Generation of interleukin-8 by plasmin from AVLPR-interleukin-8, the human fibroblast-derived neutrophil chemotactic

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H Nakagawa1, S Hatakeyama, A Ikesue

  • 1Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Sugitani, Japan.

FEBS Letters
|May 6, 1991
PubMed

Insights

Plasmin primarily cleaves Arg-Val-Leu-Pro-Arg-interleukin-8 (AVLPR-IL-8) at the Arg5-Ser6 bond, inactivating it into interleukin-8 (IL-8) and a pentapeptide. Minor cleavage also occurs at Lys8-Glu9.

Area of Science:

  • Biochemistry
  • Proteolysis
  • Cellular signaling

Background:

  • Interleukin-8 (IL-8) is a key chemokine in inflammatory responses.
  • Fibroblast-derived IL-8 can exist in precursor forms, such as Arg-Val-Leu-Pro-Arg-interleukin-8 (AVLPR-IL-8).
  • Plasmin is a serine protease involved in fibrinolysis and other physiological processes.

Purpose of the Study:

  • To investigate the specific cleavage sites of plasmin on AVLPR-IL-8.
  • To determine the products of plasmin-mediated AVLPR-IL-8 degradation.
  • To understand the implications of these cleavages for IL-8 activity.

Main Methods:

  • Enzymatic assays using purified plasmin and synthetic AVLPR-IL-8 peptide.
  • Analysis of cleavage products using mass spectrometry and Edman degradation.
  • Assessment of the biological activity of resulting peptides.

Main Results:

  • Plasmin predominantly cleaved the Arg5-Ser6 bond of AVLPR-IL-8.
  • This major cleavage generated mature interleukin-8 (IL-8) and an inactive pentapeptide.
  • A minor cleavage event was observed at the Lys8-Glu9 bond of AVLPR-IL-8.

Conclusions:

  • Plasmin effectively inactivates the precursor form AVLPR-IL-8 through specific proteolytic events.
  • The primary cleavage site (Arg5-Ser6) yields biologically active IL-8, while a secondary site (Lys8-Glu9) suggests alternative processing pathways.
  • These findings contribute to understanding the regulation of IL-8 bioavailability and function by plasmin.

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