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Departments of
* Cell Biology and
Immunology, Duke University Medical Center, Durham, NC 27710
Pulmonary surfactant is a lipoprotein complex that lowers
surface tension at the air-liquid interface of the lung and
participates in pulmonary host defense. Surfactant proteins (SP), SP-A
and SP-D, modulate a variety of immune cell functions, including the
production of cytokines and free radicals. Previous studies showed that
SP-A and SP-D inhibit lymphocyte proliferation in the presence of
accessory cells. The goal of this study was to determine whether SP-A
and SP-D directly suppress Th cell function. Both proteins inhibited
CD3+/CD4+ lymphocyte proliferation induced by
PMA and ionomycin in an IL-2-independent manner. Both proteins
decreased the number of cells entering the S and mitotic phases of the
cell cycle. Neither SP-A nor SP-D altered cell viability, apoptosis, or
secretion of IL-2, IL-4, or IFN-
when Th cells were treated with PMA
and ionomycin. However, both proteins attenuated ionomycin-induced
cytosolic free calcium ([Ca2+ ]i), but not
thapsigargin-induced changes in [Ca2+]i. In
summary, inhibition of T cell proliferation by SP-A and SP-D occurs via
two mechanisms, an IL-2-dependent mechanism observed with accessory
cell-dependent T cell mitogens and specific Ag, as well as an
IL-2-independent mechanism of suppression that potentially involves
attenuation of
[Ca2+]i.
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