Research Article

Identification and characterization of phosphorylated proteins in the human pituitary

  1. Francesco Giorgianni1,
  2. Sarka Beranova-Giorgianni1,2,3,4,
  3. Dominic M. Desiderio1,2,3,*

Article first published online: 17 SEP 2003

DOI: 10.1002/pmic.200300584

Issue

PROTEOMICS

PROTEOMICS

Volume 4, Issue 3, pages 587–598, March 2004

Additional Information

How to Cite

Giorgianni, F., Beranova-Giorgianni, S. and Desiderio, D. M. (2004), Identification and characterization of phosphorylated proteins in the human pituitary. PROTEOMICS, 4: 587–598. doi: 10.1002/pmic.200300584

Author Information

  1. 1

    The Charles B. Stout Neuroscience Mass Spectrometry Laboratory

  2. 2

    The Departments of Neurology

  3. 3

    Molecular Sciences

  4. 4

    Pharmaceutical Sciences, University of Tennessee Health Science Center, Memphis, TN, USA

*University of Tennessee Health Science Center, 847 Monroe Avenue, Room 117, Memphis, TN 38163, USA Fax: +1-901-448-7842

Publication History

  1. Issue published online: 19 FEB 2004
  2. Article first published online: 17 SEP 2003
  3. Manuscript Received: 4 MAR 2003

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Keywords:

  • Liquid chromatography-mass spectrometry;
  • Phosphoprotein;
  • Pituitary;
  • Post-translational modification

Abstract

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 phosphorylated precursor ion, we identified several previously undescribed phosphorylated peptides. The identified peptides were matched to the sequences of six pituitary proteins: the human growth hormone, chromogranin A, secretogranin I, 60S ribosomal protein P1 and/or P2, DnaJ homolog subfamily C member 5, and galanin. The phosphorylation sites of these important regulatory proteins were determined by MS/MS and MS3 analysis.

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