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Vol. 84, Issue 2, 471-478, February 1998
Department of Molecular Pathology, Chest Disease Research Institute, Kyoto University, Kyoto 606, Japan
Li, Zhong-Yuan, Yasuhiro Suzuki, Mafumi Kurozumi, Hui-Qing
Shen, and Chen-Xia Duan. Removal of a dimeric form of surfactant protein C from mouse lungs: its acceleration by reduction.
J. Appl. Physiol. 84(2): 471-478, 1998.
Clearance of hydrophobic surfactant-associated protein C (SP-C)
and its dimeric form
([SP-C]2) was
investigated. SP-C and
[SP-C]2 obtained from
proteinosis patients were fluorescently labeled and were instilled into
mouse lungs as lipid-protein complexes.
[SP-C]2 was removed
more slowly than SP-C, with apparent half-lives of 30 and 18 h,
respectively. A significant amount of
[SP-C]2 was removed as
SP-C, and the conversion rate was 0.22 µg · h
1 · mouse
1.
By correcting the removal as SP-C, we obtained 38 h for a possible half-life of [SP-C]2.
Conversion from SP-C to
[SP-C]2 seemed very slow. Decrease in glutathione (GSH) in the lung inhibited the conversion of [SP-C]2
to SP-C and GSH-treatment of liposomes accelerated clearance of
[SP-C]2. These results
suggest that the removal of [SP-C]2 from lung is
accelerated by reduction and that GSH acts as a reducing agent in the
lung.
alveolar proteinosis; glutathione; L-buthionine-(S,R)-sulfoximine; diamide
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