Search for substrates for prolyl oligopeptidase in porcine brain.
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.
Brandt
Inger
I
Laboratory of Medical Biochemistry, Department of Pharmaceutical Sciences, University of Antwerp, Universiteitsplein 1, 2610 Wilrijk, Belgium.
De Vriendt
Kris
K
Devreese
Bart
B
Van Beeumen
Jozef
J
Van Dongen
Walter
W
Augustyns
Koen
K
De Meester
Ingrid
I
Scharpé
Simon
S
Lambeir
Anne-Marie
AM
D000818:Animals; D001921:Brain / Q000201:enzymology*; D001923:Brain Chemistry; D010455:Peptides / Q000737:chemistry*; D000085822:Prolyl Oligopeptidases; D011994:Recombinant Proteins / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry*; D013552:Swine; D014020:Tissue Extracts / Q000737:chemistry
D010455:Peptides; D011994:Recombinant Proteins; D014020:Tissue Extracts; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases