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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
|
| pubmed:dateCreated |
1993-8-31
|
| pubmed:abstractText |
The regulation of cell activity, growth and metabolism by a number of growth factor receptors and proto-oncogene products involves tyrosine kinase activity resulting in autophosphorylation of the receptors and production of phosphorylated tyrosine-containing protein substrates. The identification and precise localization of phosphotyrosine (PY)-containing proteins are first steps in elucidating the functional role of tyrosine kinases in the modulation of the central nervous system and related areas. In the present report, we describe PY-containing proteins in the median eminence and adjacent pars tuberalis of the rat adenohypophysis by immunocytochemistry using light and electron microscopy, and by Western blotting analysis. PY-immunoreactivity was found to be most intense throughout the cytoplasm of a population of epithelial pars tuberalis cells. Polyacrylamide gel electrophoresis and Western blotting of tissue extracts from various brain and pituitary regions demonstrated a general pattern of 4 major bands of PY-proteins, with an additional dense band representing a 44 kDa protein that was highly phosphorylated on tyrosines and that was exclusively found in the pars tuberalis. Additional investigation for the presence of insulin receptors, a tyrosine kinase previously correlated with the distribution of PY-proteins, demonstrated a receptor localization in axons and nerve terminals in the external and internal zone of the median eminence. However, the large amount of different PY-proteins present in the secretory cell population of the pars tuberalis could not be attributed to the insulin receptor.(ABSTRACT TRUNCATED AT 250 WORDS)
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0302-766X
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
272
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
499-507
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:7687928-Animals,
pubmed-meshheading:7687928-Blotting, Western,
pubmed-meshheading:7687928-Brain,
pubmed-meshheading:7687928-Brain Chemistry,
pubmed-meshheading:7687928-Cytoplasm,
pubmed-meshheading:7687928-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:7687928-Immunohistochemistry,
pubmed-meshheading:7687928-Male,
pubmed-meshheading:7687928-Median Eminence,
pubmed-meshheading:7687928-Microscopy, Electron,
pubmed-meshheading:7687928-Phosphorylation,
pubmed-meshheading:7687928-Phosphotyrosine,
pubmed-meshheading:7687928-Pituitary Gland,
pubmed-meshheading:7687928-Protein-Tyrosine Kinases,
pubmed-meshheading:7687928-Rats,
pubmed-meshheading:7687928-Rats, Sprague-Dawley,
pubmed-meshheading:7687928-Receptor, Insulin,
pubmed-meshheading:7687928-Tyrosine
|
| pubmed:year |
1993
|
| pubmed:articleTitle |
The hypophyseal pars tuberalis is enriched with distinct phosphotyrosine-containing proteins not detected in other areas of the brain and pituitary.
|
| pubmed:affiliation |
Anatomische Anstalt, Universität München, Germany.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|