Identification of elastase in human eosinophils: immunolocalization, isolation, and partial characterization.

Abstract:

:Although an elastolytic activity in eosinophil-rich cell fractions from mice has been reported, this enzyme has not been purified and characterized as yet in any mammalian species. Eosinophilic elastase was isolated from human eosinophil fragments (cytosomes) obtained from normal and eosinophilic subjects. The enzyme was purified to apparent electrophoretic homogeneity by fast protein liquid chromatography. The enzyme shows the same physical properties of the major elastase isoenzyme of human neutrophils. In addition, like monocyte elastase, it reacts with a monoclonal antibody against human neutrophil elastase. The biochemical similarities observed between the above-mentioned enzymes and the immunolocalization findings strongly support the idea that human eosinophils and neutrophils contain the same enzyme activity. Eosinophils show immunoreactive material in both types of dense cytoplasmic granules. This observation supports the current hypothesis that the different types of eosinophilic granules represent successive morphological stages of maturation.

journal_name

Arch Biochem Biophys

authors

Lungarella G,Menegazzi R,Gardi C,Spessotto P,de Santi MM,Bertoncin P,Patriarca P,Calzoni P,Zabucchi G

doi

10.1016/0003-9861(92)90060-a

subject

Has Abstract

pub_date

1992-01-01 00:00:00

pages

128-35

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(92)90060-A

journal_volume

292

pub_type

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