Conclusions: These studies show for the first time the localization of a H+/peptide cotrasporter in nuclei of vascular smooth muscle cells and Schwann cells and its localization in lysosomes of the exocrine pancreas. It is likely that the transporter functions to move small peptides from the lysosome to the cytoplasm following intralysosomal protein degradation. The nature of the transporter function in the nucleus remains to be determined, including the possibility that peptide signaling molecules may be transmitted between nucleus and cytoplasm.
Background: PEPT1 transports di- and tripeptides through plasma membranes. Peptides are cotransported with H+, thus deriving the energy for the active transport process from an electrochemical H+ gradient. The main regions in which PEPT1 has been thought to function are the plasma membranes of the small intestinal epithelial cells for absorption of protein digestion products and in the kidney tubules for recovery of small peptides from the glomerular filtrate.
Methods: Pancreas was removed from rats and quick frozen with liquid nitrogen. Frozen sections were fixed in cold acetone. Sections were incubated with primary antibody against PEPT1, followed by a secondary antibody conjugated with fluorescein, then examined with a fluorescence microscope.
Results: Three major structures were immunopositive with the antibody to PEPT1: the nuclei of smooth muscle cells in the wall of arterioles, the nuclei of Schwann cells in unmyelinated pancreatic nerves, and lysosomes in acinar cells.