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Jeffrey A Whitsett - One of the best experts on this subject based on the ideXlab platform.
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PARP-2 interacts with TTF-1 and regulates expression of Surfactant Protein-B.
The Journal of biological chemistry, 2006Co-Authors: Yutaka Maeda, David E Loudy, Vrushank Davé, Valérie Schreiber, Thomas C. Hunter, Jeffrey A WhitsettAbstract:Thyroid transcription factor 1 (TTF-1/Nkx-2.1) plays a critical role in lung morphogenesis and regulates the expression of lung-specific genes, including the Surfactant Proteins required for pulmonary function after birth. The activity of TTF-1 is influenced by its interactions with other transcription factors and coactivators, including CBP/p300 and SRC-1. In this study, we have identified poly(ADP-ribose) polymerases (PARP-2 and PARP-1) as TTF-1 interacting Proteins that influence its transcriptional activity. Endogenous PARP-2 was coimmunoprecipitated from transformed mouse lung epithelial cell (MLE15) extracts with TTF-1 and was identified by mass spectrometry. PARP-1 and Ku70/Ku80 were also coimmunoprecipitated from the cell extracts with TTF-1. The E domain of PARP-2 interacted via the C-terminal domain of TTF-1. Both PARP-1 and PARP-2 enhanced the activity of the promoter of Surfactant Protein-B (Sftpb gene) but not other Surfactant Proteins in vitro. PARP-2 was selectively expressed in epithelial cells of the conducting and peripheral lung tubules of the fetal mouse lung from embryonic day 12.5 and was detected in bronchial epithelial cells in the adult lung at cellular sites consistent with that of Surfactant Protein B. PARP-2 and PARP-1 interact with TTF-1 and regulate the expression of Surfactant Protein B, a Protein required for lung function.
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a common mutation in the Surfactant Protein c gene associated with lung disease
The Journal of Pediatrics, 2005Co-Authors: Scott H Cameron, Aaron Hamvas, Jeffrey A Whitsett, Susan E Wert, Marco Somaschini, Paola Carrera, Gail H Deutsch, Lawrence M NogeeAbstract:Objective To determine the contribution of the Surfactant Protein C (SP-C) I73T mutation to lung disease. Study design Genomic DNA was obtained from 116 children with interstitial lung disease (ILD) or chronic lung disease of unclear cause and from 166 control subjects and was screened for the I73T mutation using an allele-specific polymerase chain reaction assay. Results The I73T mutation was found on 7 of 232 SP-C alleles from 7 unrelated children with ILD but was not found on 332 control SP-C alleles ( P Conclusions These findings support the hypothesis that the I73T mutation predisposes to or causes lung disease.
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taz interacts with ttf 1 and regulates expression of Surfactant Protein c
Journal of Biological Chemistry, 2004Co-Authors: Kwon Sik Park, Jeffrey A Whitsett, Tina Di Palma, Jeong Ho Hong, Michael B Yaffe, Mariastella ZanniniAbstract:Thyroid transcription factor 1 (TTF-1/Nkx-2.1) plays a critical role in lung morphogenesis and regulates the expression of lung-specific genes, including the Surfactant Proteins required for pulmonary function after birth. The activity of TTF-1 is influenced by its interactions with other transcription factors and coactivators, including CBP/p300 and SRC-1. In this study, we have identified poly(ADP-ribose) polymerases (PARP-2 and PARP-1) as TTF-1 interacting Proteins that influence its transcriptional activity. Endogenous PARP-2 was coimmunoprecipitated from transformed mouse lung epithelial cell (MLE15) extracts with TTF-1 and was identified by mass spectrometry. PARP-1 and Ku70/Ku80 were also coimmunoprecipitated from the cell extracts with TTF-1. The E domain of PARP-2 interacted via the C-terminal domain of TTF-1. Both PARP-1 and PARP-2 enhanced the activity of the promoter of Surfactant Protein-B (Sftpb gene) but not other Surfactant Proteins in vitro. PARP-2 was selectively expressed in epithelial cells of the conducting and peripheral lung tubules of the fetal mouse lung from embryonic day 12.5 and was detected in bronchial epithelial cells in the adult lung at cellular sites consistent with that of Surfactant Protein B. PARP-2 and PARP-1 interact with TTF-1 and regulate the expression of Surfactant Protein B, a Protein required for lung function.
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Surfactant Protein d enhances clearance of influenza a virus from the lung in vivo
Journal of Immunology, 2001Co-Authors: Ann Marie Levine, Jeffrey A Whitsett, Kevan L Hartshorn, Erika C Crouch, Thomas R KorfhagenAbstract:Mice lacking Surfactant Protein Surfactant Protein D (SP-D−/−) and wild-type mice (SP-D+/+) were infected with influenza A virus (IAV) by intranasal instillation. IAV infection increased the endogenous SP-D concentration in wild-type mice. SP-D-deficient mice showed decreased viral clearance of the Phil/82 strain of IAV and increased production of inflammatory cytokines in response to viral challenge. However, the less glycosylated strain of IAV, Mem/71, which is relatively resistant to SP-D in vitro, was cleared efficiently from the lungs of SP-D−/− mice. Viral clearance of the Phil/82 strain of IAV and the cytokine response were both normalized by the coadministration of recombinant SP-D. Since the airway is the usual portal of entry for influenza A virus and other respiratory pathogens, SP-D is likely to play an important role in innate defense responses to IAV.
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Surfactant Protein deficiency in familial interstitial lung disease
The Journal of pediatrics, 2001Co-Authors: Raouf S. Amin, Lawrence M Nogee, Susan E Wert, Robert P. Baughman, Joseph F. Tomashefski, Alan S. Brody, William M. Hull, Jeffrey A WhitsettAbstract:Abstract Objective: To determine the contribution of Surfactant Protein abnormalities to the development of chronic lung injury in a familial form of interstitial lung disease. Study design: An 11-year-old girl, her sister, and their mother who were diagnosed with chronic interstitial lung disease underwent laboratory investigation of Surfactant Protein expression in bronchoalveolar lavage fluid and lung biopsy specimens. Nineteen patients with idiopathic pulmonary fibrosis and 9 patients who were investigated for pulmonary malignancy but who did not have interstitial lung disease served as control subjects. Results: The 3 family members were found to have absent Surfactant Protein C (SP-C) and decreased levels of SP-A and SP-B in bronchoalveolar lavage fluid (BALF). Immunostaining for pulmonary Surfactant Proteins in lung biopsy specimens obtained from both children demonstrated a marked decrease of pro-SP-C in the alveolar epithelial cells but strong staining for pro-SP-B, SP-B, SP-A, and SP-D. No deviations from published Surfactant Protein B or C coding sequences were identified by DNA sequence analysis. All control subjects had a detectable level of SP-C in the BALF. Conclusion: The apparent absence of SP-C and a decrease in the levels of SP-A and SP-B are associated with familial interstitial lung disease. (J Pediatr 2001;139:85-92)
Thomas R Korfhagen - One of the best experts on this subject based on the ideXlab platform.
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Surfactant Protein d enhances clearance of influenza a virus from the lung in vivo
Journal of Immunology, 2001Co-Authors: Ann Marie Levine, Jeffrey A Whitsett, Kevan L Hartshorn, Erika C Crouch, Thomas R KorfhagenAbstract:Mice lacking Surfactant Protein Surfactant Protein D (SP-D−/−) and wild-type mice (SP-D+/+) were infected with influenza A virus (IAV) by intranasal instillation. IAV infection increased the endogenous SP-D concentration in wild-type mice. SP-D-deficient mice showed decreased viral clearance of the Phil/82 strain of IAV and increased production of inflammatory cytokines in response to viral challenge. However, the less glycosylated strain of IAV, Mem/71, which is relatively resistant to SP-D in vitro, was cleared efficiently from the lungs of SP-D−/− mice. Viral clearance of the Phil/82 strain of IAV and the cytokine response were both normalized by the coadministration of recombinant SP-D. Since the airway is the usual portal of entry for influenza A virus and other respiratory pathogens, SP-D is likely to play an important role in innate defense responses to IAV.
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increased metalloProteinase activity oxidant production and emphysema in Surfactant Protein d gene inactivated mice
Proceedings of the National Academy of Sciences of the United States of America, 2000Co-Authors: Susan E Wert, Thomas R Korfhagen, Gary F Ross, Machiko Ikegami, Ann Marie Levine, Mitsuhiro Yoshida, Tracy Jones, James H Fisher, Jeffrey A WhitsettAbstract:Targeted ablation of the Surfactant Protein D (SP-D) gene caused chronic inflammation, emphysema, and fibrosis in the lungs of SP-D (−/−) mice. Although lung morphology was unperturbed during the first 2 weeks of life, airspace enlargement was observed by 3 weeks and progressed with advancing age. Inflammation consisted of hypertrophic alveolar macrophages and peribronchiolar-perivascular monocytic infiltrates. These abnormalities were associated with increased activity of the matrix metalloProteinases, MMP2 and MMP9, and immunostaining for MMP9 and MMP12 in alveolar macrophages. Hydrogen peroxide production by isolated alveolar macrophages also was increased significantly (10-fold). SP-D plays a critical role in the suppression of alveolar macrophage activation, which may contribute to the pathogenesis of chronic inflammation and emphysema.
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Surfactant Protein a enhances respiratory syncytial virus clearance in vivo
Journal of Clinical Investigation, 1999Co-Authors: Ann Marie Levine, Jeffrey A Whitsett, M D Bruno, Jodie Gwozdz, James M Stark, Thomas R KorfhagenAbstract:To determine the role of Surfactant Protein-A(SP-A) in antiviral host defense, mice lacking SP-A (SP-A–/–) were produced by targeted gene inactivation. SP-A–/– and control mice (SP-A+/+) were infected with respiratory syncytial virus (RSV) by intratracheal instillation. Pulmonary infiltration after infection was more severe in SP-A–/– than in SP-A+/+ mice and was associated with increased RSV plaque-forming units in lung homogenates. Pulmonary infiltration with polymorphonuclear leukocytes was greater in the SP-A–/– mice. Levels of proinflammatory cytokines tumor necrosis factor-α and interleukin-6 were enhanced in lungs of SP-A–/– mice. After RSV infection, superoxide and hydrogen peroxide generation was deficient in macrophages from SP-A–/– mice, demonstrating a critical role of SP-A in oxidant production associated with RSV infection. Coadministration of RSV with exogenous SP-A reduced viral titers and inflammatory cells in the lung of SP-A–/– mice. These findings demonstrate that SP-A plays an important host defense role against RSV in vivo.
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Surfactant Protein d regulates Surfactant phospholipid homeostasis in vivo
Journal of Biological Chemistry, 1998Co-Authors: Thomas R Korfhagen, Susan E Wert, Vladimir Sheftelyevich, Michael S Burhans, Michael D Bruno, Gary F Ross, Mildred T Stahlman, Alan H Jobe, Machiko Ikegami, Jeffrey A WhitsettAbstract:Surfactant Protein D (SP-D) is a 43-kDa member of the collectin family of collagenous lectin domain-containing Proteins that is expressed in epithelial cells of the lung. The SP-D gene was targeted by homologous recombination in embryonic stem cells that were used to produce SP-D (+/-) and SP-D (-/-) mice. Both SP-D (-/-) and SP-D (+/-) mice survived normally in the perinatal and postnatal periods. Whereas no abnormalities were observed in SP-D (+/-) mice, alveolar and tissue phosphatidylcholine pool sizes were markedly increased in SP-D (-/-) mice. Increased numbers of large foamy alveolar macrophages and enlarged alveoli were also observed in SP-D (-/-) mice. Phospholipid composition was unaltered in SP-D (-/-) mice, but Surfactant morphology was abnormal, consisting of dense phospholipid membranous arrays with decreased tubular myelin. The pulmonary lipoidosis in the SP-D (-/-) mice was not associated with accumulation of Surfactant Proteins B or C, or their mRNAs, distinguishing the disorder from alveolar Proteinosis syndromes. Surfactant Protein A mRNA was reduced and, SP-A Protein appeared to be reduced in SP-D (-/-) compared with wild type mice. Targeting of the mouse SP-D gene caused accumulation of Surfactant lipid and altered phospholipid structures, demonstrating a previously unsuspected role for SP-D in Surfactant lipid homeostasis in vivo.
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Surfactant Protein a deficient mice are susceptible to pseudomonas aeruginosa infection
American Journal of Respiratory Cell and Molecular Biology, 1998Co-Authors: Ann Marie Levine, Jeffrey A Whitsett, M D Bruno, James M Stark, Kim E Kurak, Thomas R KorfhagenAbstract:To determine the role of Surfactant Protein-A (SP-A) in host defense, the murine SP-A locus was targeted by homologous recombination to produce mice lacking SP-A. SP-A−/− and wild-type mice were infected with mucoid Pseudomonas aeruginosa by intratracheal instillation. Pulmonary bacterial loads were greater in SP-A−/− than in wild-type mice, with increased numbers of mucoid P. aeruginosa in lung homogenates at 6 and 24 h after infection. Pulmonary infiltration with polymorphonuclear leukocytes (PMN) was similar in both groups; however, an earlier influx of PMN into the lung occurred in the SP-A−/− mice. The number of bacteria phagocytosed by alveolar macrophages was decreased in the SP-A−/− mice at 1 h after infection. Superoxide-radical generation by PMN was similar for the SP-A−/− and wild-type mice, but nitrite levels were increased in SP-A−/− mice. Concentrations of tumor necrosis factor-α, interleukin-6, and macrophage inflammatory Protein-2 (proinflammatory cytokines) were greater in bronchoalveolar...
J Y Paton - One of the best experts on this subject based on the ideXlab platform.
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Surfactant Protein levels in severe respiratory syncytial virus infection.
American journal of respiratory and critical care medicine, 1999Co-Authors: M H Kerr, J Y PatonAbstract:Infection with respiratory syncytial virus (RSV) is a common cause of respiratory disease in infancy. Surfactant phospholipids have been shown to be reduced in severe RSV infection. Reduction in Surfactant Proteins might also contribute to the pathogenesis of this disease. We investigated daily levels of Surfactant Proteins in bronchoalveolar lavage (BAL) fluid from 18 ventilated infants with RSV infection (median age 3.1 mo) and in a control group of 16 ventilated surgical patients (median age 0.4 mo). Surfactant Proteins were measured by ELISA, total Protein by the Lowry method. Surfactant Protein A (SP-A) was reduced in BAL fluid from children with RSV infection (median 5.6 micrograms/ml; range 0.6 to 151.9 micrograms/ml) compared with control samples (median 9.0 micrograms/ml; range 0.5 to 139.6 micrograms/ml, p = 0.0368). Surfactant Protein B (SP-B) was lower in the RSV group (median 12.0 ng/ml; range 0 to 60. 8 ng/ml) than in control patients (median 118.1 ng/ml; range 0 to 778.2 ng/ml, p < 0.0000). Surfactant Protein D (SP-D) was also reduced in the RSV group (median 130.3 ng/ml; range 0 to 1,486.0 ng/ml) versus median 600.4 ng/ml; range 0 to 1,869.0 ng/ml, p < 0. 0000. Total Protein levels were higher in the RSV group (median 0.49 mg/ml; range 0.13 to 2.46 mg/ml versus median 0.36 mg/ml; range 0.07 to 1.65 mg/ml, p = 0.0079). The median value of SP-A was significantly lower in the initial sample (2.3 micrograms/ml) than in the final one (6.0 micrograms/ml). However, no significant correlation was found between Surfactant Protein concentrations and disease severity measured by arterial alveolar oxygen ratio. We conclude that alterations in Surfactant Protein concentrations are present in severe RSV infection and speculate that these may contribute to the abnormalities of lung function seen in this condition.
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Surfactant Protein levels in severe respiratory syncytial virus infection.
American Journal of Respiratory and Critical Care Medicine, 1999Co-Authors: M H Kerr, J Y PatonAbstract:Infection with respiratory syncytial virus (RSV) is a common cause of respiratory disease in infancy. Surfactant phospholipids have been shown to be reduced in severe RSV infection. Reduction in Surfactant Proteins might also contribute to the pathogenesis of this disease. We investigated daily levels of Surfactant Proteins in bronchoalveolar lavage (BAL) fluid from 18 ventilated infants with RSV infection (median age 3.1 mo) and in a control group of 16 ventilated surgical patients (median age 0.4 mo). Surfactant Proteins were measured by ELISA, total Protein by the Lowry method. Surfactant Protein A (SP-A) was reduced in BAL fluid from children with RSV infection (median 5.6 μ g/ml; range 0.6 to 151.9 μ g/ml) compared with control samples (median 9.0 μ g/ml; range 0.5 to 139.6 μ g/ml, p = 0.0368). Surfactant Protein B (SP-B) was lower in the RSV group (median 12.0 ng/ml; range 0 to 60.8 ng/ml) than in control patients (median 118.1 ng/ml; range 0 to 778.2 ng/ml, p < 0.0000). Surfactant Protein D (SP-D) ...
Ann Marie Levine - One of the best experts on this subject based on the ideXlab platform.
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Surfactant Protein d enhances clearance of influenza a virus from the lung in vivo
Journal of Immunology, 2001Co-Authors: Ann Marie Levine, Jeffrey A Whitsett, Kevan L Hartshorn, Erika C Crouch, Thomas R KorfhagenAbstract:Mice lacking Surfactant Protein Surfactant Protein D (SP-D−/−) and wild-type mice (SP-D+/+) were infected with influenza A virus (IAV) by intranasal instillation. IAV infection increased the endogenous SP-D concentration in wild-type mice. SP-D-deficient mice showed decreased viral clearance of the Phil/82 strain of IAV and increased production of inflammatory cytokines in response to viral challenge. However, the less glycosylated strain of IAV, Mem/71, which is relatively resistant to SP-D in vitro, was cleared efficiently from the lungs of SP-D−/− mice. Viral clearance of the Phil/82 strain of IAV and the cytokine response were both normalized by the coadministration of recombinant SP-D. Since the airway is the usual portal of entry for influenza A virus and other respiratory pathogens, SP-D is likely to play an important role in innate defense responses to IAV.
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increased metalloProteinase activity oxidant production and emphysema in Surfactant Protein d gene inactivated mice
Proceedings of the National Academy of Sciences of the United States of America, 2000Co-Authors: Susan E Wert, Thomas R Korfhagen, Gary F Ross, Machiko Ikegami, Ann Marie Levine, Mitsuhiro Yoshida, Tracy Jones, James H Fisher, Jeffrey A WhitsettAbstract:Targeted ablation of the Surfactant Protein D (SP-D) gene caused chronic inflammation, emphysema, and fibrosis in the lungs of SP-D (−/−) mice. Although lung morphology was unperturbed during the first 2 weeks of life, airspace enlargement was observed by 3 weeks and progressed with advancing age. Inflammation consisted of hypertrophic alveolar macrophages and peribronchiolar-perivascular monocytic infiltrates. These abnormalities were associated with increased activity of the matrix metalloProteinases, MMP2 and MMP9, and immunostaining for MMP9 and MMP12 in alveolar macrophages. Hydrogen peroxide production by isolated alveolar macrophages also was increased significantly (10-fold). SP-D plays a critical role in the suppression of alveolar macrophage activation, which may contribute to the pathogenesis of chronic inflammation and emphysema.
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Surfactant Protein a enhances respiratory syncytial virus clearance in vivo
Journal of Clinical Investigation, 1999Co-Authors: Ann Marie Levine, Jeffrey A Whitsett, M D Bruno, Jodie Gwozdz, James M Stark, Thomas R KorfhagenAbstract:To determine the role of Surfactant Protein-A(SP-A) in antiviral host defense, mice lacking SP-A (SP-A–/–) were produced by targeted gene inactivation. SP-A–/– and control mice (SP-A+/+) were infected with respiratory syncytial virus (RSV) by intratracheal instillation. Pulmonary infiltration after infection was more severe in SP-A–/– than in SP-A+/+ mice and was associated with increased RSV plaque-forming units in lung homogenates. Pulmonary infiltration with polymorphonuclear leukocytes was greater in the SP-A–/– mice. Levels of proinflammatory cytokines tumor necrosis factor-α and interleukin-6 were enhanced in lungs of SP-A–/– mice. After RSV infection, superoxide and hydrogen peroxide generation was deficient in macrophages from SP-A–/– mice, demonstrating a critical role of SP-A in oxidant production associated with RSV infection. Coadministration of RSV with exogenous SP-A reduced viral titers and inflammatory cells in the lung of SP-A–/– mice. These findings demonstrate that SP-A plays an important host defense role against RSV in vivo.
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Surfactant Protein a deficient mice are susceptible to pseudomonas aeruginosa infection
American Journal of Respiratory Cell and Molecular Biology, 1998Co-Authors: Ann Marie Levine, Jeffrey A Whitsett, M D Bruno, James M Stark, Kim E Kurak, Thomas R KorfhagenAbstract:To determine the role of Surfactant Protein-A (SP-A) in host defense, the murine SP-A locus was targeted by homologous recombination to produce mice lacking SP-A. SP-A−/− and wild-type mice were infected with mucoid Pseudomonas aeruginosa by intratracheal instillation. Pulmonary bacterial loads were greater in SP-A−/− than in wild-type mice, with increased numbers of mucoid P. aeruginosa in lung homogenates at 6 and 24 h after infection. Pulmonary infiltration with polymorphonuclear leukocytes (PMN) was similar in both groups; however, an earlier influx of PMN into the lung occurred in the SP-A−/− mice. The number of bacteria phagocytosed by alveolar macrophages was decreased in the SP-A−/− mice at 1 h after infection. Superoxide-radical generation by PMN was similar for the SP-A−/− and wild-type mice, but nitrite levels were increased in SP-A−/− mice. Concentrations of tumor necrosis factor-α, interleukin-6, and macrophage inflammatory Protein-2 (proinflammatory cytokines) were greater in bronchoalveolar...
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Surfactant Protein a deficient mice are susceptible to group b streptococcal infection
Journal of Immunology, 1997Co-Authors: Ann Marie Levine, Jeffrey A Whitsett, Gary F Ross, M D Bruno, Karen M Huelsman, Thomas R KorfhagenAbstract:To determine the role of Surfactant Protein A (SP-A) in host defense, the murine SP-A locus was targeted by homologous recombination to produce mice lacking SP-A. SP-A -/- and control mice were infected with group B streptococcus (GBS) by intratracheal instillation. Pulmonary infiltration 6 and 24 h following infection was more severe in SP-A -/- than in control mice, and was associated with increased numbers of GBS in lung homogenates. Dissemination of GBS to the spleen was observed more frequently in SP-A -/- mice. Pulmonary infiltration with macrophages was similar in both groups; however, the number of bacteria associated with alveolar macrophages was decreased in the SP-A-deficient mice. There was no detectable compensatory increase in Surfactant Protein D, the other known pulmonary collectin, in response to GBS instillation. SP-A plays an important role in vivo, enhancing clearance of GBS from the lung and inhibiting systemic dissemination of the organism.
M H Kerr - One of the best experts on this subject based on the ideXlab platform.
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Surfactant Protein levels in severe respiratory syncytial virus infection.
American journal of respiratory and critical care medicine, 1999Co-Authors: M H Kerr, J Y PatonAbstract:Infection with respiratory syncytial virus (RSV) is a common cause of respiratory disease in infancy. Surfactant phospholipids have been shown to be reduced in severe RSV infection. Reduction in Surfactant Proteins might also contribute to the pathogenesis of this disease. We investigated daily levels of Surfactant Proteins in bronchoalveolar lavage (BAL) fluid from 18 ventilated infants with RSV infection (median age 3.1 mo) and in a control group of 16 ventilated surgical patients (median age 0.4 mo). Surfactant Proteins were measured by ELISA, total Protein by the Lowry method. Surfactant Protein A (SP-A) was reduced in BAL fluid from children with RSV infection (median 5.6 micrograms/ml; range 0.6 to 151.9 micrograms/ml) compared with control samples (median 9.0 micrograms/ml; range 0.5 to 139.6 micrograms/ml, p = 0.0368). Surfactant Protein B (SP-B) was lower in the RSV group (median 12.0 ng/ml; range 0 to 60. 8 ng/ml) than in control patients (median 118.1 ng/ml; range 0 to 778.2 ng/ml, p < 0.0000). Surfactant Protein D (SP-D) was also reduced in the RSV group (median 130.3 ng/ml; range 0 to 1,486.0 ng/ml) versus median 600.4 ng/ml; range 0 to 1,869.0 ng/ml, p < 0. 0000. Total Protein levels were higher in the RSV group (median 0.49 mg/ml; range 0.13 to 2.46 mg/ml versus median 0.36 mg/ml; range 0.07 to 1.65 mg/ml, p = 0.0079). The median value of SP-A was significantly lower in the initial sample (2.3 micrograms/ml) than in the final one (6.0 micrograms/ml). However, no significant correlation was found between Surfactant Protein concentrations and disease severity measured by arterial alveolar oxygen ratio. We conclude that alterations in Surfactant Protein concentrations are present in severe RSV infection and speculate that these may contribute to the abnormalities of lung function seen in this condition.
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Surfactant Protein levels in severe respiratory syncytial virus infection.
American Journal of Respiratory and Critical Care Medicine, 1999Co-Authors: M H Kerr, J Y PatonAbstract:Infection with respiratory syncytial virus (RSV) is a common cause of respiratory disease in infancy. Surfactant phospholipids have been shown to be reduced in severe RSV infection. Reduction in Surfactant Proteins might also contribute to the pathogenesis of this disease. We investigated daily levels of Surfactant Proteins in bronchoalveolar lavage (BAL) fluid from 18 ventilated infants with RSV infection (median age 3.1 mo) and in a control group of 16 ventilated surgical patients (median age 0.4 mo). Surfactant Proteins were measured by ELISA, total Protein by the Lowry method. Surfactant Protein A (SP-A) was reduced in BAL fluid from children with RSV infection (median 5.6 μ g/ml; range 0.6 to 151.9 μ g/ml) compared with control samples (median 9.0 μ g/ml; range 0.5 to 139.6 μ g/ml, p = 0.0368). Surfactant Protein B (SP-B) was lower in the RSV group (median 12.0 ng/ml; range 0 to 60.8 ng/ml) than in control patients (median 118.1 ng/ml; range 0 to 778.2 ng/ml, p < 0.0000). Surfactant Protein D (SP-D) ...