Distribution of tripeptidyl-peptidase II in the central nervous system of rat.
Tripeptidyl-peptidase II (TPP II) is a high molecular weight serine peptidase which removes tripeptides from a free N-terminus of longer peptides. Since it had previously been demonstrated that the enzyme can inactivate enkephalins and dynorphins in vitro by removing the N-terminal Tyr-Gly-Gly peptide, we wanted to see whether TPP II could be involved in this process also in vivo. Therefore, the localization of TPP II in different cerebral regions of rat was investigated by immunoblot analysis and activity measurements. It could be shown that TPP II is relatively evenly distributed in the central nervous system of rat. This indicates that the physiological role of the enzyme is probably not a specific degradation of enkephalins, but rather pertains to the general turnover of proteins.
Tomkinson
B
B
Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, Uppsala.
Nyberg
F
F
D000595:Amino Acid Sequence; D000626:Aminopeptidases; D000818:Animals; D001921:Brain / Q000201:enzymology*; D002531:Cerebellum / Q000201:enzymology; D003342:Corpus Striatum / Q000201:enzymology; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D005625:Frontal Lobe / Q000201:enzymology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007031:Hypothalamus / Q000201:enzymology; D015151:Immunoblotting; D008099:Liver / Q000201:enzymology; D008297:Male; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D012697:Serine Endopeptidases / Q000032:analysis* / Q000134:cerebrospinal fluid / Q000378:metabolism; D013116:Spinal Cord / Q000201:enzymology*; D014018:Tissue Distribution
D010446:Peptide Fragments; D000626:Aminopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C048001:tripeptidyl-peptidase 2; D012697:Serine Endopeptidases