Conclusion
In the present study we demonstrated the presence of the high-affinity, low capacity peptide transporter PEPT2 at the translational level in dorsal root ganglia of the species guinea pig by employing immunohistochemistry. This finding provides new insights into the fate of peptide fragments, following DPP IV-mediated proteolysis. The results indicate, that the fragments may be re-utilized via uptake mechanisms in the peripheral nervous system of the guinea pig. For the rat nervous system, several studies demonstrated the presence of the transporter mRNA in nervous system astrocytes, satellite cells, subependymal cells, ependymal cells and cells of the choroid plexus6.7.
The expression of the transporter in glial cells of the guinea pig peripheral nervous system (PNS) suggests a role of the transporter within the intraganglionic neuropeptide metabolism. Apart from a role of the transporter as a scavenging system for DPP IV products, the carrier may also catalyze the uptake of biologically active short chain peptides such as carnosine, or the neuropeptide N-acetylaspartateglutamate (NAAG9) and thyreotropin releasing hormone (TRH, Glu-His-Pro10).
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Thai Dinh, Q., Peiser, C., Fischer, A., Groneberg, D.A. (2004). Re-Uptake Mechanisms of Peptide Fragments after DPP IV-Mediated Proteolysis in the Peripheral Nervous System. In: Back, N., Cohen, I.R., Kritchevsky, D., Lajtha, A., Paoletti, R. (eds) Dipeptidyl Aminopeptidases in Health and Disease. Advances in Experimental Medicine and Biology, vol 524. Springer, Boston, MA. https://doi.org/10.1007/0-306-47920-6_9
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DOI: https://doi.org/10.1007/0-306-47920-6_9
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