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1 The Cardiovascular Institute and 2 Division of Neonatology, Michael Reese Hospital and Medical Center, Chicago, Illinois 60616; and 3 Division of Cardiology, Evangelismos General Hospital, GR-11526 Athens, Greece
Recent work from this laboratory demonstrated
potent inhibition of apoptosis in human alveolar epithelial cells
(AECs) by the angiotensin-converting enzyme inhibitor captopril
[B. D. Uhal, C. Gidea, R. Bargout, A. Bifero, O. Ibarra-Sunga,
M. Papp, K. Flynn, and G. Filippatos. Am. J. Physiol. 275 (Lung Cell. Mol. Physiol. 19): L1013-L1017,
1998]. On this basis, we hypothesized that apoptosis
in this cell type might be induced by angiotensin II (ANG
II) through its interaction with the ANG II receptor. Purified ANG II induced dose-dependent apoptosis in both the human AEC-derived A549 cell line and in primary type II pneumocytes isolated
from adult Wistar rats as detected by nuclear and chromatin morphology,
caspase-3 activity, and increased binding of annexin V. Apoptosis also
was induced in primary rat AECs by purified angiotensinogen. The
nonselective ANG II-receptor antagonist saralasin completely abrogated
both ANG II- and angiotensinogen-induced apoptosis at a concentration
of 50 µg/ml. With RT-PCR, both cell types expressed the ANG
II-receptor subtypes 1 and 2 and angiotensin-converting enzyme (ACE).
The nonthiol ACE inhibitor lisinopril blocked apoptosis induced by
angiotensinogen, but not apoptosis induced by purified ANG II. These
data demonstrate the presence of a functional ANG II-dependent pathway
for apoptosis in human and rat AECs and suggest a role for the ANG II
receptor and ACE in the induction of AEC apoptosis in vivo.
programmed cell death; type II pneumocyte; angiotensin-converting enzyme; pulmonary fibrosis; granular pneumocytes
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