Linked Life Data

9888509

Source:http://linkedlifedata.com/resource/pubmed/id/9888509

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1999-4-13
pubmed:abstractText
The role of MAP Kinase (MAPK/ERK) in adrenal growth and steroidogenesis is unclear, though in other tissues it is known to act as an integrator of mitogenic signals originating from receptor tyrosine kinases and G-protein coupled receptors. Angiotensin II (AngII) is a major regulator of tissue differentiation and function in the adrenal, acting mainly through the AT1 receptor. Immunocytochemical and enzyme assay methods were used to study the distribution of MAPK and the action of AngII and associated antagonists saralasin and losartan(DuP753) in the rat adrenal gland. MAPK is localised in the zona glomerulosa (ZG) and the medulla, but absent from the zonae fasiculata and reticularis (ZF/ZR). Stimulation with AngII led to decreases in cytosolic and increases in nuclear MAPK activity, and its redistribution from the cytoplasm in unstimulated cells to its localisation around the nucleus, which was confirmed by immunocytochemistry. This translocation was inhibited in the presence of the AngII antagonist saralasin. Therefore, MAPK is located in the glomerulosa, where the AT1 receptor is localised and concerned with aldosterone biosynthesis, and in the medulla where MAPK activation results from AT2R activation. The results indicate the importance of the glomerulosa as the main site of cell proliferation in the adrenal cortex, and that MAPK may represent new signalling pathways related to zone function in the adrenal gland.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0743-5800
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
373-80
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:articleTitle
MAP Kinase in the rat adrenal gland.
pubmed:affiliation
Department of Biochemistry, Queen Mary & Westfield College, London, UK.
pubmed:publicationType
Journal Article