Cysteine proteinase inhibitors produced by mononuclear phagocytes

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Abstract
Monocytes were separated from human peripheral blood and allowed to attach to culture flasks, after which the content and production of a number of cysteine proteinase inhibitors was assayed. These were: a low molecular weight (MW 12000) acid cysteine proteinase inhibitor (ACPI); a low-molecular weight inhibitor of the same size with neutral pH (NCPI), and α-cysteine proteinase inhibitor with a molecular weight around 90000 (α-CPI). Only NCPI was detectable in the cultures at the beginning of the incubation, and it was synthesized and released into the incubation mixture during the incubation, especially if the cells were stimulated with silica. The amount of NCPI contained in and released from the cells was drastically decreased by puromycin. Immunoblots after cell electrophoresis in polyacrylamide gel revealed only one molecular form of NCPI with a molecular weight of 12000 both in the cells and in the culture medium. No ACPI or α-CPI could be detected.