Human neutrophil elastase: degradation of basement membrane components and immunolocalization in the tissue.

Abstract:

:Human neutrophil elastase was purified to homogeneity as two isozymes named E1 and E2. The isozymes degraded Type IV collagen, laminin, fibronectin, and heparan sulfate proteoglycan similarly to each other. The degradation of such basement membrane components by elastase may assist the extravasation of neutrophils in the process of inflammation. Among the substrates tested, only type V collagen, which is susceptible to neutrophil gelatinase, was resistant to elastase. This broad substrate specificity of the enzyme may also contribute to tissue destruction at the sites of inflammation. We produced a monoclonal antibody against the purified enzyme and applied it to immunohistochemical studies. In bronchopneumonia and polyarteritis nodosa, elastase was associated with the cleaved elastic fibers, indicating that the enzyme really destroys tissue in vivo. In the exudates of rheumatoid joint, elastase was stained as diffuse fine granules. Immunohistochemical studies with the monoclonal antibody will provide a complementary way to disclose the mechanism of diseases related to neutrophil infiltration.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Watanabe H,Hattori S,Katsuda S,Nakanishi I,Nagai Y

doi

10.1093/oxfordjournals.jbchem.a123277

subject

Has Abstract

pub_date

1990-11-01 00:00:00

pages

753-9

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

108

pub_type

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