TY - JOUR
T1 - Effects of N-acetyl-L-tryptophan on desorption of the protein-bound uremic toxin indoxyl sulfate and effects on uremic sarcopenia
AU - Ohashi, Atsushi
AU - Nakatani, Masashi
AU - Hori, Hideo
AU - Nakai, Shigeru
AU - Tsuchida, Kunihiro
AU - Hasegawa, Midori
AU - Tsuboi, Naotake
N1 - Publisher Copyright:
© 2023 The Authors. Therapeutic Apheresis and Dialysis published by John Wiley & Sons Australia, Ltd on behalf of International Society for Apheresis and Japanese Society for Apheresis.
PY - 2023/12
Y1 - 2023/12
N2 - Introduction: Indoxyl sulfate (IS) is a protein-bound uremic toxin that causes uremic sarcopenia. IS has poor dialysis clearance; however, the addition of a binding competitor improves its removal efficiency. Methods: Dialysis experiments were performed using N-acetyl-l-tryptophan (L-NAT) instead of l-tryptophan (Trp) using pooled sera obtained from dialysis patients. The molecular structures of L-NAT and Trp were similar to that of IS. Therefore, we examined whether Trp and L-NAT were involved in muscle atrophy in the same manner as IS by performing culture experiments using a human myotube cell line. Results: The removal efficiency of L-NAT was the same as that of Trp. However, L-NAT concentrations in the pooled sera increased at the end of the experiment. Trp (1 mM) decreased the area of human myocytes, similar to IS, whereas L-NAT did not. Conclusion: L-NAT is a binding competitor with the ability to remove protein-bound IS while preventing sarcopenia.
AB - Introduction: Indoxyl sulfate (IS) is a protein-bound uremic toxin that causes uremic sarcopenia. IS has poor dialysis clearance; however, the addition of a binding competitor improves its removal efficiency. Methods: Dialysis experiments were performed using N-acetyl-l-tryptophan (L-NAT) instead of l-tryptophan (Trp) using pooled sera obtained from dialysis patients. The molecular structures of L-NAT and Trp were similar to that of IS. Therefore, we examined whether Trp and L-NAT were involved in muscle atrophy in the same manner as IS by performing culture experiments using a human myotube cell line. Results: The removal efficiency of L-NAT was the same as that of Trp. However, L-NAT concentrations in the pooled sera increased at the end of the experiment. Trp (1 mM) decreased the area of human myocytes, similar to IS, whereas L-NAT did not. Conclusion: L-NAT is a binding competitor with the ability to remove protein-bound IS while preventing sarcopenia.
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U2 - 10.1111/1744-9987.14047
DO - 10.1111/1744-9987.14047
M3 - Article
C2 - 37596835
AN - SCOPUS:85168365463
SN - 1744-9979
VL - 27
SP - 1023
EP - 1027
JO - Therapeutic Apheresis and Dialysis
JF - Therapeutic Apheresis and Dialysis
IS - 6
ER -