HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: 288/4/L692    most recent 00362.2004v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (11) Citing Articles via Google Scholar Google Scholar Articles by Erpenbeck, V. J. Articles by Hohlfeld, J. M. Search for Related Content PubMed PubMed Citation Articles by Erpenbeck, V. J. Articles by Hohlfeld, J. M.

Surfactant protein D increases phagocytosis and aggregation of pollen-allergen starch granules

¹Fraunhofer Institute of Toxicology and Experimental Medicine; ²Department of Respiratory Medicine, Hannover Medical School; ⁴Department of Anatomy, Hannover Medical School, Hannover; ⁵Altana Pharma AG, Konstanz, Germany; ³Department of Cell Biology, Duke University Medical Center, Durham; and ⁶Environmental Protection Agency, Chapel Hill, North Carolina

Submitted 27 September 2004 ; accepted in final form 4 December 2004

Recent studies have shown that surfactant components, in particular the collectins surfactant protein (SP)-A and -D, modulate the phagocytosis of various pathogens by alveolar macrophages. This interaction might be important not only for the elimination of pathogens but also for the elimination of inhaled allergens and might explain anti-inflammatory effects of SP-A and SP-D in allergic airway inflammation. We investigated the effect of surfactant components on the phagocytosis of allergen-containing pollen starch granules (PSG) by alveolar macrophages. PSG were isolated from Dactylis glomerata or Phleum pratense, two common grass pollen allergens, and incubated with either rat or human alveolar macrophages in the presence of recombinant human SP-A, SP-A purified from patients suffering from alveolar proteinosis, a recombinant fragment of human SP-D, dodecameric recombinant rat SP-D, or the commercially available surfactant preparations Curosurf and Alveofact. Dodecameric rat recombinant SP-D enhanced binding and phagocytosis of the PSG by alveolar macrophages, whereas the recombinant fragment of human SP-D, SP-A, or the surfactant lipid preparations had no effect. In addition, recombinant rat SP-D bound to the surface of the PSG and induced aggregation. Binding, aggregation, and enhancement of phagocytosis by recombinant rat SP-D was completely blocked by EDTA and inhibited by D-maltose and to a lesser extent by D-galactose, indicating the involvement of the carbohydrate recognition domain of SP-D in these functions. The modulation of allergen phagocytosis by SP-D might play an important role in allergen clearance from the lung and thereby modulate the allergic inflammation of asthma.

innate immunity; antigen processing; allergy; lung

This article has been cited by other articles:

				C. Muhlfeld, B. Rothen-Rutishauser, F. Blank, D. Vanhecke, M. Ochs, and P. Gehr Interactions of nanoparticles with pulmonary structures and cellular responses Am J Physiol Lung Cell Mol Physiol, May 1, 2008; 294(5): L817 - L829. [Abstract] [Full Text] [PDF]

				M. Ikegami, K. Carter, K. Bishop, A. Yadav, E. Masterjohn, W. Brondyk, R. K. Scheule, and J. A. Whitsett Intratracheal Recombinant Surfactant Protein D Prevents Endotoxin Shock in the Newborn Preterm Lamb Am. J. Respir. Crit. Care Med., June 15, 2006; 173(12): 1342 - 1347. [Abstract] [Full Text] [PDF]

				D. C. Malherbe, V. J. Erpenbeck, S. N. Abraham, E. C. Crouch, J. M. Hohlfeld, and J. R. Wright Surfactant protein D decreases pollen-induced IgE-dependent mast cell degranulation Am J Physiol Lung Cell Mol Physiol, November 1, 2005; 289(5): L856 - L866. [Abstract] [Full Text] [PDF]