization during human epidermal development and differentiation.
pubmed:affiliation
Department of Dermatology, University of California VA Medical Center, San Francisco, California.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't