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

Frontiers in Endocrinology
Akikazu YasudaYasushi Shigeri

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 α-melanocyte-stimulating hormone (MSH), hydroxylation of a proline residue in β-MSH, and the phosphorylated form of corticotropin-like intermediate lobe peptide.

Citations

Mar 19, 2014·Frontiers in Endocrinology·Sho KakizawaAkiyoshi Takahashi
Oct 12, 2016·Experimental and Molecular Pathology·Rafael Carvalho TorresVinicius F Carvalho

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Methods Mentioned

BETA
acetylation
amidation
CLIP
phospho-CLIP

Software Mentioned

LAMMA

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