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B and Matrix Metalloproteinase Production in Alveolar Macrophages via Oxidant-Sensitive Pathways1
Division of Pulmonary Biology, Children’s Hospital Medical Center, Cincinnati, OH 45229
Targeted ablation of the surfactant protein D (SP-D) gene caused
progressive pulmonary emphysema associated with pulmonary infiltration
by foamy alveolar macrophages (AMs), increased hydrogen peroxide
production, and matrix metalloproteinase (MMP)-2, -9, and -12
expression. In the present study, the mechanisms by which SP-D
influences macrophage MMP activity were assessed in AMs from
SP-D-/- mice. Tissue lipid peroxides and reactive
carbonyls were increased in lungs of SP-D-/- mice,
indicating oxidative stress. Immunohistochemical staining of AMs from
SP-D-/- mice demonstrated that NF-
B was highly
expressed and translocated to the nucleus. Increased NF-B binding
was detected by EMSA in nuclear extracts of AMs isolated from
SP-D-/- mice. Antioxidants
N-acetylcysteine and pyrrolidine dithiocarbamate
inhibited MMP production by AMs from SP-D-/- mice. To
assess whether increased oxidant production influenced NF-B
activation and production of MMP-2 and -9, AMs from
SP-D-/- mice were treated with the NADPH oxidase
inhibitors diphenylene iodonium chloride and apocynin. Inhibition of
NADPH oxidase suppressed NF-B binding by nuclear extracts and
decreased production of MMP-2 and 9 in AMs from SP-D-/-
mice. SN-50, a synthetic NF-B-inhibitory peptide, decreased MMP
production by AMs from SP-D-/- mice. Oxidant production
and reactive oxygen species were increased in lungs of
SP-D-/- mice, in turn activating NF-B and MMP
expression. SP-D plays an unexpected inhibitory role in the regulation
of NF-B in AMs.
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