B. Loenders et al., LOCALIZATION OF EXTRACELLULAR-SUPEROXIDE DISMUTASE IN RAT LUNG - NEUTROPHILS AND MACROPHAGES AS CARRIERS OF THE ENZYME, Free radical biology & medicine, 24(7-8), 1998, pp. 1097-1106
Immunohistochemistry (IHC) and in situ hybridization (ISH) was used to
localize extracellular superoxide dismutase (EC-SOD) and its mRNA in
rat lung before and after a lipopolysaccharide (LPS)- and hyperoxia-in
duced inflammation. In control rats, EC-SOD mRNA was synthesized in ma
crophages and in cells of the arterial vessel walls and the alveolar s
epta. The EC-SOD protein was mainly localized in plasma and on the api
cal side of the epithelial cells located near bronchus-associated lymp
hoid tissue (BALT). ISH did not reveal major changes in the distributi
on of EC-SOD mRNA upon induction of inflammation. In contrast, IHC dem
onstrated a progressive staining of the epithelium of the larger bronc
hi for the protein. Neutrophils and macrophages invading the lung show
ed an intensive staining for the EC-SOD protein concomitantly with a d
ecrease of the enzyme in the plasma. Twenty-four hours after LPS stimu
lation only a spotty positivity remained on neutrophils in and between
the alveolar spaces. In the bronchoalveolar lavage fluid (BALF), only
macrophages showed a strong positivity for EC-SOD mRNA while the prot
ein was detected in macrophages and neutrophils. Exposure to hyperoxia
did not affect the distribution of EC-SOD mRNA and protein. The prese
nted data demonstrated that in lung tissue the EC-SOD enzyme may have
a protective function for activated macrophages, neutrophils, and lymp
oid tissue-associated epithelial cells. (C) 1998 Elsevier Science Inc.