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Search for substrates for prolyl oligopeptidase in porcine brain |
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| Authors: | Brandt Inger De Vriendt Kris Devreese Bart Van Beeumen Jozef Van Dongen Walter Augustyns Koen De Meester Ingrid Scharpé Simon Lambeir Anne-Marie |
| Institution: | aLaboratory of Medical Biochemistry, Department of Pharmaceutical Sciences, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium bLaboratory for Protein Biochemistry and Protein Engineering, University of Gent, KL Ledeganckstraat 35, 9000 Gent, Belgium cCenter for Mass Spectrometry and Proteome Analysis, University of Antwerp, Groenenborgerlaan 171, 2020 Antwerpen, Belgium dLaboratory of Medicinal Chemistry, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium |
| Abstract: | The function of prolyl oligopeptidase (PO) has been associated with several disorders of the central nervous system. The purpose of this study was to identify endogenous substrates for recombinant porcine PO in porcine brain. The smaller polypeptides were extracted from total brain homogenates and fractionated by two-dimensional chromatography prior to incubation with PO. Shifts in the mass spectrum between the control and the incubated sample, marked potential substrates. Using MSMS peptide sequencing techniques, we identified several fragments of intracellular proteins as potential substrates, which opens new perspectives for finding the function of PO in the intracellular space. |
| Keywords: | Prolyl oligopeptidase Brain Peptidomics 2D chromatography Mass spectrometry |
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