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. 1995 Jan;57(1):129-34.
doi: 10.1002/jlb.57.1.129.

Inactivation of interleukin-8 by aminopeptidase N (CD13)

N Kanayama  1 , Y Kajiwara, J Goto, E el Maradny, K Maehara, K Andou, T Terao
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Inactivation of interleukin-8 by aminopeptidase N (CD13)

N Kanayama et al. J Leukoc Biol. 1995 Jan.

Abstract

Aminopeptidase (APN) was found to degrade interleukin-8 (IL-8) and inactivate its chemotactic activity. The chemotactic activity of IL-8 was decreased by APN or neutrophil plasma membranes dose- and time-dependently. The chemotactic activity was not inactivated in the presence of bestatin or WM15 monoclonal antibody. The expression of IL-8 was measured by flow cytometry. On lipopolysaccharide (LPS) stimulation, IL-8 expression increased for 60 min and then decreased markedly. In contrast, on treatment with LPS and bestatin, the expression of IL-8 increased continuously for at least 120 min. These results suggest that the expression and release of IL-8 from phagocytic cells are regulated by the proteolytic effect of APN on IL-8.

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