The Experts below are selected from a list of 37431 Experts worldwide ranked by ideXlab platform
Heikki Vapaatalo - One of the best experts on this subject based on the ideXlab platform.
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cardiovascular activity of milk casein derived Tripeptides and plant sterols in spontaneously hypertensive rats
Journal of Physiology and Pharmacology, 2009Co-Authors: Pauliina Jäkälä, Anu M. Turpeinen, Eve Péré, Risto Lehtinen, Riitta Korpela, Heikki VapaataloAbstract:: The effect of chronic treatment with fermented milk products containing bioactive Tripeptides and plant sterols on blood pressure and vascular function was investigated in spontaneously hypertensive rats (SHR). Six-weeks old male SHR (n=36) were randomized into 4 groups by body weight and blood pressure to receive either Lactobacillus helveticus fermented standard milk product (containing Tripeptides Ile-Pro-Pro, Val-Pro-Pro and Leu-Pro-Pro), test product with enzymatically produced Tripeptides without or with plant sterols or control product without the active constituents for 8 weeks. Systolic blood pressure (SBP) was measured weekly using the tail-cuff method. Thoracic aorta and mesenteric artery were excised for vascular response measurements. At the end, SBP values vs. control product group were: standard product group -14 mmHg (P<0.05), test product group -12 mmHg and test product +sterols group -7 mmHg. The average daily Tripeptide dose was 2.8-5.2 mg/kg. Total serum cholesterol in the test product +sterols group tended to be lower than in the test product group (P=0.10) whereas serum plant sterol (campesterol, sitosterol) concentrations were higher (P<0.001). In conclusion, bioactive Tripeptide-containing milk products attenuated the blood pressure development in SHR. The plant sterols did not improve this effect. Vascular responses did not markedly differ between the groups, except that endothelium-derived hyperpolarizing factor (EDHF) -related aortic relaxation was demonstrated in the test product +sterols group.
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casein derived bioactive Tripeptides ile pro pro and val pro pro attenuate the development of hypertension and improve endothelial function in salt loaded goto kakizaki rats
Journal of Functional Foods, 2009Co-Authors: Pauliina Jäkälä, Anne Hakala, Anu M. Turpeinen, Riitta Korpela, Heikki VapaataloAbstract:Abstract Increased blood pressure and plasma cholesterol concentration are the major risk factors for cardiovascular diseases. We have previously shown that fermented milk products containing casein-derived bioactive Tripeptides, isoleucine-proline-proline (Ile-Pro-Pro) and valine-proline-proline (Val-Pro-Pro) partly inhibit the blood pressure increase in spontaneously hypertensive rats (SHR). In the present study, we investigated the effect of bioactive Tripeptide-containing fermented milk products (with or without plant sterols) on blood pressure and vascular function in salt-loaded type 2 diabetic Goto–Kakizaki (GK) rats after 8 weeks’ treatment. The development of blood pressure was attenuated in the groups receiving Tripeptide-containing products (−10 to −12 mmHg vs. the control product group, P
Janne E. Tønder - One of the best experts on this subject based on the ideXlab platform.
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pyrrolidinone modified di and Tripeptides highly diastereoselective preparation and investigation of their stability
Organic and Biomolecular Chemistry, 2007Co-Authors: Anthony Murray, David Tanner, Janne E. Tønder, Masood HosseiniAbstract:Pyrrolidine-2,4-diones have been identified as a novel starting point for the synthesis of peptide analogues. This paper describes a method for the efficient and diastereoselective incorporation of this moiety into peptide chains to furnish di- and Tripeptide analogs. The stability of these pyrrolidinone modified di- and Tripeptides was found to be markedly improved when compared to that of a natural peptide. In addition, solid phase peptide synthesis employing a pyrrolidinone containing Tripeptide is demonstrated.
Alessandro Romano - One of the best experts on this subject based on the ideXlab platform.
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Di- and Tripeptide transport in vertebrates: the contribution of teleost fish models
Journal of Comparative Physiology B, 2017Co-Authors: Tiziano Verri, Amilcare Barca, Barbara Piccinni, Carlo Storelli, Paola Pisani, Alessandro RomanoAbstract: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.
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Di- and Tripeptide transport in vertebrates: the contribution of teleost fish models
Journal of Comparative Physiology B, 2017Co-Authors: Tiziano Verri, Amilcare Barca, Barbara Piccinni, Carlo Storelli, Paola Pisani, Alessandro RomanoAbstract: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.
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transport of di and Tripeptides in teleost fish intestine
Aquaculture Research, 2010Co-Authors: Tiziano Verri, Amilcare Barca, Alessandro Romano, Hannelore Daniel, Gabor Kottra, Carlo StorelliAbstract:The initial observation of peptide absorption in fish intestine dates back to 1981, when, in rainbow trout (Oncorhynchus mykiss), the rate of intestinal absorption of the dipeptide glycylglycine (Gly-Gly) was compared in vivo with the rate of absorption of its component amino acid glycine (Gly). The description of the identification of the underlying mechanisms that allow di- and Tripeptide transport across the plasma membranes in fish was provided in 1991, when the first evidence of peptide transport activity was reported in brush-border membrane vesicles of intestinal epithelial cells of Mozambique tilapia (Oreochromis mossambicus) by monitoring uptake of radiolabelled glycyl-l-phenylalanine (Gly-l-Phe). Since then, the existence of a carrier-mediated, H+-dependent transport of di- and Tripeptides (H+/peptide cotransport) in the brush-border membrane of fish enterocytes has been confirmed in many teleost species by a variety of biochemical approaches, providing basic kinetics and substrate specificities of the transport activity. In 2003, the first peptide transporter from a teleost fish, i.e. the zebrafish (Danio rerio) PEPtide transporter 1 (PEPT1), was cloned and functionally characterized in the Xenopus laevis oocyte expression system as a low-affinity/high-capacity system. PEPT1 is the protein in brush-border membranes responsible for translocation of intact di- and Tripeptides released from dietary protein by luminal and membrane-bound proteases and peptidases. The transporter possesses affinities for the peptide substrates in the 0.1–10 mM range, depending on the structure and physicochemical nature of the substrates. After the molecular and functional characterization of the zebrafish transporter, the interest in PEPT1 in teleost fish has increased and approaches for cloning and functional characterization of PEPT1 orthologues from other fish species, some of them of the highest commercial value, are now underway. In this paper, we provide a brief overview of the transport of di- and Tripeptides in teleost fish intestine by recalling the bulk of biochemical, biophysical and physiological observations collected in the pre-cloning era and by recapitulating the more recent molecular and functional data.
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Transport of di‐ and Tripeptides in teleost fish intestine
Aquaculture Research, 2010Co-Authors: Tiziano Verri, Amilcare Barca, Alessandro Romano, Hannelore Daniel, Gabor Kottra, Carlo StorelliAbstract:The initial observation of peptide absorption in fish intestine dates back to 1981, when, in rainbow trout (Oncorhynchus mykiss), the rate of intestinal absorption of the dipeptide glycylglycine (Gly-Gly) was compared in vivo with the rate of absorption of its component amino acid glycine (Gly). The description of the identification of the underlying mechanisms that allow di- and Tripeptide transport across the plasma membranes in fish was provided in 1991, when the first evidence of peptide transport activity was reported in brush-border membrane vesicles of intestinal epithelial cells of Mozambique tilapia (Oreochromis mossambicus) by monitoring uptake of radiolabelled glycyl-l-phenylalanine (Gly-l-Phe). Since then, the existence of a carrier-mediated, H+-dependent transport of di- and Tripeptides (H+/peptide cotransport) in the brush-border membrane of fish enterocytes has been confirmed in many teleost species by a variety of biochemical approaches, providing basic kinetics and substrate specificities of the transport activity. In 2003, the first peptide transporter from a teleost fish, i.e. the zebrafish (Danio rerio) PEPtide transporter 1 (PEPT1), was cloned and functionally characterized in the Xenopus laevis oocyte expression system as a low-affinity/high-capacity system. PEPT1 is the protein in brush-border membranes responsible for translocation of intact di- and Tripeptides released from dietary protein by luminal and membrane-bound proteases and peptidases. The transporter possesses affinities for the peptide substrates in the 0.1–10 mM range, depending on the structure and physicochemical nature of the substrates. After the molecular and functional characterization of the zebrafish transporter, the interest in PEPT1 in teleost fish has increased and approaches for cloning and functional characterization of PEPT1 orthologues from other fish species, some of them of the highest commercial value, are now underway. In this paper, we provide a brief overview of the transport of di- and Tripeptides in teleost fish intestine by recalling the bulk of biochemical, biophysical and physiological observations collected in the pre-cloning era and by recapitulating the more recent molecular and functional data.
Carlo Storelli - One of the best experts on this subject based on the ideXlab platform.
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Di- and Tripeptide transport in vertebrates: the contribution of teleost fish models
Journal of Comparative Physiology B, 2017Co-Authors: Tiziano Verri, Amilcare Barca, Barbara Piccinni, Carlo Storelli, Paola Pisani, Alessandro RomanoAbstract: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.
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Di- and Tripeptide transport in vertebrates: the contribution of teleost fish models
Journal of Comparative Physiology B, 2017Co-Authors: Tiziano Verri, Amilcare Barca, Barbara Piccinni, Carlo Storelli, Paola Pisani, Alessandro RomanoAbstract: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.
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transport of di and Tripeptides in teleost fish intestine
Aquaculture Research, 2010Co-Authors: Tiziano Verri, Amilcare Barca, Alessandro Romano, Hannelore Daniel, Gabor Kottra, Carlo StorelliAbstract:The initial observation of peptide absorption in fish intestine dates back to 1981, when, in rainbow trout (Oncorhynchus mykiss), the rate of intestinal absorption of the dipeptide glycylglycine (Gly-Gly) was compared in vivo with the rate of absorption of its component amino acid glycine (Gly). The description of the identification of the underlying mechanisms that allow di- and Tripeptide transport across the plasma membranes in fish was provided in 1991, when the first evidence of peptide transport activity was reported in brush-border membrane vesicles of intestinal epithelial cells of Mozambique tilapia (Oreochromis mossambicus) by monitoring uptake of radiolabelled glycyl-l-phenylalanine (Gly-l-Phe). Since then, the existence of a carrier-mediated, H+-dependent transport of di- and Tripeptides (H+/peptide cotransport) in the brush-border membrane of fish enterocytes has been confirmed in many teleost species by a variety of biochemical approaches, providing basic kinetics and substrate specificities of the transport activity. In 2003, the first peptide transporter from a teleost fish, i.e. the zebrafish (Danio rerio) PEPtide transporter 1 (PEPT1), was cloned and functionally characterized in the Xenopus laevis oocyte expression system as a low-affinity/high-capacity system. PEPT1 is the protein in brush-border membranes responsible for translocation of intact di- and Tripeptides released from dietary protein by luminal and membrane-bound proteases and peptidases. The transporter possesses affinities for the peptide substrates in the 0.1–10 mM range, depending on the structure and physicochemical nature of the substrates. After the molecular and functional characterization of the zebrafish transporter, the interest in PEPT1 in teleost fish has increased and approaches for cloning and functional characterization of PEPT1 orthologues from other fish species, some of them of the highest commercial value, are now underway. In this paper, we provide a brief overview of the transport of di- and Tripeptides in teleost fish intestine by recalling the bulk of biochemical, biophysical and physiological observations collected in the pre-cloning era and by recapitulating the more recent molecular and functional data.
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Transport of di‐ and Tripeptides in teleost fish intestine
Aquaculture Research, 2010Co-Authors: Tiziano Verri, Amilcare Barca, Alessandro Romano, Hannelore Daniel, Gabor Kottra, Carlo StorelliAbstract:The initial observation of peptide absorption in fish intestine dates back to 1981, when, in rainbow trout (Oncorhynchus mykiss), the rate of intestinal absorption of the dipeptide glycylglycine (Gly-Gly) was compared in vivo with the rate of absorption of its component amino acid glycine (Gly). The description of the identification of the underlying mechanisms that allow di- and Tripeptide transport across the plasma membranes in fish was provided in 1991, when the first evidence of peptide transport activity was reported in brush-border membrane vesicles of intestinal epithelial cells of Mozambique tilapia (Oreochromis mossambicus) by monitoring uptake of radiolabelled glycyl-l-phenylalanine (Gly-l-Phe). Since then, the existence of a carrier-mediated, H+-dependent transport of di- and Tripeptides (H+/peptide cotransport) in the brush-border membrane of fish enterocytes has been confirmed in many teleost species by a variety of biochemical approaches, providing basic kinetics and substrate specificities of the transport activity. In 2003, the first peptide transporter from a teleost fish, i.e. the zebrafish (Danio rerio) PEPtide transporter 1 (PEPT1), was cloned and functionally characterized in the Xenopus laevis oocyte expression system as a low-affinity/high-capacity system. PEPT1 is the protein in brush-border membranes responsible for translocation of intact di- and Tripeptides released from dietary protein by luminal and membrane-bound proteases and peptidases. The transporter possesses affinities for the peptide substrates in the 0.1–10 mM range, depending on the structure and physicochemical nature of the substrates. After the molecular and functional characterization of the zebrafish transporter, the interest in PEPT1 in teleost fish has increased and approaches for cloning and functional characterization of PEPT1 orthologues from other fish species, some of them of the highest commercial value, are now underway. In this paper, we provide a brief overview of the transport of di- and Tripeptides in teleost fish intestine by recalling the bulk of biochemical, biophysical and physiological observations collected in the pre-cloning era and by recapitulating the more recent molecular and functional data.
Tiziano Verri - One of the best experts on this subject based on the ideXlab platform.
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Di- and Tripeptide transport in vertebrates: the contribution of teleost fish models
Journal of Comparative Physiology B, 2017Co-Authors: Tiziano Verri, Amilcare Barca, Barbara Piccinni, Carlo Storelli, Paola Pisani, Alessandro RomanoAbstract: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.
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Di- and Tripeptide transport in vertebrates: the contribution of teleost fish models
Journal of Comparative Physiology B, 2017Co-Authors: Tiziano Verri, Amilcare Barca, Barbara Piccinni, Carlo Storelli, Paola Pisani, Alessandro RomanoAbstract: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.
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transport of di and Tripeptides in teleost fish intestine
Aquaculture Research, 2010Co-Authors: Tiziano Verri, Amilcare Barca, Alessandro Romano, Hannelore Daniel, Gabor Kottra, Carlo StorelliAbstract:The initial observation of peptide absorption in fish intestine dates back to 1981, when, in rainbow trout (Oncorhynchus mykiss), the rate of intestinal absorption of the dipeptide glycylglycine (Gly-Gly) was compared in vivo with the rate of absorption of its component amino acid glycine (Gly). The description of the identification of the underlying mechanisms that allow di- and Tripeptide transport across the plasma membranes in fish was provided in 1991, when the first evidence of peptide transport activity was reported in brush-border membrane vesicles of intestinal epithelial cells of Mozambique tilapia (Oreochromis mossambicus) by monitoring uptake of radiolabelled glycyl-l-phenylalanine (Gly-l-Phe). Since then, the existence of a carrier-mediated, H+-dependent transport of di- and Tripeptides (H+/peptide cotransport) in the brush-border membrane of fish enterocytes has been confirmed in many teleost species by a variety of biochemical approaches, providing basic kinetics and substrate specificities of the transport activity. In 2003, the first peptide transporter from a teleost fish, i.e. the zebrafish (Danio rerio) PEPtide transporter 1 (PEPT1), was cloned and functionally characterized in the Xenopus laevis oocyte expression system as a low-affinity/high-capacity system. PEPT1 is the protein in brush-border membranes responsible for translocation of intact di- and Tripeptides released from dietary protein by luminal and membrane-bound proteases and peptidases. The transporter possesses affinities for the peptide substrates in the 0.1–10 mM range, depending on the structure and physicochemical nature of the substrates. After the molecular and functional characterization of the zebrafish transporter, the interest in PEPT1 in teleost fish has increased and approaches for cloning and functional characterization of PEPT1 orthologues from other fish species, some of them of the highest commercial value, are now underway. In this paper, we provide a brief overview of the transport of di- and Tripeptides in teleost fish intestine by recalling the bulk of biochemical, biophysical and physiological observations collected in the pre-cloning era and by recapitulating the more recent molecular and functional data.
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Transport of di‐ and Tripeptides in teleost fish intestine
Aquaculture Research, 2010Co-Authors: Tiziano Verri, Amilcare Barca, Alessandro Romano, Hannelore Daniel, Gabor Kottra, Carlo StorelliAbstract:The initial observation of peptide absorption in fish intestine dates back to 1981, when, in rainbow trout (Oncorhynchus mykiss), the rate of intestinal absorption of the dipeptide glycylglycine (Gly-Gly) was compared in vivo with the rate of absorption of its component amino acid glycine (Gly). The description of the identification of the underlying mechanisms that allow di- and Tripeptide transport across the plasma membranes in fish was provided in 1991, when the first evidence of peptide transport activity was reported in brush-border membrane vesicles of intestinal epithelial cells of Mozambique tilapia (Oreochromis mossambicus) by monitoring uptake of radiolabelled glycyl-l-phenylalanine (Gly-l-Phe). Since then, the existence of a carrier-mediated, H+-dependent transport of di- and Tripeptides (H+/peptide cotransport) in the brush-border membrane of fish enterocytes has been confirmed in many teleost species by a variety of biochemical approaches, providing basic kinetics and substrate specificities of the transport activity. In 2003, the first peptide transporter from a teleost fish, i.e. the zebrafish (Danio rerio) PEPtide transporter 1 (PEPT1), was cloned and functionally characterized in the Xenopus laevis oocyte expression system as a low-affinity/high-capacity system. PEPT1 is the protein in brush-border membranes responsible for translocation of intact di- and Tripeptides released from dietary protein by luminal and membrane-bound proteases and peptidases. The transporter possesses affinities for the peptide substrates in the 0.1–10 mM range, depending on the structure and physicochemical nature of the substrates. After the molecular and functional characterization of the zebrafish transporter, the interest in PEPT1 in teleost fish has increased and approaches for cloning and functional characterization of PEPT1 orthologues from other fish species, some of them of the highest commercial value, are now underway. In this paper, we provide a brief overview of the transport of di- and Tripeptides in teleost fish intestine by recalling the bulk of biochemical, biophysical and physiological observations collected in the pre-cloning era and by recapitulating the more recent molecular and functional data.
