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Short N-terminal galanin fragments are occurring naturally in vivo
Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Medicine and Health Sciences.ORCID iD: 0000-0001-5751-3622
Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Medicine and Health Sciences. Region Östergötland, Center for Diagnostics, Department of Clinical Chemistry.
2017 (English)In: Neuropeptides, ISSN 0143-4179, E-ISSN 1532-2785, Vol. 63Article in journal (Refereed) Published
Abstract [en]

The galanin family currently consists of four peptides, namely galanin, galanin-message associated peptide, galanin-like peptide and alarin. Unlike galanin that signals through three different G protein-coupled receptors; GALL, GAL(2), and GAL(3), binding at its N-terminal end, the cognate receptors for other members of the galanin family are currently unknown. Research using short N-terminal galanin fragments generated either by enzymatic cleavage or solid-phase synthesis has revealed differences in their receptor binding properties exerting numerous biological effects distinct from galanin(1-29) itself. Our studies on tissue extracts derived from rat small intestine and bovine gut using chromatographic techniques and sensitive galanin(1-16)-specific radioimmunoassay revealed the presence of immunoreactive compounds reacting with antiserum against galanin(1-16) distributed in distinct elution volumes. These results suggested a possible presence of short N-terminal galanin fragments also in vivo. Moreover, employing immunoaffinity chromatography and reverse-phase high performance liquid chromatography (HPLC) followed by mass spectrometry allowed specific enrichment of these immunoreactive compounds from rat tissues and identification of their molecular structure. Indeed, our study revealed presence of several distinct short N-terminal galanin sequences in rat tissue. To prove their receptor binding, four of the identified sequences were synthetized, namely, galanin(1-13), galanin(1-16), galanin(1.20), galanin(6-20), and tested on coronal rat brain sections competing with I-125-labeled galanin(1-29). Our autoradiographs confirmed that galanin(1-13), galanin(1-16), and galanin(1-20) comprehensively displaced I-125-galanin(1-29) but galanin (6-20) did not. Here we show, for the first time, that short N-terminal galanin fragments occur naturally in rat tissues and that similar or identical galanin sequences can be present also in tissues of other species. Biological significance: This study is first to provide an evidence of the presence of short N-terminal galanin fragments in vivo in a biological system and provides further foundations for the previous studies using synthetized short N-terminal galanin fragments.

Place, publisher, year, edition, pages
Churchill Livingstone , 2017. Vol. 63
Keyword [en]
Galanin; Receptor; Neuropeptide; Affinity chromatography; High-performance liquid chromatography (HPLC); Mass spectrometry (MS); Post-translational modification (PTM); Autoradiography
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:liu:diva-139625DOI: 10.1016/j.npep.2017.03.005ISI: 000405880200001PubMedID: 28434790Scopus ID: 2-s2.0-85018571577OAI: oai:DiVA.org:liu-139625DiVA: diva2:1133721
Note

Funding Agencies|County Council of Ostergotland

Available from: 2017-08-16 Created: 2017-08-16 Last updated: 2017-09-08Bibliographically approved

Open Access in DiVA

The full text will be freely available from 2018-04-07 15:02
Available from 2018-04-07 15:02

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CiteExportLink to record
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