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Identification of interleukin-8 converting enzyme as cathepsin L by Kensaku Ohashi; Masanobu Naruto; Toshio Nakaki; Emiko Sano is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Identification of interleukin-8 converting enzyme as cathepsin L about?

IL-8 is produced by various cells, and the NH(2)-terminal amino acid sequence of IL-8 displays heterogeneity among cell types. The mature form of IL-8 has 72 amino acids (72IL-8), while a precursor form (77IL-8) of IL-8 has five additional amino acids to the 72IL-8 NH(2)-terminal. However, it has been unclear how IL-8 is processed to yield the mature form. In this study, converting enzyme was purified as a single 31-kDa band on silver-stained polyacrylamide gel from 160 l of cultured fibroblast supernatant by sequential chromatography. NH(2)-terminal amino acid sequence analysis revealed a sequence, EAPRSVDWRE, which was identified as a partial sequence of cathepsin L. Polyclonal antibodies raised against cathepsin L recognized the purified converting enzyme on Western blot. Moreover, human hepatic cathepsin L cleaved 77IL-8 between Arg(5) and Ser(6), which is the same cleavage site as the putative converting enzyme, resulting in 72IL-8 formation. These data indicate that the converting enzyme of the partially purified fraction of the human fibroblast culture supernatant was cathepsin L. Furthermore, 72IL-8 was sevenfold more potent than 77IL-8 in a neutrophil chemotaxis assay. The

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Author

Kensaku Ohashi; Masanobu Naruto; Toshio Nakaki; Emiko Sano

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 1570-9639)

Published

2003

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)