The anti-inflammatory peptide Ac-SDKP is released from thymosin-β4 by renal meprin-α and prolyl oligopeptidase.

@article{Kumar2016TheAP,
  title={The anti-inflammatory peptide Ac-SDKP is released from thymosin-β4 by renal meprin-α and prolyl oligopeptidase.},
  author={Nitin Kumar and Pablo Nakagawa and Branislava Janic and Cesar A Romero and Morel Elvis Eyiowawi Worou and Sumit R Monu and Edward L. Peterson and Jacqueline Shaw and Frederick A. Valeriote and Elimelda Moige Ongeri and Jean-Marie Vianney Niyitegeka and Nour Eddine Rhaleb and Oscar A. Carretero},
  journal={American journal of physiology. Renal physiology},
  year={2016},
  volume={310 10},
  pages={
          F1026-34
        }
}
N-acetyl-seryl-aspartyl-lysyl-proline (Ac-SDKP) is a natural tetrapeptide with anti-inflammatory and antifibrotic properties. Previously, we have shown that prolyl oligopeptidase (POP) is involved in the Ac-SDKP release from thymosin-β4 (Tβ4). However, POP can only hydrolyze peptides shorter than 30 amino acids, and Tβ4 is 43 amino acids long. This indicates that before POP hydrolysis takes place, Tβ4 is hydrolyzed by another peptidase that releases NH2-terminal intermediate peptide(s) with… CONTINUE READING

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Production of angiotensin converting enzyme by cultured bovine endothelial cells.

  • Clinical and experimental pharmacology & physiology
  • 1981
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