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http://purl.uniprot.org/citations/16910874http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16910874http://www.w3.org/2000/01/rdf-schema#comment"

Context

Although it is well established that thyrotropin (TSH) initiates signal transduction systems resulting in protein kinase(s) activation, the phosphorylated targets have not been fully characterized.

Objective/design

In FRTL-5 thyroid cells, we used two-dimensional (2D) gel images of silver-stained proteins isolated from FRTL-5 thyroid cells following TSH stimulation to identify potential phosphorylation targets.

Results

We characterized a 90 kDa protein that had undergone a pH shift and subsequently identified it as heat shock protein-90 (hsp-90) following in-gel trypsin digestion and mass spectroscopy. This was confirmed by Western blot using a monoclonal antibody against hsp-90. Western blot analysis of the 2D gel images using a polyclonal antibody directed at phosphoserine/threonine sites showed that TSH induced the phosphorylation of hsp-90. Western blotting of hsp-90 following stimulators of the signal transduction systems mediated by TSH indicated that TSH-mediated hsp-90 phosphorylation occurs through protein kinases A and C.

Conclusion

In summary, we have demonstrated that TSH action stimulates the phosphorylation of hsp-90 in FRTL-5 thyroid cells. Abnormalities of hsp-90 phosphorylation may be a mediator in the development of thyroid disease."xsd:string
http://purl.uniprot.org/citations/16910874http://purl.org/dc/terms/identifier"doi:10.1089/thy.2006.16.737"xsd:string
http://purl.uniprot.org/citations/16910874http://purl.uniprot.org/core/author"Ginsberg J."xsd:string
http://purl.uniprot.org/citations/16910874http://purl.uniprot.org/core/author"Brindley D.N."xsd:string
http://purl.uniprot.org/citations/16910874http://purl.uniprot.org/core/author"Labedz T."xsd:string
http://purl.uniprot.org/citations/16910874http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16910874http://purl.uniprot.org/core/name"Thyroid"xsd:string
http://purl.uniprot.org/citations/16910874http://purl.uniprot.org/core/pages"737-742"xsd:string
http://purl.uniprot.org/citations/16910874http://purl.uniprot.org/core/title"Phosphorylation of heat shock protein-90 by TSH in FRTL-5 thyroid cells."xsd:string
http://purl.uniprot.org/citations/16910874http://purl.uniprot.org/core/volume"16"xsd:string
http://purl.uniprot.org/citations/16910874http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16910874
http://purl.uniprot.org/citations/16910874http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16910874
http://purl.uniprot.org/uniprot/#_A0A0F7RQR3-mappedCitation-16910874http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16910874
http://purl.uniprot.org/uniprot/#_A6K3J3-mappedCitation-16910874http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16910874
http://purl.uniprot.org/uniprot/#_P04652-mappedCitation-16910874http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16910874
http://purl.uniprot.org/uniprot/A6K3J3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16910874
http://purl.uniprot.org/uniprot/A0A0F7RQR3http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16910874
http://purl.uniprot.org/uniprot/P04652http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16910874