Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1989-4-13
|
pubmed:abstractText |
Treatment of AR4-2J cells with dexamethasone at 10 nM for 96 h inhibited cell replication by 75% and increased cell size (30%), protein content (1.6-fold) and protein synthesis (2-fold). The increase in protein synthesis was largely due to a 5 to 10-fold increase in the synthesis of secretory proteins. Amylase activity increased 20 to 30-fold in cellular homogenates and 10 to 20-fold in culture medium. Both in the presence and absence of dexamethasone AR4-2J cells release their secretory proteins by constitutive secretion. The proportion of newly synthesized amylase retained by the cells over the 14 h labeling period increased from 15 to 30% with hormone treatment. As judged by comigration on polyacrylamide gels and Western blots analyzed by immunospecific sera, AR4-2J cells synthesize and secrete the majority of known pancreatic secretory proteins. Dexamethasone increased the synthesis of trypsinogen 12 to 16-fold, chymotrypsinogen 4.5 to 6-fold, the group of procarboxypeptidases 6-fold, and amylase 7 to 10-fold. Messenger RNA levels for trypsinogen, amylase and lipase were each increased 4 to 5-fold. At the ultrastructural level dexamethasone led to significant increases in rough endoplasmic reticulum (RER) (30-fold) and Golgi elements (1.5-fold) and to the de novo appearance of electron-opaque granules (0.1-0.5 microns) which were shown to contain amylase by immunolocalization techniques employing protein A-gold. Dexamethasone also led to the formation of gap junctions between AR4-2J cells. These findings indicate that AR4-2J cells provide a model for differentiation of pancreatic acinar cells which should also be studied for the differentiation markers for the regulated secretory pathway.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amylases,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Chymotrypsinogen,
http://linkedlifedata.com/resource/pubmed/chemical/Glucocorticoids,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trypsinogen
|
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0171-9335
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
47
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
101-11
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:2465895-Amylases,
pubmed-meshheading:2465895-Animals,
pubmed-meshheading:2465895-Carboxypeptidases,
pubmed-meshheading:2465895-Carcinoma,
pubmed-meshheading:2465895-Cell Line,
pubmed-meshheading:2465895-Chymotrypsinogen,
pubmed-meshheading:2465895-Cytoplasmic Granules,
pubmed-meshheading:2465895-Endoplasmic Reticulum,
pubmed-meshheading:2465895-Glucocorticoids,
pubmed-meshheading:2465895-Golgi Apparatus,
pubmed-meshheading:2465895-Microscopy, Electron,
pubmed-meshheading:2465895-Neoplasm Proteins,
pubmed-meshheading:2465895-Pancreatic Neoplasms,
pubmed-meshheading:2465895-Rats,
pubmed-meshheading:2465895-Trypsinogen,
pubmed-meshheading:2465895-Tumor Cells, Cultured
|
pubmed:year |
1988
|
pubmed:articleTitle |
Coupled induction of exocrine proteins and intracellular compartments involved in the secretory pathway in AR4-2J cells by glucocorticoids.
|
pubmed:affiliation |
Laboratory for Cell Biology and Cell Pathology, University of Marburg/Federal Republic of Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|