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Journal articles on the topic 'Protein-Surfactant'

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Published: 7 September 2023

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1

La Mesa, Camillo. "Polymer–surfactant and protein–surfactant interactions." Journal of Colloid and Interface Science 286, no. 1 (June 2005): 148–57. http://dx.doi.org/10.1016/j.jcis.2004.12.038.

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2

Thompson, Mark W. "Surfactant Protein B Deficiency: Insights into Surfactant Function through Clinical Surfactant Protein Deficiency." American Journal of the Medical Sciences 321, no. 1 (January 2001): 26–32. http://dx.doi.org/10.1097/00000441-200101000-00005.

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3

Wright, Jo Rae, Paul Borron, Karen G. Brinker, and Rodney J. Folz. "Surfactant Protein A." American Journal of Respiratory Cell and Molecular Biology 24, no. 5 (May 2001): 513–17. http://dx.doi.org/10.1165/ajrcmb.24.5.f208.

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4

CASALS, Cristina, Miguel L. F. RUANO, Eugenio MIGUEL, Paloma SANCHEZ, and Jesus PEREZ-GIL. "SURFACTANT PROTEIN-C ENHANCES LIPID AGGREGATION ACTIVITY OF SURFACTANT PROTEIN-A." Biochemical Society Transactions 22, no. 3 (August 1, 1994): 370S. http://dx.doi.org/10.1042/bst022370s.

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5

Mason, Robert J., Kelly Greene, and Dennis R. Voelker. "Surfactant protein A and surfactant protein D in health and disease." American Journal of Physiology-Lung Cellular and Molecular Physiology 275, no. 1 (July 1, 1998): L1—L13. http://dx.doi.org/10.1152/ajplung.1998.275.1.l1.

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Surfactant protein (SP) A and SP-D are collagenous glycoproteins with multiple functions in the lung. Both of these proteins are calcium-dependent lectins and are structurally similar to mannose-binding protein and bovine conglutinin. Both form polyvalent multimeric structures for interactions with pathogens, cells, or other molecules. SP-A is an integral part of the surfactant system, binds phospholipids avidly, and is found in lamellar bodies and tubular myelin. Initially, most research interest focused on its role in surfactant homeostasis. Recently, more attention has been placed on the role of SP-A as a host defense molecule and its interactions with pathogens and phagocytic cells. SP-D is much less involved with the surfactant system. SP-D appears to be primarily a host defense molecule that binds surfactant phospholipids poorly and is not found in lamellar inclusion bodies or tubular myelin. Both SP-A and SP-D bind a wide spectrum of pathogens including viruses, bacteria, fungi, and pneumocystis. In addition, both molecules have been measured in the systemic circulation by immunologic methods and may be useful biomarkers of disease. The current challenges are characterization of the three-dimensional crystal structure of SP-A and SP-D, molecular cloning of their receptors, and determination of their precise physiological functions in vivo.
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6

Sorensen, Grith Lykke, Steffen Husby, and Uffe Holmskov. "Surfactant protein A and surfactant protein D variation in pulmonary disease." Immunobiology 212, no. 4-5 (June 2007): 381–416. http://dx.doi.org/10.1016/j.imbio.2007.01.003.

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7

Ikegami, M., T. R. Korfhagen, M. D. Bruno, J. A. Whitsett, and A. H. Jobe. "Surfactant metabolism in surfactant protein A-deficient mice." American Journal of Physiology-Lung Cellular and Molecular Physiology 272, no. 3 (March 1, 1997): L479—L485. http://dx.doi.org/10.1152/ajplung.1997.272.3.l479.

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In the present study we asked if surfactant metabolism was altered in surfactant protein (SP) A-deficient mice in vivo. Although previous studies in vitro demonstrated that SP-A modulates surfactant secretion and reuptake by type II cells, mice made SP-A deficient by homologous recombination grow and reproduce normally and have normal lung function. Alveolar and lung tissue saturated phophatidylcholine (Sat PC) pools were 50 and 26% larger, respectively, in SP-A(-/-) mice than in SP-A(+/+) mice. Radiolabeled choline and palmitate incorporation into lung Sat PC was similar both in vivo and for lung tissue slices in vitro from SP-A(+/+) and SP-A(-/-) mice. Percent secretion of radiolabeled Sat PC was unchanged from 3 to 15 h, although SP-A(-/-) mice retained more labeled Sat PC in the alveolar lavages at 48 h (consistent with the increased surfactant pool sizes). Clearance of radiolabeled dipalmitoylphosphatidylcholine and SP-B from the air spaces after intratracheal injection was similar in SP-A(-/-) and SP-A(+/+) mice. Lack of SP-A had minimal effects on the overall metabolism of Sat PC or SP-B in mice.
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8

Korfhagen, Thomas R., Vladimir Sheftelyevich, Michael S. Burhans, Michael D. Bruno, Gary F. Ross, Susan E. Wert, Mildred T. Stahlman, et al. "Surfactant Protein-D Regulates Surfactant Phospholipid Homeostasisin Vivo." Journal of Biological Chemistry 273, no. 43 (October 23, 1998): 28438–43. http://dx.doi.org/10.1074/jbc.273.43.28438.

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9

Fulton, Barbara K., and Mary M. Davis. "SURFACTANT PROTEIN B DEFICIENCY." Pediatric Pathology & Molecular Medicine 21, no. 5 (January 2002): 507–11. http://dx.doi.org/10.1080/pdp.21.5.507.511.

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10

De Pasquale, Carmine G., Leonard F. Arnolda, Ian R. Doyle, Philip E. Aylward, Derek P. Chew, and Andrew D. Bersten. "Plasma Surfactant Protein-B." Circulation 110, no. 9 (August 31, 2004): 1091–96. http://dx.doi.org/10.1161/01.cir.0000140260.73611.fa.

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11

Fulton, Barbara K., and Mary M. Davis. "SURFACTANT PROTEIN B DEFICIENCY." Pediatric Pathology & Molecular Medicine 21, no. 5 (September 1, 2002): 507–11. http://dx.doi.org/10.1080/02770930290056578.

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12

Johansson, Jan, Magnus Gustafsson, Marie Palmblad, Shahparak Zaltash, Bengt Robertson, and Tore Curstedt. "Synthetic Surfactant Protein Analogues." Biology of the Neonate 74, Suppl. 1 (1998): 9–14. http://dx.doi.org/10.1159/000047029.

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13

Gohon, Yann, and Jean-Luc Popot. "Membrane protein–surfactant complexes." Current Opinion in Colloid & Interface Science 8, no. 1 (March 2003): 15–22. http://dx.doi.org/10.1016/s1359-0294(03)00013-x.

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14

Nogee, Lawrence M. "Surfactant Protein-B Deficiency." Chest 111, no. 6 (June 1997): 129S—135S. http://dx.doi.org/10.1378/chest.111.6_supplement.129s-a.

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15

Kingma, Paul S., and Jeffrey A. Whitsett. "In defense of the lung: surfactant protein A and surfactant protein D." Current Opinion in Pharmacology 6, no. 3 (June 2006): 277–83. http://dx.doi.org/10.1016/j.coph.2006.02.003.

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16

Suwabe, Akira, Robert J. Mason, and Dennis R. Voelker. "Calcium Dependent Association of Surfactant Protein A with Pulmonary Surfactant: Application to Simple Surfactant Protein A Purification." Archives of Biochemistry and Biophysics 327, no. 2 (March 1996): 285–91. http://dx.doi.org/10.1006/abbi.1996.0123.

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17

Chen, Jianshe, and Eric Dickinson. "Protein/surfactant interfacial interactions part 1. Flocculation of emulsions containing mixed protein + surfactant." Colloids and Surfaces A: Physicochemical and Engineering Aspects 100 (July 1995): 255–65. http://dx.doi.org/10.1016/0927-7757(95)03204-q.

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18

Chen, Jianshe, and Eric Dickinson. "Protein/surfactant interfacial interactions paet 2. Electrophoretic mobility of mixed protein + surfactant systems." Colloids and Surfaces A: Physicochemical and Engineering Aspects 100 (July 1995): 267–77. http://dx.doi.org/10.1016/0927-7757(95)03205-r.

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19

Chen, Jianshe, and Eric Dickinson. "Protein/surfactant interfacial interactions Part 3. Competitive adsorption of protein + surfactant in emulsions." Colloids and Surfaces A: Physicochemical and Engineering Aspects 101, no. 1 (August 1995): 77–85. http://dx.doi.org/10.1016/0927-7757(95)03206-s.

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20

Ballard, Philip L., Jeffrey D. Merrill, Rodolfo I. Godinez, Marye H. Godinez, William E. Truog, and Roberta A. Ballard. "Surfactant Protein Profile of Pulmonary Surfactant in Premature Infants." American Journal of Respiratory and Critical Care Medicine 168, no. 9 (November 2003): 1123–28. http://dx.doi.org/10.1164/rccm.200304-479oc.

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21

Beers, Michael F., Aaron Hamvas, Michael A. Moxley, Linda W. Gonzales, Susan H. Guttentag, Kola O. Solarin, William J. Longmore, Lawrence M. Nogee, and Philip L. Ballard. "Pulmonary Surfactant Metabolism in Infants Lacking Surfactant Protein B." American Journal of Respiratory Cell and Molecular Biology 22, no. 3 (March 2000): 380–91. http://dx.doi.org/10.1165/ajrcmb.22.3.3645.

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22

Chen, J. "Protein/protein and protein/surfactant interactions in emulsion systems." Carbohydrate Polymers 25, no. 3 (1994): 217. http://dx.doi.org/10.1016/0144-8617(94)90213-5.

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23

TAKEDA, Kunio, and Yoshiko MORIYAMA. "Interaction of Surfactant with Protein." Oleoscience 11, no. 1 (2011): 3–10. http://dx.doi.org/10.5650/oleoscience.11.3.

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24

Haczku, A., G. Vass, and S. Kierstein. "Surfactant protein D and asthma." Clinical Experimental Allergy 34, no. 12 (December 2004): 1815–18. http://dx.doi.org/10.1111/j.1365-2222.2004.02134.x.

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25

Brown-Augsburger, Patricia, Donald Chang, Kevin Rust, and Edmond C. Crouch. "Biosynthesis of Surfactant Protein D." Journal of Biological Chemistry 271, no. 31 (August 2, 1996): 18912–19. http://dx.doi.org/10.1074/jbc.271.31.18912.

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26

Ikegami, Machiko, and Alan H. Jobe. "Surfactant protein metabolism in vivo." Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1408, no. 2-3 (November 1998): 218–25. http://dx.doi.org/10.1016/s0925-4439(98)00069-6.

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27

Brown, Nathan J., Jan Johansson, and Annelise E. Barron. "Biomimicry of Surfactant Protein C." Accounts of Chemical Research 41, no. 10 (October 21, 2008): 1409–17. http://dx.doi.org/10.1021/ar800058t.

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28

Brown, George W. "Effects of protein-free surfactant." Journal of Pediatrics 109, no. 3 (September 1986): 562. http://dx.doi.org/10.1016/s0022-3476(86)80144-5.

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29

McCormick, C. C., J. A. Hobden, C. L. Balzli, J. M. Reed, A. R. Caballero, B. S. Denard, A. Tang, and R. J. O'Callaghan. "Surfactant Protein D inPseudomonas aeruginosaKeratitis." Ocular Immunology and Inflammation 15, no. 5 (January 2007): 371–79. http://dx.doi.org/10.1080/09273940701486423.

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30

Deo, Namita, Steffen Jockusch, Nicholas J. Turro, and P. Somasundaran. "Surfactant Interactions with Zein Protein." Langmuir 19, no. 12 (June 2003): 5083–88. http://dx.doi.org/10.1021/la020854s.

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31

He, Yanchun, and Erika Crouch. "Surfactant Protein D Gene Regulation." Journal of Biological Chemistry 277, no. 22 (March 23, 2002): 19530–37. http://dx.doi.org/10.1074/jbc.m201126200.

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32

Mitchell, Patrick D., and Paul M. O’Byrne. "Surfactant Protein-D and Asthma." Chest 149, no. 5 (May 2016): 1121–22. http://dx.doi.org/10.1016/j.chest.2015.12.038.

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33

Cheng, Shu Ian, and David C. Stuckey. "Protein recovery from surfactant precipitation." Biotechnology Progress 27, no. 6 (August 25, 2011): 1614–22. http://dx.doi.org/10.1002/btpr.671.

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34

Park, Ik Soo, Jang Won Sohn, Ho Joo Yoon, Dong Ho Shin, and Sung Soo Park. "Effect of Dexamethasone on Gene Expression of Surfactant Protein B and Surfactant Protein C." Tuberculosis and Respiratory Diseases 54, no. 4 (2003): 439. http://dx.doi.org/10.4046/trd.2003.54.4.439.

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35

Herting, Egbert, Holger Schiffmann, Christian Roth, and Jan Johansson. "Surfactant lavage demonstrates protein fibrils in a neonate with congenital surfactant protein b deficiency." American Journal of Respiratory and Critical Care Medicine 166, no. 9 (November 2002): 1292–94. http://dx.doi.org/10.1164/ajrccm.166.9.267e.

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36

Whitsett, J. A., L. M. Nogee, T. E. Weaver, and A. D. Horowitz. "Human surfactant protein B: structure, function, regulation, and genetic disease." Physiological Reviews 75, no. 4 (October 1, 1995): 749–57. http://dx.doi.org/10.1152/physrev.1995.75.4.749.

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Elucidation of the structure and function of the hydrophobic surfactant protein (SP-B) and the SP-B gene has provided critical insight into surfactant homeostasis and control of respiratory epithelial cell gene expression. Surfactant protein B, in concert with surfactant protein A (SP-A), surfactant protein C (SP-C), and surfactant phospholipids, contributes to the structure and function of surfactant particles, determining surface activities and pathways by which surfactant phospholipids and proteins are processed, routed, packaged, and secreted from lamellar bodies by type II epithelial cells. After secretion, SP-B plays an essential role in determining the structure of tubular myelin, the stability and rapidity of spreading, and the recycling of surfactant phospholipids. The biochemical and structural signals underlying the homeostasis of alveolar surfactant are likely mediated by interactions between the surfactant proteins and phospholipids producing discrete structural forms that vary in size, aproprotein, and phospholipid content. Distinctions in structure, protein, and size are likely to determine the function of surfactant particles, their catabolism, or recycling by alveolar macrophages and airway epithelial cells. Analysis of the genetic controls governing the SP-B gene has led to the definition of DNA-protein interactions that determine respiratory epithelial cell gene expression in general. The important role of SP-B in lung function was defined by the study of a lethal neonatal respiratory disease, hereditary SP-B deficiency, caused by mutations in the human SP-B gene.
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37

Barnett, Rebecca C., Xin Lin, Michael Barravecchia, Rosemary A. Norman, Karen L. de Mesy Bentley, Fabeha Fazal, Jennifer L. Young, and David A. Dean. "Featured Article: Electroporation-mediated gene delivery of surfactant protein B (SP-B) restores expression and improves survival in mouse model of SP-B deficiency." Experimental Biology and Medicine 242, no. 13 (June 5, 2017): 1345–54. http://dx.doi.org/10.1177/1535370217713000.

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Surfactant Protein B Deficiency is a rare but lethal monogenetic, congenital lung disease of the neonate that is unresponsive to any treatment except lung transplantation. Based on the potential that gene therapy offers to treat such intractable diseases, our objective was to test whether an electroporation-based gene delivery approach could restore surfactant protein B expression and improve survival in a compound knockout mouse model of surfactant protein B deficiency. Surfactant protein B expression can be shut off in these mice upon withdrawl of doxycycline, resulting in decreased levels of surfactant protein B within four days and death due to lung dysfunction within four to seven days. Control or one of several different human surfactant protein B-expressing plasmids was delivered to the lung by aspiration and electroporation at the time of doxycycline removal or four days later. Plasmids expressing human surfactant protein B from either the UbC or CMV promoter expressed surfactant protein B in these transgenic mice at times when endogenous surfactant protein B expression was silenced. Mean survival was increased 2- to 5-fold following treatment with the UbC or CMV promoter-driven plasmids, respectively. Histology of all surfactant protein B treated groups exhibited fewer neutrophils and less alveolar wall thickening compared to the control groups, and electron microscopy revealed that gene transfer of surfactant protein B resulted in lamellar bodies that were similar in the presence of electron-dense, concentric material to those in surfactant protein B-expressing mice. Taken together, our results show that electroporation-mediated gene delivery of surfactant protein B-expressing plasmids improves survival, lung function, and lung histology in a mouse model of surfactant protein B deficiency and suggest that this may be a useful approach for the treatment of this otherwise deadly disease. Impact statement Surfactant protein B (SP-B) deficiency is a rare but lethal genetic disease of neonates that results in severe respiratory distress with no available treatments other than lung transplantation. The present study describes a novel treatment for this disease by transferring the SP-B gene to the lungs using electric fields in a mouse model. The procedure is safe and results in enough expression of exogenous SP-B to improve lung histology, lamellar body structure, and survival. If extended to humans, this approach could be used to bridge the time between diagnosis and lung transplantation and could greatly increase the likelihood of affected neonates surviving to transplantation and beyond.
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38

Eijking, EP, DS Strayer, GJ van Daal, R. Tenbrinck, TA Merritt, E. Hannappel, and B. Lachmann. "In vivo and in vitro inactivation of bovine surfactant by an anti-surfactant monoclonal antibody." European Respiratory Journal 4, no. 10 (November 1, 1991): 1245–50. http://dx.doi.org/10.1183/09031936.93.04101245.

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In this study the importance of a low-weight surfactant protein (11 kDa) is demonstrated by selectively blocking this protein with a monoclonal antibody. In adult rats respiratory failure was induced by repeated bronchoalveolar lavage to remove all pulmonary surfactant. It was shown that surfactant mixed with the antibody was not capable of restoring lung function when compared with surfactant alone or surfactant mixed with control serum. Using the pulsating bubble surfactometer, it could be demonstrated that surfactant mixed with this antibody had a significant higher minimum surface tension when compared with surfactant alone, or surfactant mixed with an unrelated mouse immunoglobulin G (IgG). The inhibition of surfactant function by the monoclonal antibody suggests the importance of the 11 kDa protein for normal surfactant function.
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39

Ikegami, Machiko, Elizabeth A. Scoville, Shawn Grant, Thomas Korfhagen, William Brondyk, Ronald K. Scheule, and Jeffrey A. Whitsett. "Surfactant Protein-D and Surfactant Inhibit Endotoxin-Induced Pulmonary Inflammation." Chest 132, no. 5 (November 2007): 1447–54. http://dx.doi.org/10.1378/chest.07-0864.

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40

Qua Hiansen, Joshua, Eleonora Keating, Alex Aspros, Li-Juan Yao, Karen J. Bosma, Cory M. Yamashita, James F. Lewis, and Ruud A. W. Veldhuizen. "Cholesterol-mediated surfactant dysfunction is mitigated by surfactant protein A." Biochimica et Biophysica Acta (BBA) - Biomembranes 1848, no. 3 (March 2015): 813–20. http://dx.doi.org/10.1016/j.bbamem.2014.12.009.

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41

Cañadas, Olga, Bárbara Olmeda, Alejandro Alonso, and Jesús Pérez-Gil. "Lipid–Protein and Protein–Protein Interactions in the Pulmonary Surfactant System and Their Role in Lung Homeostasis." International Journal of Molecular Sciences 21, no. 10 (May 25, 2020): 3708. http://dx.doi.org/10.3390/ijms21103708.

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Pulmonary surfactant is a lipid/protein complex synthesized by the alveolar epithelium and secreted into the airspaces, where it coats and protects the large respiratory air–liquid interface. Surfactant, assembled as a complex network of membranous structures, integrates elements in charge of reducing surface tension to a minimum along the breathing cycle, thus maintaining a large surface open to gas exchange and also protecting the lung and the body from the entrance of a myriad of potentially pathogenic entities. Different molecules in the surfactant establish a multivalent crosstalk with the epithelium, the immune system and the lung microbiota, constituting a crucial platform to sustain homeostasis, under health and disease. This review summarizes some of the most important molecules and interactions within lung surfactant and how multiple lipid–protein and protein–protein interactions contribute to the proper maintenance of an operative respiratory surface.
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42

Bates, Sandra R., Chandra Dodia, Jian-Qin Tao, and Aron B. Fisher. "Surfactant protein-A plays an important role in lung surfactant clearance: evidence using the surfactant protein-A gene-targeted mouse." American Journal of Physiology-Lung Cellular and Molecular Physiology 294, no. 2 (February 2008): L325—L333. http://dx.doi.org/10.1152/ajplung.00341.2007.

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Previous studies with the isolated perfused rat lung showed that both clathrin- and actin-mediated pathways are responsible for endocytosis of dipalmitoylphosphatidylcholine (DPPC)-labeled liposomes by granular pneumocytes in the intact lung. Using surfactant protein-A (SP-A) gene-targeted mice, we examined the uptake of [3H]DPPC liposomes by isolated mouse lungs under basal and secretagogue-stimulated conditions. Unilamellar liposomes composed of [3H]DPPC: phosphatidylcholine:cholesterol:egg phosphatidylglycerol (10:5:3:2 mol fraction) were instilled into the trachea of anesthetized mice, and the lungs were perfused (2 h). Uptake was calculated as percentage of instilled disintegrations per minute in the postlavaged lung. Amantadine, an inhibitor of clathrin and, thus, receptor-mediated endocytosis via clathrin-coated pits, decreased basal [3H]DPPC uptake by 70% in SP-A +/+ but only by 20% in SP-A −/− lung, data compatible with an SP-A/receptor-regulated lipid clearance pathway in the SP-A +/+ mice. The nonclathrin, actin-dependent process was low in the SP-A +/+ lung but accounted for 55% of liposome endocytosis in the SP-A −/− mouse. With secretagogue (8-bromoadenosine 3′,5′-cyclic monophosphate) treatment, both clathrin- and actin-dependent lipid clearance were elevated in the SP-A +/+ lungs while neither pathway responded in the SP-A −/− lungs. Binding of iodinated SP-A to type II cells isolated from both genotypes of mice was similar indicating a normal SP-A receptor status in the SP-A −/− lung. Inclusion of SP-A with instilled liposomes served to “rescue” the SP-A −/− lungs by reestablishing secretagogue-dependent enhancement of liposome uptake. These data are compatible with a major role for receptor-mediated endocytosis of DPPC by granular pneumocytes, a process critically dependent on SP-A.
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43

Boggaram, V., and R. K. Margana. "Rabbit surfactant protein C: cDNA cloning and regulation of alternatively spliced surfactant protein C mRNAs." American Journal of Physiology-Lung Cellular and Molecular Physiology 263, no. 6 (December 1, 1992): L634—L644. http://dx.doi.org/10.1152/ajplung.1992.263.6.l634.

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Surfactant protein C (SP-C), a hydrophobic protein of pulmonary surfactant is essential for surfactant function. Toward elucidating molecular mechanisms that mediate regulation of SP-C gene expression in rabbit lung, we isolated and characterized cDNAs encoding rabbit SP-C and studied the regulation of SP-C gene expression during fetal lung development and by adenosine 3',5'-cyclic monophosphate (cAMP) and dexamethasone in fetal lung tissues in vitro. We found that rabbit SP-C is highly homologous to SP-C of other species and is encoded by two mRNAs that differ by an insertion of 31 nucleotides in the 3' untranslated regions. SP-C mRNAs were classified into two types based on the nucleotide sequence; type I represents RNA without the 31 nucleotide insert and comprises approximately 80–90% of total SP-C mRNA content, whereas type II represents RNA containing the insert and comprises approximately 10–20% of total SP-C mRNA content. SP-C mRNAs were induced in a coordinate manner during fetal lung development and by cAMP and dexamethasone in fetal lung tissues in vitro. Southern hybridization analysis of genomic DNA suggested that SP-C mRNAs are encoded by a single gene. Polymerase [corrected] chain reaction-amplification of genomic DNA with oligonucleotide primers flanking the insertional sequence and sequence analysis of amplified DNA showed that SP-C mRNAs are produced by alternative use of 3' splice sites of intron 5 of SP-C gene.
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44

Boggaram, Vijayakumar, and Ramgopal K. Margana. "Rabbit surfactant protein C: cDNA cloning and regulation of alternatively spliced surfactant protein C mRNAs." American Journal of Physiology-Lung Cellular and Molecular Physiology 264, no. 1 (January 1, 1993): 1. http://dx.doi.org/10.1152/ajplung.1993.264.1.1-b.

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Pages L634–L644: Vijayakumar Boggaram and Ramgopal K. Margana. “Rabbit surfactant protein C: cDNA cloning and regulation of alternatively spliced surfactant protein C mRNAs.” Page L634, left-hand column, in the abstract, the sentence beginning on line 22 should read: Southern hybridization analysis of genomic DNA suggested that SP-C mRNAs are encoded by a single gene. Polymerase chain reaction-amplification of genomic DNA with oligonucleotide primers flanking the insertional sequence and sequence analysis of amplified DNA showed that SP-C mRNAs are produced by alternative use of 3' splice sites of intron 5 of SP-C gene. Page L634, left-hand column, paragraph 2, line 4 should read: SP-A [relative molecular weight ( Mr)≈35,000] and SP-D ( Mr ≈43,000) are hydrophilic proteins that are similar in having collagenous amino-terminus domain and noncollagenous lectinlike carboxy-terminus domain. SP-B ( Mr ≈8,000) and SP-C ( Mr ≈5,000) are hydrophobic proteins derived from larger precursor proteins by amino- and carboxy-terminus proteolytic processing.
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45

Boggaram, Vijayakumar, and Ramgopal K. Margana. "Rabbit surfactant protein C: cDNA cloning and regulation of alternatively spliced surfactant protein C mRNAs." American Journal of Physiology-Lung Cellular and Molecular Physiology 264, no. 2 (February 1, 1993): 1. http://dx.doi.org/10.1152/ajplung.1993.264.2.1-b.

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Pages L634–L644: Vijayakumar Boggaram and Ramgopal K. Margana. “Rabbit surfactant protein C: cDNA cloning and regulation of alternatively spliced surfactant protein C mRNAs.” Page L634, left-hand column, in the abstract, the sentence beginning on line 22 should read: Southern hybridization analysis of genomic DNA suggested that SP-C mRNAs are encoded by a single gene. Polymerase chain reaction-amplification of genomic DNA with oligonucleotide primers flanking the insertional sequence and sequence analysis of amplified DNA showed that SP-C mRNAs are produced by alternative use of 3' splice sites of intron 5 of SP-C gene. Page L634, left-hand column, paragraph 2, line 4 should read: SP-A [relative molecular weight (Mr) ≈35,000] and SP-D (Mr≈43,000) are hydrophilic proteins that are similar in having collagenous amino-terminus domain and noncollagenous lectinlike carboxy-terminus domain. SP-B (Mr ap8,000) and SP-C (Mr ap5,000) are hydrophobic proteins derived from larger precursor proteins by amino- and carboxy-terminus proteolytic processing.
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46

Hamvas, Aaron. "Inherited Surfactant Protein-B Deficiency and Surfactant Protein-C Associated Disease: Clinical Features and Evaluation." Seminars in Perinatology 30, no. 6 (December 2006): 316–26. http://dx.doi.org/10.1053/j.semperi.2005.11.002.

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47

Tokieda, Keisuke, Machiko Ikegami, Susan E. Wert, John E. Baatz, Yong Zou, and Jeffrey A. Whitsett. "Surfactant Protein B Corrects Oxygen-Induced Pulmonary Dysfunction in Heterozygous Surfactant Protein B–Deficient Mice." Pediatric Research 46, no. 6 (December 1999): 708. http://dx.doi.org/10.1203/00006450-199912000-00014.

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48

Kim, Hyojin Lee, Arnold Mcauley, and Joseph Mcguire. "Protein Effects on Surfactant Adsorption Suggest the Dominant Mode of Surfactant-Mediated Stabilization of Protein." Journal of Pharmaceutical Sciences 103, no. 5 (May 2014): 1337–45. http://dx.doi.org/10.1002/jps.23908.

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49

Chander, A., and A. B. Fisher. "Regulation of lung surfactant secretion." American Journal of Physiology-Lung Cellular and Molecular Physiology 258, no. 6 (June 1, 1990): L241—L253. http://dx.doi.org/10.1152/ajplung.1990.258.6.l241.

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Secretion of lung surfactant is the direct step in release of the lipoprotein-like product, synthesized in lung epithelial type II cells, onto the alveolar surface. Release of surfactant phosphatidylcholine (PC) proceeds via formation of surface pores during exocytosis of lamellar bodies. Surfactant secretion is regulated locally in the lung by changes in ventilation rate, possibly mediated by distension and altered intracellular pH. Secretion is also stimulated by various agents, including agonists for beta-adrenergic, purinoceptors, and vasopressin receptors and is associated with increased cytosolic Ca2+, cellular adenosine 3',5'-cyclic monophosphate, and activation of protein kinases. Limited studies suggest that secretion of surfactant protein A may be regulated by both cAMP-dependent and protein kinase C-dependent pathways. The integration of these various mechanisms for the in vivo regulation of surfactant secretion remains largely unexplored. Future research into the mechanisms involved in lamellar body fusion with the plasma membrane, role of protein phosphorylation, transient changes in cAMP and Ca2+, and coordination between the secretion of phospholipid and protein components of surfactant should enhance our understanding of secretion of surfactant “lipoprotein.”
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50

Elhalwagi, Baher M., Mei Zhang, Machiko Ikegami, Harriet S. Iwamoto, Randall E. Morris, Marian L. Miller, Krista Dienger, and Francis X. McCormack. "Normal Surfactant Pool Sizes and Inhibition-Resistant Surfactant from Mice That Overexpress Surfactant Protein A." American Journal of Respiratory Cell and Molecular Biology 21, no. 3 (September 1999): 380–87. http://dx.doi.org/10.1165/ajrcmb.21.3.3676.

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