Identification and characterization of phosphorylated proteins in the human pituitary

  title={Identification and characterization of phosphorylated proteins in the human pituitary},
  author={Francesco Giorgianni and Sarka Beranova‐Giorgianni and Dominic M. Desiderio},
Post‐translational modifications of proteins from the human pituitary gland play an important role in the regulation of different body functions. We report 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. By combining an immobilized metal affinity column‐based enrichment method with MS/MS conditions that favor the neutral loss of phosphoric acid from a… 
Phosphoproteomic analysis of the human pituitary
The application of the in-gel IEF-LC-MS/MS approach to the study of the pituitary phosphoproteome provides a direct glimpse into the phosphoprotein machinery operating within the human pituitsary tissue microenvironment.
Characterisation of protein phosphorylation in Arabidopsis thaliana and Chlamydomonas reinhardtii based on affinity chromatography and mass spectrometry
In a targeted analysis the speculative in vivo phosphorylation site of the metabolic key enzyme phosphoenolpyruvate carboxylase in A. thaliana could be confirmed and the results indicate that temperature has a profound effect on the phosphorylated level of SPS by influencing the activity or abundance of the kinase responsible for SPSosphorylation.
Proteomics analysis of growth hormone isoforms in the human pituitary
The results provide novel clues for further studies of the functions, and mechanisms of action, of hGH in the human pituitary and in growth hormone‐related diseases.
An integrated strategy for identification and relative quantification of site-specific protein phosphorylation using liquid chromatography coupled to MS2/MS3.
Site-specific differential in vitro phosphorylation of native protein was demonstrated after incubation of the recombinant protein with cold-adapted plant leaf extracts from A. thaliana, suggesting regulatory phosphorylated events of this key enzyme under stress response.
Neuroendocrine Protein 7B2 Can Be Inactivated by Phosphorylation within the Secretory Pathway*
It is determined that 7B2 can be phosphorylated in Rin cells and cultured chromaffin cells, but not in AtT-20 cells, and it is suggested that this may be analogous to the phosphorylating inactivation of BiP, which impairs its ability to bind substrate.
Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites.
This study reveals the practicality of liquid chromatography-mass spectrometry(n) neutral loss scanning for large-scale identification and quantification of protein phosphorylation in the analysis of cell signaling in a native mammalian system.
Toward a global characterization of the phosphoproteome in prostate cancer cells: Identification of phosphoproteins in the LNCaP cell line
A fully non‐gel‐based methodology was applied to obtain an initial panel of phosphoproteins from the LNCaP human prostate cancer cell line, and 137 phosphorylation sites in 81 phosphiproteins were identified.
Combining metal oxide affinity chromatography (MOAC) and selective mass spectrometry for robust identification of in vivo protein phosphorylation sites
A novel phosphoprotein enrichment procedure MOAC was applied to seed proteins of A. thaliana and to proteins extracted from C. reinhardtii, providing high confidence in the identification of phosphoproteins and their corresponding phosphorylation sites and is proposed as a strategy adaptable to other plant tissues.