the multiplicity of post-translational modifications in pro-opiomelanocortin-derived peptides

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ID: 133822
2013
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Abstract
The precursor protein, pro-opiomelanocortin (POMC) undergoes extensive post-translational processing in a tissue-specific manner to yield various biologically active peptides involved in diverse cellular functions. The recently developed method of matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) for direct tissue analysis has proved to be a powerful tool for investigating the distribution of peptides and proteins. In particular, topological mass spectrometry analysis using MALDI-MS can selectively provide a mass profile of the hormones included in cell secretory granules. An advantage of this technology is that it is possible to analyze a frozen thin slice section, avoiding an extraction procedure. Subsequently, tandem mass spectrometry (MS/MS) has a profound impact on addressing the modified residues in the hormone molecules. Based on these strategies with mass spectrometry, several interesting molecular forms of POMC-derived peptides have been found in the fish pituitary, such as novel sites of acetylation in -melanocyte-stimulating hormone (MSH), hydroxylation of a proline residue in -MSH, and the phosphorylated form of corticotropin-like intermediate lobe peptide (CLIP).
Reference Key
eyasuda2013frontiersthe Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Akikazu eYasuda;Leslie Sargent Jones;Yasushi eShigeri
Journal aip advances
Year 2013
DOI
10.3389/fendo.2013.00186
URL
http://journal.frontiersin.org/Journal/10.3389/fendo.2013.00186/full
Keywords
pomc post-translational modification end clinical endocrinology topological mass spectrometry analysisdiseases of the endocrine glands

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