Identification and characterization of phosphorylated proteins in the human pituitary

Francesco Giorgianni, Sarka Beranova, Dominic M. Desiderio

Research output: Contribution to journalArticle

54 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)587-598
Number of pages12
JournalProteomics
Volume4
Issue number3
DOIs
StatePublished - Mar 1 2004

Fingerprint

Chromogranin B
Galanin
Chromogranin A
Peptides
Proteins
Human Growth Hormone
Pituitary Gland
Post Translational Protein Processing
Tandem Mass Spectrometry
Liquid Chromatography
Phosphorylation
Liquid chromatography
Metals
Ions
Mass spectrometry
ribosomal phosphoprotein P2
phosphoric acid
ribosomal phosphoprotein P1

All Science Journal Classification (ASJC) codes

  • Genetics
  • Molecular Biology

Cite this

Identification and characterization of phosphorylated proteins in the human pituitary. / Giorgianni, Francesco; Beranova, Sarka; Desiderio, Dominic M.

In: Proteomics, Vol. 4, No. 3, 01.03.2004, p. 587-598.

Research output: Contribution to journalArticle

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