Linked Life Data

1316927

Source:http://linkedlifedata.com/resource/pubmed/id/1316927

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6 Suppl
pubmed:dateCreated
1992-6-25
pubmed:abstractText
Nuclear retinoic acid receptors (RAR) are likely to mediate many of the pleiotypic cutaneous actions of retinoids by acting as ligand-dependent enhancer factors. The presence of nuclear RAR in skin was confirmed by identification of a 45-kDa nuclear RA binding activity by fast protein liquid chromatography (FPLC). Analysis of RNA extracted from skin specimens demonstrated expression of RAR-alpha and RAR-gamma transcripts, as well as expression of the homologous low-affinity receptor, RXR-alpha. Both isoforms of RAR-gamma RAR-gamma 1 and RAR-gamma 2 were detectable, with RAR-gamma 1 being the more strongly expressed. FPLC analysis also demonstrated a 15-kDa peak of specific RA binding activity, consistent with the presence of cellular retinoic acid binding protein (CRABP). Of the two known forms of CRABP, CRABP-II was much more strongly expressed than CRABP-I at the level of steady-state mRNA. CRABP-II was also expressed in keratinocytes and fibroblasts in vitro. CRABP-II was up-regulated by agents that induce keratinocyte differentiation, and inhibited by prolonged exposure to high concentrations of RA. In contrast, CRABP-II was consistently induced by RA in dermal, but not in lung fibroblasts. CRABP-I was expressed at low to undetectable levels under all these conditions. The presence of tissue-specific and differentiation-related regulation of CRABP-II suggests that it may be an important regulator of RA action in human skin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-202X
pubmed:author
pubmed:issnType
Print
pubmed:volume
98
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
36S-41S
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Retinoic acid receptors and binding proteins in human skin.
pubmed:affiliation
Department of Dermatology, University of Michigan, Ann Arbor 48109-0672.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't