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Am J Physiol Lung Cell Mol Physiol 284: L140-L147, 2003. First published August 30, 2002; doi:10.1152/ajplung.00125.2002
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Vol. 284, Issue 1, L140-L147, January 2003

Surfactant protein A differentially regulates peripheral and inflammatory neutrophil chemotaxis

Trista L. Schagat1, Jessica A. Wofford1, Kelly E. Greene2, and Jo Rae Wright1

1 Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710; and 2 Department of Medicine, National Jewish Medical and Research Center, Denver, Colorado 80206

Surfactant protein A (SP-A), a pulmonary lectin, plays an important role in regulating innate immune cell function. Besides accelerating pathogen clearance by pulmonary phagocytes, SP-A also stimulates alveolar macrophage chemotaxis and directed actin polymerization. We hypothesized that SP-A would also stimulate neutrophil chemotaxis. With the use of a Boyden chamber assay, we found that SP-A (0.5-25 µg/ml) did not stimulate chemotaxis of rat peripheral neutrophils or inflammatory bronchoalveolar lavage (BAL) neutrophils isolated from LPS-treated lungs. However, SP-A affected neutrophil chemotaxis toward the bacterial peptide formyl-met-leu-phe (fMLP). Surprisingly, the effect was different for the two neutrophil populations: SP-A reduced peripheral neutrophil chemotaxis toward fMLP (49 ± 5% fMLP alone) and enhanced inflammatory BAL neutrophil chemotaxis (277 ± 48% fMLP alone). This differential effect was not seen for the homologous proteins mannose binding lectin and complement protein 1q but was recapitulated by type IV collagen. SP-A bound both neutrophil populations comparably and did not alter formyl peptide binding. These data support a role for SP-A in regulating neutrophil migration in pulmonary tissue.

lung; formyl-met-leu-phe; collectin; inflammation


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