anti-Solute Carrier Family 15 (H+/Peptide Transporter), Member 2 (SLC15A2) Antibodies

Cow (Bovine) Solute Carrier Family 15 (H+/Peptide Transporter), Member 2 (SLC15A2) interaction partners

1. Responses of oligopeptide transporter 2 (PepT2) to lactogenic hormones and oligopeptide inferred that it may play an important role in bovine mammary gland.

Zebrafish Solute Carrier Family 15 (H+/Peptide Transporter), Member 2 (SLC15A2) interaction partners

1. We characterized the functional properties of a novel zebrafish peptide transporter orthologous to mammalian and avian PEPT2, described its gene (pept2) structure, and determined mRNA tissue distribution

Rabbit Solute Carrier Family 15 (H+/Peptide Transporter), Member 2 (SLC15A2) interaction partners

1. beta-Klotho participates in the regulation of the peptide transporters PEPT1 and PEPT2.

2. Data suggest that USP18 (Ubiquitin-like specific protease 18) sensitive cellular functions include activity of the peptide transporters PEPT1 and PEPT2.

3. SPAK is a powerful regulator of peptide transporters PEPT1 and PEPT2

Mouse (Murine) Solute Carrier Family 15 (H+/Peptide Transporter), Member 2 (SLC15A2) interaction partners

1. We found marked changes in protein expression and functional activity of PhT1 and PepT2, the former predominating in adult and the latter in neonate

2. JAK3 is a powerful regulator of the peptide transporters PEPT1 and PEPT2.

3. The study presents a pharmacokinetic model to quantitate the distribution kinetics of glycylsarcosine, a substrate of PepT2, in blood, cerebrospinal fluid and kidney in wild-type and PepT2 knockout mice.

4. Peptide transport in the mammary gland

5. PEPT2 is responsible for dipeptide uptake in choroid plexus tissue

6. PEPT2 is the main system responsible for tubular reabsorption of peptide-bound amino acids, although this does not lead to major changes in renal excretion of protein or free amino acids.

7. Studies in transgenic mice demonstrated that PEPT2 was responsible for over 90% of carnosine uptake in choroid plexus. These findings elucidate the unique role of PEPT2 in regulating neuropeptide homeostasis at the blood-cerebrospinal fluid interface

8. The role of PEPT2 in the uptake of glycylsarcosine and 5-aminolevulinic acid in choroid plexus whole tissue from wild type and knockout mice.

9. PEPT2-mediated dipeptide transport in enteric glia could contribute to the clearance of neuropeptides in the ENS.

10. Pept2 mRNA was the highest in kidney, followed by brain and lung

11. When fed diets with different protein contents, Pept2-/- mice adapted food intake to dietary protein content with higher consumption rates on low protein and reduced food intake rates on the high protein diet.

12. Astrocytes from neonatal PEPT2-/- mice had reduced ALA and carnosine uptake compared to PEPT2+/+ mice. Results demonstrate that PEPT2 is the primary transporter responsible for the astrocytic uptake of ALA and carnosine.

13. PEPT2 is predominantly a system for reabsorption of cys-gly originating from glutathione break-down, thus contributing to resynthesis of glutathione .

14. Renal PEPT2 is responsible for the reabsorption of cefadroxil in kidney. Choroid plexus PEPT2 limits the exposure of cefadroxil in CSF.

15. PEPT2 to be the dominant transporter for the reabsorption of di- and tripeptides and its pharmacological substrates in the organism, and for the removal of these substrates from the cerebrospinal fluid

16. Report influence of genetic knockout of Pept2 on the in vivo disposition of endogenous and exogenous carnosine in wild-type and Pept2 null mice.

Human Solute Carrier Family 15 (H+/Peptide Transporter), Member 2 (SLC15A2) interaction partners

1. PEPT2 is expressed in keratinocytes and involved in skin oligopeptide uptake.

2. PEPT2 is functionally expressed in H441 cells, making the cell line a good in vitro model to study PEPT2 function and its regulation in human distal lung.

3. In vitro study displayed different response to sorafenib depending on the genotype of SLC15A2.

4. This study showed that ALAD2 and hPEPT2*2 may be valuable markers of risk, and indicate novel mechanisms of lead-induced neurotoxicity

5. OSR1 has the capacity to downregulate the peptide transporters PEPT1 and PEPT2 by decreasing the carrier protein abundance in the cell membrane

6. JAK3 is a powerful regulator of the peptide transporters PEPT1 and PEPT2.

7. LNCaP expresses high levels of PEPT2 and PHT1.

8. ALAD2 and hPEPT2*2 polymorphisms may exaggerate Pb blood burden in boys.

9. PEPT1,PEPT2, PHT1, and PHT2 are expressed in human nasal epithelium.

10. PepT2-mRNA is expressed in U373-MG and glial cells but showed no regulation of PepT2-mRNA expression in both cell types.

11. Data identify Drosophila Yin and PEPT2 as evolutionarily conserved phagosome-associated transporters.

12. anserine is recognized by the proton-coupled peptide transporters PEPT1 and PEPT2 with medium affinity. Anserine is able to displace other substrates from the transport process.

13. Higher blood lead burden in children with the PEPT2*2 mutation may suggest that this common genetic variant is a biomarker of increased vulnerability to the neurotoxic effects of lowest level lead exposure.

14. the two identified aminoterminal regions in mammalian peptide carriers play an important role in determining the substrate affinity and also other characteristic features of the two transporter subtypes.

15. expression, localization and functional aspects of this protein in the normal respiratory tract and in cystic fibrosis

16. Amino acid substitution at Arg57 in PEPT2 causes a complete loss of transport function.

17. polymorphisms in the gene encoding hPEPT2 can alter substrate transport and therefore could affect drug disposition in vivo

18. expression and function of the peptide transporter PepT2 (SLC15A2) in differentiated primary cultures of upper airway lung epithelia

19. functionalities of PEPT1 and PEPT2 were largely conserved in terms of glycylsarcosine uptake kinetics and inhibitor specificity

20. PEPT2-PDZK1 interaction thus plays a physiologically important role in both oligopeptide handling as well as peptide-like drug transport in the human kidney