Phosphoproteomic analysis of the human pituitary.

Article Details

Citation

Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F

Phosphoproteomic analysis of the human pituitary.

Pituitary. 2006;9(2):109-20.

PubMed ID
16807684 [ View in PubMed
]
Abstract

The pituitary is the central endocrine gland that regulates the functions of various target organs in the human body. Because of the pivotal regulatory role of the pituitary, it is essential to define on a global scale the components of the pituitary protein machinery, including a comprehensive characterization of the post-translational modifications of the pituitary proteins. Of particular interest is the examination of the phosphorylation status of the pituitary in health and disease. Towards the goal of global profiling of pituitary protein phosphorylation, we report here the application of the in-gel IEF-LC-MS/MS approach to the study of the pituitary phosphoproteome. The analytical strategy combined isoelectric focusing in immobilized pH gradient strips with immobilized metal ion affinity chromatography and mass spectrometry. With this method, a total of 50 phosphorylation sites were characterized in 26 proteins. Because the investigation involved primary tissue, the findings provide a direct glimpse into the phosphoprotein machinery operating within the human pituitary tissue microenvironment.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Fibrinogen alpha chainP02671Details
Pro-opiomelanocortinP01189Details
VitronectinP04004Details
Heat shock protein HSP 90-alphaP07900Details
Prostaglandin E synthase 3Q15185Details
cAMP-dependent protein kinase type II-alpha regulatory subunitP13861Details
Triosephosphate isomeraseP60174Details
Hepatoma-derived growth factorP51858Details