Characterization of pulmonary surfactant protein D: its copurification with lipids

Kuroki, Yoshio; Shiratori, Masanori; Ogasawara, Yoshinori; Tsuzuki, Akihiro; Akino, Toyoaki

doi:10.1016/0005-2760(91)90006-4

Cited by 49 publications

(41 citation statements)

References 24 publications

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“…1 104±31 ng/ml. Hence, as previously reported (18,31) the majority of SP-D is soluble and not surfactant-associated. Based on our findings using purified SP-Ds, the concentrations of SP-D present in these BAL samples would be sufficient to show functional activity vs. IAV.…”

Section: Resultssupporting

confidence: 85%

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Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses.

Hartshorn

Crouch²,

White³

et al. 1994

J. Clin. Invest.

304

343

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We tested the hypothesis that pulmonary surfactant-associated lectins -surfactant proteins A and D (SP-A, and -D) contribute to initial protective mechanisms against influenza A viruses (IAVs). SP-D potently inhibited hemagglutination activity of several strains of IAV as well as causing viral aggregation. SP-D enhanced neutrophil binding of 1AV and neutrophil respiratory burst responses to the virus. Neutrophil dysfunction resulting from 1AV exposure was diminished when the virus was pre-incubated with SP-D. Each of these effects was mediated by the calcium-dependent carbohydrate-binding property of SP-D. Native SP-D preparations of both human and rat origin, as well as recombinant rat SP-D, had similar activity. SP-A also inhibited IAV hemagglutination activity. We have previously reported that related mammalian serum lectins (mannose-binding lectin [MBL] and conglutinin) have similar effects. SP-D was at least 10-fold more potent at causing hemagglutination inhibition than were SP-A or MBL. SP-D was shown to contribute to potent anti-IAV activity of human bronchoalveolar lavage fluid. These results suggest that SP-D-alone, and in conjunction with SP-A and phagocytic cells-constitutes an important component of the natural immune response to 1AV infection within the respiratory tract. (J. Clin. Invest.

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Section: Resultssupporting

confidence: 85%

“…We then subjected the BAL samples to a 10,000 g centrifugation. The vast majority of SP-A (99%) is insoluble and is concentrated in the surfactant pellet by this maneuver (31) bind to BSA (200 ,g/ml) alone or buffer alone. Purified SP-D also did not bind in this setting (data not shown).…”

Section: Resultsmentioning

confidence: 99%

Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses.

Hartshorn

Crouch²,

White³

et al. 1994

J. Clin. Invest.

304

343

View full text Add to dashboard Cite

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“…A clear function for SP-D is not known, but it seems that SP-D is not important for the structural organization of the surfactant lipids, since it is not associated with the bronchoalveolar lavage pellet (29), it is not secreted together with the surfactant lipids, it is not found in tubular myelin, and it is not able to aggregate phospholipid liposomes (29). SP-A, on the other hand, is an essential component in the structural organization of surfactant, since it is necessary for the formation of tubular myelin in vitro (33,34), it is localized at the corners of the tubular myelin network (17), and it is able to aggregate phospholipid liposomes (35,36).…”

Section: Voorhout Veenendaal Kuroki Ogasawara Van Golde Geuzementioning

confidence: 99%

Immunocytochemical localization of surfactant protein D (SP-D) in type II cells, Clara cells, and alveolar macrophages of rat lung.

Voorhout

Veenendaal²,

Kuroki³

et al. 1992

J Histochem Cytochem.

176

122

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We investigated the cellular and subcellular distribution of surfactant protein D (SPD) by immunogold l a w g in lungs of adult rats that had been given bovine s e " albumin coupled to 5-nm gold (BSAG) for 2 hr to visualize the endocytotic pathway. Specific gold labeling for SPD was found in alveolar Type II cells, Clara cells, and alveolar macrophages. In Type II cells abundant labeling was observed in the endoplasmic reticulum, whereas the Golgi complex and multivesicular bodies were labeled to a limited extent only. Lamellar bodies did not seem to contain SPD. Gold labeling in alveolar macrophages was restricted to structures containing endocytosed BSAG. In Clara ceh labeling was found in the endoplasmic reticulum, the Golgi complex, and was most ,ntroductionPulmonary surfactant is a complex mixture of lipids and proteins (1,2) which prevents the alveoli from collapsing at end expiration (3). Surfactant is synthesized by alveolar Type I1 cells, in which it is stored in lamellar bodies. On fusion of the limiting membrane of lamellar bodies with the apical plasma membrane, pulmonary surfactant is secreted into the alveolar space, where it is transformed into tubular myelin (4). Some surfactant constituents are not synthesized solely by the alveolar Type I1 cell but also by non-ciliated broncheolar epithelial (Clara) cells (5,6).Surfactant protein D (SP-D) is a collagenous surfactant-associated glycoprotein which is synthesized and secreted by freshly isolated rat Type I1 cells and has been isolated from rat bronchoalveolar lavage fluids (7-9). In rat lung it is synthesized as a 39.3 KD primary translation product that undergoes post-translational N-linked glycosylation, as well as hydroxylation and glycosylation of lysine residues within the collagenous domain (10). SP-D is secreted as a 43 KD protein and is isolated from bronchoalveolar lavage as a prominent in granules present in the apical domain of the cell. Double labeling experiments with anti-surfactant protein A (SPA) showed that both SPA and SPD were present in the same granules. However, SPA was distributed throughout the granule contents, whereas SPD was confined to the periphery of the granule. The Clara cell granules are considered seaetory granules and not lysosomes, because they were not labeled for the lysosomal markers cathepsin D and LGP120, and they did not contain endocytosed BSAG. multimeric complex of disulfide-bonded trimers composed of apparently identical subunits. SP-D is a calcium-dependent carbohydrate binding protein (9) which is structurally related to surfactant protein A (SP-A), conglutinin, and other collagenous C-type lectins (11,12). The structural similarities of SP-D and SP-A suggest that these two proteins have similar functions. Both SP-A (13) and SP-D (14) have been found immunohistochemically in alveolar Type I1 cells and Clara cells of the rat lung at the light microscopic (LM) level, and recently SP-D has been localized in Type I1 cells and in the airspace of silica-treated rats at the electron microscopic (EM) level (...

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“…Uterine contractions have been reported to accelerate the secretion of pulmonary surfactant into the alveolar space and to decrease the amount of amniotic fluid by reabsorption of liquid across the pulmonary epithelium and outflow of liquid through the trachea (25)(26)(27)(28)(29). Three quarters of rat SP-D appears to exist in a soluble form, whereas 99% of rat SP-A exists in the form of a lipid protein complex (30). These findings may be related to the results of a clinical study of SP-A that showed elevated levels of SP-A with labor (24).…”

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confidence: 99%

Surfactant Protein D in Newborn Infants: Factors Influencing Surfactant Protein D Levels in Umbilical Cord Blood and Capillary Blood

et al. 2005

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Surfactant protein D (SP-D) is a collectin that plays an important role in the innate immune system. The role of SP-D in the metabolism of surfactant is as yet quite unclear. The aims of this study were to establish normal values of SP-D in the umbilical cord blood and capillary blood of mature newborn infants and to assess the influence of perinatal conditions on these levels. A total of 458 infants were enrolled in the present study. Umbilical cord blood was drawn at the time of birth and capillary blood at age 4 to 10 d. The concentration of SP-D in umbilical cord blood and capillary blood was measured by enzyme-linked immunosorbent assay. The median concentration of SP-D in umbilical cord blood was 392.1 ng/mL and was found to be influenced by maternal smoking and labor. The median concentration of SP-D in capillary blood was 777.5 ng/mL and was found to be influenced by the mode of delivery, the highest levels being observed in infants born by cesarean section. It was concluded that SP-D concentrations in umbilical cord blood and capillary blood are highly variable and depend on several perinatal conditions. Further studies are needed to elucidate the effect of respiratory distress and infection on SP-D concentrations. Collectins are oligomeric molecules consisting of carbohydrate recognition domains attached to collagen-like regions (5). In humans, three well-studied collectins are known at present (6). These are MBL, which is a serum protein, SP-A, and SP-D. SP-A and SP-D are mainly produced in the epithelial cells of the lungs, but SP-D is also found in epithelial cells and secretory glands in the gastrointestinal tract and in other tissues (7). SP-D plays an important role in the innate immune defense by binding to specific carbohydrate and lipid structures on the surface of microorganisms: bacteria, viral particles, fungi, and protozoa (8 -11). This binding mediates effector mechanisms like aggregation, chemotaxis, mediation of phagocytosis, and permeabilization (12). Pulmonary infections in adults have been shown to cause significant changes in SP-D levels (13). Whether SP-D has a role in avoiding infections in newborn babies has to our knowledge not been investigated.Both structural and promoter variants are known for the MBL gene, and several alleles correlate with low values of MBL in serum and lead to an increased risk of infectious diseases in otherwise healthy children (14,15). Three polymorphisms have been identified in the coding sequence of human SP-D: codons corresponding to amino acid residue 11 (Met11Thr), residue 160 (Ala160Thr), and residue 270 (Ser270Thr) in the mature protein. Two clinical studies have associated the SP-D variants of amino acid 11 with disease. The SP-D allele coding for methionine 11 has been associated with severe respiratory syncytial virus infection in infants, whereas threonine 11 has been suggested to increase susceptibility to tuberculosis (16,17). However, the connection between structural genetic variance and serum SP-D has not been investigated. We have perfo...

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Characterization of pulmonary surfactant protein D: its copurification with lipids

Cited by 49 publications

References 24 publications

Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses.

Evidence for a protective role of pulmonary surfactant protein D (SP-D) against influenza A viruses.

Immunocytochemical localization of surfactant protein D (SP-D) in type II cells, Clara cells, and alveolar macrophages of rat lung.

Surfactant Protein D in Newborn Infants: Factors Influencing Surfactant Protein D Levels in Umbilical Cord Blood and Capillary Blood

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