Borron, Paul;
McCormack, Francis X.;
Elhalwagi, Baher M.;
Chroneos, Zissis C.;
Lewis, James F.;
Zhu, Sha;
Wright, Jo Rae;
Shepherd, Virginia L.;
Possmayer, Fred;
Inchley, Kevin;
Fraher, Laurence J.
Surfactant protein A inhibits T cell proliferation via its collagen-like tail and a 210-kDa receptor
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Media type:
E-Article
Title:
Surfactant protein A inhibits T cell proliferation via its collagen-like tail and a 210-kDa receptor
Contributor:
Borron, Paul;
McCormack, Francis X.;
Elhalwagi, Baher M.;
Chroneos, Zissis C.;
Lewis, James F.;
Zhu, Sha;
Wright, Jo Rae;
Shepherd, Virginia L.;
Possmayer, Fred;
Inchley, Kevin;
Fraher, Laurence J.
imprint:
American Physiological Society, 1998
Published in:
American Journal of Physiology-Lung Cellular and Molecular Physiology, 275 (1998) 4, Seite L679-L686
Description:
<jats:p>Investigation of possible mechanisms to describe the hyporesponsiveness of pulmonary leukocytes has led to the study of pulmonary surfactant and its constituents as immune suppressive agents. Pulmonary surfactant is a phospholipid-protein mixture that reduces surface tension in the lung and prevents collapse of the alveoli. The most abundant protein in this mixture is a hydrophilic molecule termed surfactant-associated protein A (SP-A). Previously, we showed that bovine (b) SP-A can inhibit human T lymphocyte proliferation and interleukin-2 production in vitro. Results presented in this investigation showed that different sources of human SP-A and bSP-A as well as recombinant rat SP-A inhibited human T lymphocyte proliferation in a dose-dependent manner. A structurally similar collagenous protein, C1q, did not block the in vitro inhibitory action of SP-A. The addition of large concentrations of mannan to SP-A-treated cultures also did not disrupt inhibition, suggesting that the effect is not mediated by the carbohydrate recognition domain of SP-A. Use of recombinant mutant SP-As revealed that a 36-amino acid Arg-Gly-Asp (RGD) motif-containing span of the collagen-like domain was responsible for the inhibition of T cell proliferation. A polyclonal antiserum directed against an SP-A receptor (SP-R210) completely blocked the inhibition of T cell proliferation by SP-A. These results emphasize a potential role for SP-A in dampening lymphocyte responses to exogenous stimuli. The data also provide further support for the concept that SP-A maintains a balance between the clearance of inhaled pathogens and protection against collateral immune-mediated damage.</jats:p>