Phosphoproteomic analysis of the human pituitary

  title={Phosphoproteomic analysis of the human pituitary},
  author={Sarka Beranova‐Giorgianni and Yingxin Zhao and Dominic M. Desiderio and Francesco Giorgianni},
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… 
Proteomics of the human pituitary tissue: bioanalytical methods and applications.
The main features of the bioanalytical workflows used in pituitary proteomics are described, and major applications in pituitsary proteome mapping, differential protein expression profiling in health and disease, and discovery of post-translational modifications in Pituitary proteins are summarized.
Mass Spectrometry: Applications in Phosphoproteomics
Characterization of the phosphoproteomes in cells, tissues and biological fluids provides an excellent foundation on which to build new knowledge of living systems.
Characterization of the phosphoproteome in LNCaP prostate cancer cells by in-gel isoelectric focusing and tandem mass spectrometry.
The application of in-gel IEF LC-MS/MS to the mapping of the phosphoproteome in the LNCaP human prostate cancer cell line is reported on, which attests to the power of the chosen analytical methodology.
Phosphoproteome mapping of cardiomyocyte mitochondria in a rat model of heart failure
The phosphoprotein panel discovered in this study provides a foundation for future differential phosphoproteome profiling toward an integrated understanding of the role of mitochondrial phosphorylation in heart failure.
Phosphoproteome analysis by in-gel isoelectric focusing and tandem mass spectrometry.
This chapter describes an in-gel isoelectric focusing-liquid chromatography-tandem mass spectrometry (IEF-LC-MS/MS) analytical strategy for phosphoproteome mapping that identifies the phosphopeptides/proteins through database searches, and assignment of the sites of phosphorylation in these proteins.
Proteome Analysis of Subsarcolemmal Cardiomyocyte Mitochondria: A Comparison of Different Analytical Platforms
Results of this study provide a large-scale view of the proteome in subsarcolemmal mitochondria from the rat heart, and aid in the selection of optimal bioanalytical platforms for differential protein expression profiling of mitochondria in health and disease.
Technologies and challenges in large‐scale phosphoproteomics
Methods for state‐of‐the‐art MS‐based analysis of protein phosphorylation as well as the strategies employed in large‐scale phosphoproteomic experiments are described with focus on the various challenges and limitations this field currently faces.


Identification and characterization of phosphorylated proteins in the human pituitary
This work reports on the application of a liquid chromatography‐tandem mass spectrometry (MS/MS) based approach to detect and characterize phosphorylated proteins in a whole human pituitary digest, and identified several previously undescribed phosphorylation peptides.
Analysis of the proteome in the human pituitary
The application of proteomics for the mapping of major proteins in a normal (control) pituitary and establishes a two‐dimensional reference database of the human pituitaries, which will serve as a tool for further proteomics studies of pituitsary protein expression in health and disease.
Proteomics and Transcriptomics Analyses of Secretagogin Down-Regulation in Human Non-Functional Pituitary Adenomas
Results suggest that secretagogin might play a role in human non-functional pituitary adenomas, and may provide clues to clarify the basic molecular mechanisms of pituitARY adenoma formation, and to identify new tumor-related markers.
Toward a global analysis of the human pituitary proteome by multiple gel-based technology.
Categorization of the identified proteins revealed that MGT provides an excellent and largely unbiased access to proteins with diverse characteristics, including low-abundance proteins, membrane proteins, and proteins with extremes in pI and MW.
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This work reports the use of a mass spectrometry-based methodology permitting the first proteomic-scale phosphorylation site analysis of primary animal tissue, identifying over 500 proteinosphorylation sites in the developing mouse brain.
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  • G. Baumann
  • Biology, Medicine
    Hormone Research in Paediatrics
  • 1999
A highly heterogeneous mixture of GH fragments has been demonstrated and the implications of this heterogeneity relate to differences between GH immunoassays, such that assay results cannot be compared between laboratories.
Synthesis and secretion of phosphorylated growth hormone by rat pituitary glands in vitro.
A reference map of a human pituitary adenoma proteome
The two‐dimensional gel electrophoresis (2‐DE) reference map of a pituitary adenoma tissue proteome is described here and a good reproducibility of the 2‐D gel pattern was attained.
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A combined theoretical and experimental approach for the analysis of Septin 2 (Sept2) monophosphorylation in vivo is presented, raising the possibility that different septins may undergo distinct phosphorylation events that could control their functions in important cellular processes such as neurotransmission or cytokinesis.
Characterization and location of post‐translational modifications on chromogranin B from bovine adrenal medullary chromaffin granules
Using a combination of proteomic techniques including two‐dimensional gel electrophoresis, Western blot, high‐performance liquid chromatography purification, enzymatic digestion, sequencing, carbohydrate analysis, matrix‐assisted laser desorption/ionization‐time of flight and liquid Chromatography mass spectrometry analysis, 18 post‐translational modifications on bovine CGB are located.