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2007 ; 101
(5
): 1278-91
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Angiotensin converting enzyme 2 is primarily epithelial and is developmentally
regulated in the mouse lung
#MMPMID17340620
Wiener RS
; Cao YX
; Hinds A
; Ramirez MI
; Williams MC
J Cell Biochem
2007[Aug]; 101
(5
): 1278-91
PMID17340620
show ga
Angiotensin converting enzyme (ACE) 2 is a carboxypeptidase that shares 42% amino
acid homology with ACE. Little is known about the regulation or pattern of
expression of ACE2 in the mouse lung, including its definitive cellular
distribution or developmental changes. Based on Northern blot and RT-PCR data, we
report two distinct transcripts of ACE2 in the mouse lung and kidney and describe
a 5' exon 1a previously unidentified in the mouse. Western blots show multiple
isoforms of ACE2, with predominance of a 75-80 kDa protein in the mouse lung
versus a 120 kDa form in the mouse kidney. Immunohistochemistry localizes ACE2
protein to Clara cells, type II cells, and endothelium and smooth muscle of small
and medium vessels in the mouse lung. ACE2 mRNA levels peak at embryonic day 18.5
in the mouse lung, and immunostaining demonstrates protein primarily in the
bronchiolar epithelium at that developmental time point. In murine cell lines
ACE2 is strongly expressed in the Clara cell line mtCC, as opposed to the low
mRNA expression detected in E10 (type I-like alveolar epithelial cell line),
MLE-15 (type II alveolar epithelial cell line), MFLM-4 (fetal pulmonary
vasculature cell line), and BUMPT-7 (renal proximal tubule cell line). In
summary, murine pulmonary ACE2 appears to be primarily epithelial, is
developmentally regulated, and has two transcripts that include a previously
undescribed exon.