Author: Kanayama, Naohiro; Kajiwara, Yayoi; Goto, Junko; Maradny, Emad EL; Maehara, Kayoko; Andou, Katuaki; Terao, Toshihiko
Title: Inactivation of interleukinâ€8 by aminopeptidase N (CD13) Cord-id: 1fyiru4x Document date: 1995_1_1
ID: 1fyiru4x
Snippet: Aminopeptidase (APN) was found to degrade interleukinâ€8 (ILâ€8) and inactivate its chemotactic activity. The chemotactic activity of ILâ€8 was decreased by APN or neutrophil plasma membranes dose†and timeâ€dependently. The chemotactic activity was not inactivated in the presence of bestatin or WM15 monoclonal antibody. The expression of ILâ€8 was measured by flow cytometry. On lipopolysaccharide (LPS) stimulation, ILâ€8 expression increased for 60 min and then decreased markedly. In co
Document: Aminopeptidase (APN) was found to degrade interleukinâ€8 (ILâ€8) and inactivate its chemotactic activity. The chemotactic activity of ILâ€8 was decreased by APN or neutrophil plasma membranes dose†and timeâ€dependently. The chemotactic activity was not inactivated in the presence of bestatin or WM15 monoclonal antibody. The expression of ILâ€8 was measured by flow cytometry. On lipopolysaccharide (LPS) stimulation, ILâ€8 expression increased for 60 min and then decreased markedly. In contrast, on treatment with LPS and bestatin, the expression of ILâ€8 increased continuously for at least 120 min. These results suggest that the expression and release of ILâ€8 from phagocytic cells are regulated by the proteolytic effect of APN on ILâ€8. J. Leukoc. Biol. 57: 129–134; 1995.
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