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

Erpenbeck, Veit J.; Malherbe, Delphine C.; Sommer, Stefanie; Schmiedl, Andreas; Steinhilber, W; Ghio, Andrew J.; Krug, Norbert; Wright, Jo Rae; Hohlfeld, Jens M.

doi:10.1152/ajplung.00362.2004

Cited by 67 publications

(57 citation statements)

References 34 publications

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“…The SP-D-induced aggregation of TNP-PSG was observed in both PBS ϩ 1% BSA and in Tyrode buffer (data not shown). In addition, SP-D aggregated both uncoated and TNP-coated PSG (data not shown), consistent with our previous results (17). Therefore, PSG aggregation was not the result of TNP labeling of the PSG.…”

Section: Sp-d Increases Tnp-psg Binding To Mast Cells Malhotra and Csupporting

confidence: 92%

“…The SP-A used in this study was obtained by butanol extraction of lavage of alveolar proteinosis patients, whereas Wang et al (48) used non-butanol-extracted SP-A. Interestingly, Erpenbeck and colleagues (16,17) also demonstrated that SP-D, but not SP-A, which was also isolated by butanol extraction, increased PSG uptake by alveolar macrophages.…”

Section: Sp-d Multimerization Is Important For Psg Aggregation Andmentioning

confidence: 86%

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Surfactant protein D decreases pollen-induced IgE-dependent mast cell degranulation

Malherbe¹,

Erpenbeck²,

Abraham³

et al. 2005

American Journal of Physiology-Lung Cellular and Molecular Phys

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(49). Surfactant has the following two known functions: a mechanical role in preventing alveolar collapse during breathing and a host defense role in lung innate immunity. Two of the four surfactant proteins have been shown to participate in host defense. SP-A and SP-D bind to bacteria, viruses, and fungi (12, 49) and enhance pathogen uptake by alveolar macrophages (38, 45), neutrophils (21), and dendritic cells (8). In addition, SP-A and SP-D are chemoattractants for alveolar macrophages (50) and neutrophils (13). Cytokine production by alveolar macrophages (36, 39) and dendritic cell maturation (7) are modulated by SP-A, and both SP-A and SP-D inhibit mitogen-stimulated lymphocyte proliferation (4 -6). These in vitro findings are corroborated by studies showing that SP-A and SP-D null mice are more susceptible to bacterial and viral infections than are wild-type animals (24 -27).SP-A and SP-D are members of the collectin family of proteins (12, 49). The collectins are composed of four domains, a short amino-terminal domain, a triple helical collagen region, a trimeric coiled-coil domain (neck), and a carboxy-terminal C-type lectin carbohydrate recognition domain (CRD; see Refs. 12 and 49). Binding of the collectins to bacteria is mediated in large part via interaction of the CRD with oligosaccharides on the pathogen (11). Both SP-A and SP-D are oligomeric and consist of three monomers that assemble into a trimer that undergoes further multimerization. Six SP-A trimers assemble in an octadecameric structure resembling a bouquet of tulips, whereas four trimers of SP-D form a dodecamer in the shape of a cruciform (12,49). Several functions of SP-A and SP-D have been shown to be dependent on their state of oligmerization (10,20).Although the effects of SP-A and SP-D on many types of innate and adaptive immune cells have been investigated, relatively little is known about their regulation of mast cell function. Mast cells, which reside at the interface of the host and the environment (skin, small intestine, lung), execute diverse functions that contribute to the immune response (1, 31). For example, mast cells have Fc⑀RI receptors that, when bound by IgE and cross-linked to an allergen, induce a signaling cascade leading to the release of mast cell granule contents (3,23). This degranulation process releases mediators, including histamine, which is a vasoactive amine that provokes a variety of responses that occur in allergy and asthma, such as vasodilatation and smooth muscle constriction (3). Until recently, mast cells were considered to be harmful to the host because of their key role in allergy and asthma. However, recent data have revealed that mast cells also contribute to host defense (32-34).A few recent studies have investigated interactions of surfactant proteins with allergens and regulation of allergenmediated cellular responses. For example, both SP-A and SP-D bind via their CRDs to dust mite allergens in a calciumdependent manner (47). This interaction of surfactant with dust mite allergens inhibits ...

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Section: Sp-d Increases Tnp-psg Binding To Mast Cells Malhotra and Csupporting

confidence: 92%

Section: Sp-d Multimerization Is Important For Psg Aggregation Andmentioning

confidence: 86%

Surfactant protein D decreases pollen-induced IgE-dependent mast cell degranulation

Malherbe¹,

Erpenbeck²,

Abraham³

et al. 2005

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…Pulmonary surfactant is a protein-and lipid-rich complex synthesized by alveolar type 2 cells and secreted onto the air/tissue interface of the alveoli ( 11,28 ). Lipids constitute Fig.…”

Section: Discussionmentioning

confidence: 99%

Phosphatidylinositol inhibits respiratory syncytial virus infection

Numata

Kandasamy

Nagashima

et al. 2015

Journal of Lipid Research

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“…SP-A has been shown to enhance phagocytosis of IgG-opsonized particles (23) and complement-coated particles (24) and to preferentially bind apoptotic neutrophils, which aides in their removal from the inflamed lung (25,26). SP-D is known to aggregate and aid in the removal of pollen starch granules (27,28), to bind and enhance clearance of genomic DNA and apoptotic cells (29), and to aggregate and remove nanoparticles (30).…”

Section: Roles Of Sp-a/-d In Cell-mediated Immunitymentioning

confidence: 99%

Eosinophil-Associated Lung Diseases. A Cry for Surfactant Proteins A and D Help?

Ledford

Addison

Foster

et al. 2014

Am J Respir Cell Mol Biol

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Surfactant proteins (SP)-A and SP-D (SP-A/-D) play important roles in numerous eosinophil-dominated diseases, including asthma, allergic bronchopulmonary aspergillosis, and allergic rhinitis. In these settings, SP-A/-D have been shown to modulate eosinophil chemotaxis, inhibit eosinophil mediator release, and mediate macrophage clearance of apoptotic eosinophils. Dysregulation of SP-A/-D function in eosinophil-dominated diseases is also not uncommon. Alterations in serum SP-A/-D levels are associated with disease severity in allergic rhinitis and chronic obstructive pulmonary disease. Furthermore, oligimerization of SP-A/-D, necessary for their proper function, can be perturbed by reactive nitrogen species, which are increased in eosinophilic disease. In this review, we highlight the associations of eosinophilic lung diseases with SP-A and SP-D levels and functions.

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

Cited by 67 publications

References 34 publications

Surfactant protein D decreases pollen-induced IgE-dependent mast cell degranulation

Surfactant protein D decreases pollen-induced IgE-dependent mast cell degranulation

Phosphatidylinositol inhibits respiratory syncytial virus infection

Eosinophil-Associated Lung Diseases. A Cry for Surfactant Proteins A and D Help?

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