Di- and tripeptide transport in vertebrates: the contribution of teleost fish models.
Solute Carrier 15 (SLC15) family, alias H+-coupled oligopeptide cotransporter family, is a group of membrane transporters known for their role in the cellular uptake of di- and tripeptides (di/tripeptides) and peptide-like molecules. Of its members, SLC15A1 (PEPT1) chiefly mediates intestinal absorption of luminal di/tripeptides from dietary protein digestion, while SLC15A2 (PEPT2) mainly allows renal tubular reabsorption of di/tripeptides from ultrafiltration, SLC15A3 (PHT2) and SLC15A4 (PHT1) possibly interact with di/tripeptides and histidine in certain immune cells, and SLC15A5 has unknown function. Our understanding of this family in vertebrates has steadily increased, also due to the surge of genomic-to-functional information from 'non-conventional' animal models, livestock, poultry, and aquaculture fish species. Here, we review the literature on the SLC15 transporters in teleost fish with emphasis on SLC15A1 (PEPT1), one of the solute carriers better studied amongst teleost fish because of its relevance in animal nutrition. We report on the operativity of the transporter, the molecular diversity, and multiplicity of structural-functional solutions of the teleost fish orthologs with respect to higher vertebrates, its relevance at the intersection of the alimentary and osmoregulative functions of the gut, its response under various physiological states and dietary solicitations, and its possible involvement in examples of total body plasticity, such as growth and compensatory growth. By a comparative approach, we also review the few studies in teleost fish on SLC15A2 (PEPT2), SLC15A4 (PHT1), and SLC15A3 (PHT2). By representing the contribution of teleost fish to the knowledge of the physiology of di/tripeptide transport and transporters, we aim to fill the gap between higher and lower vertebrates.
Laboratory of General Physiology, Department of Biological and Environmental Sciences and Technologies, University of Salento, Via Provinciale Lecce-Monteroni, 73100, Lecce, Italy. tiziano.verri@unisalento.it.
Tiziano
T
Verri
Laboratory of General Physiology, Department of Biological and Environmental Sciences and Technologies, University of Salento, Via Provinciale Lecce-Monteroni, 73100, Lecce, Italy.
Amilcare
A
Barca
Institute of Clinical Physiology, Italian National Research Council, Lecce, Italy.
Paola
P
Pisani
Laboratory of General Physiology, Department of Biological and Environmental Sciences and Technologies, University of Salento, Via Provinciale Lecce-Monteroni, 73100, Lecce, Italy.
Barbara
B
Piccinni
Laboratory of General Physiology, Department of Biological and Environmental Sciences and Technologies, University of Salento, Via Provinciale Lecce-Monteroni, 73100, Lecce, Italy.
Carlo
C
Storelli
Neuropathology Unit, Institute of Experimental Neurology and Division of Neuroscience, IRCCS San Raffaele Scientific Institute, Milan, Italy.
Alessandro
A
Romano
D000818:Animals; D029941:Fish Proteins / Q000378:metabolism*; D005399:Fishes / Q000378:metabolism*; D006801:Humans; D023421:Models, Animal; D009842:Oligopeptides / Q000378:metabolism*; D027981:Symporters / Q000378:metabolism*
D029941:Fish Proteins; D009842:Oligopeptides; D027981:Symporters
Adaptation; Circadian rhythms; Compensatory growth; Dietary protein; Digestive physiology; Epithelial physiology; Fasting; Feeding; Food deprivation; Growth; Immune system physiology; Ontogeny; Osmoregulation; Peptide absorption; Peptide transport; Protein digestion; Renal physiology