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Type 1-prophospholipase A2 propeptide immunoreactivity is released from activated granulocytes.

Abstract：

OBJECTIVE:To establish a ELISA assay to measure release of type 1-phospholipase A2 propeptide from activated granulocytes. Human type 1-prophospholipase A2 (1-proPLA2) is biosynthesized and stored as inactive zymogen. Activation involves tryptic-like cleavage at the N-terminus, with equimolar release of the heptapeptide DSGISPR. METHODS:Using antibodies directed to the carboxyterminus of synthetic DSGISPR we developed a sensitive solid-phase ELISA specific for the released propeptide that accurately reports the activation of 1-proPLA2. The presence of the 1-proPLA2 precursor itself can be determined by trypsinization of the sample and subsequent assay for free DSGISPR. RESULTS:Using this ELISA, we demonstrated the presence of immunoreactive DSGISPR and its 14 kDa 1-proPLA2-like precursor in human granulocytes, but their absence in human macrophages and lymphocytes. Stimulation of cultured granulocytes with 1 pM of TNF alpha or GM-CSF caused rapid release of DSGISPR and precursor into the surrounding medium. The immunoreactive signal coeluted with standard synthetic DSGISPR on G50 Sephadex chromatography. CONCLUSION:Release of DSGISPR immunoreactivity appears to be a specific consequence of granulocyte activation of potential relevance to the clinical pathophysiology of conditions like acute lung injury.

journal_name

Clin Biochem

journal_title

Clinical biochemistry

authors

Rae D,Sumar N,Beechey-Newman N,Gudgeon M,Hermon-Taylor J

doi

10.1016/0009-9120(94)00068-7

subject

Has Abstract

pub_date

1995-02-01 00:00:00

pages

71-8

issue

1

eissn

0009-9120

issn

1873-2933

pii

0009912094000687

journal_volume

28

pub_type

杂志文章

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