the multiplicity of post-translational modifications in pro-opiomelanocortin-derived peptides
Clicks: 236| ID | 133822 |
|---|---|
| Ref. Key (ref-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 |
| 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). |
| Raw Reference | |
| Journal Name | aip advances |
| Published | in : 2013 with DOI : 10.3389/fendo.2013.00186 on pages: - |
| Citations | Citations not found |
| URL |
Link:
10.3389/fendo.2013.00186
|
| Keywords | pomc; post-translational modification; end; clinical endocrinology; topological mass spectrometry analysisdiseases of the endocrine glands; |
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