Seminars in Perinatology
Volume 32, Issue 5 , Pages 367-370 , October 2008

Posttranslational Regulation of Surfactant Protein B Expression

  • Susan Guttentag, MD

      Affiliations

    • Corresponding Author InformationAddress reprint requests to Susan Guttentag, MD, Abramson Research Center 416G, Children's Hospital of Philadelphia, 3516 Civic Center Blvd., Philadelphia, PA 19104-4318

References 

  1. Bachofen H, Schurch S. Alveolar surface forces and lung architecture. Compar Biochem Physiol. 2001;129:183–193
  2. Jobe AH, Ikegami M. Biology of surfactant. Clin Perinatol. 2001;28:655–669vii-viii
  3. Veldhuizen EJ, Haagsman HP. Role of pulmonary surfactant components in surface film formation and dynamics. Biochim Biophys Acta. 2000;1467:255–270
  4. Hawgood S, Derrick M, Poulain F. Structure and properties of surfactant protein B. Biochim Biophys Acta. 1998;1408:150–160
  5. Weaver TE. Synthesis (Processing and secretion of surfactant proteins B and C). Biochim Biophys Acta. 1998;1408:173–179
  6. Ryan MA, Qi X, Serrano AG, et al. Mapping and analysis of the lytic and fusogenic domains of surfactant protein B. Biochemistry. 2005;44:861–872
  7. Weaver TE, Conkright JJ. Function of surfactant proteins B and C. Annu Rev Physiol. 2001;63:555–578
  8. Eijking EP, Strayer DS, van Daal GJ, et al. In vivo and in vitro inactivation of bovine surfactant by an anti-surfactant monoclonal antibody. Eur Respir J. 1991;4:1245–1250
  9. Ingenito EP, Mora R, Cullivan M, et al. Decreased surfactant protein-B expression and surfactant dysfunction in a murine model of acute lung injury. Am J Respir Cell Mol Biol. 2001;25:35–44
  10. Nesslein LL, Melton KR, Ikegami M, et al. Partial Sp-B deficiency perturbs lung function and causes air space abnormalities. Am J Physiol Lung Cell Mol Physiol. 2005;288:L1154–L1161
  11. Gunther A, Siebert C, Schmidt R, et al. Surfactant alterations in severe pneumonia (acute respiratory distress syndrome, and cardiogenic lung edema). Am J Respir Crit Care Med. 1996;153:176–184
  12. Guttentag S, Robinson L, Zhang P, et al. Cysteine protease activity is required for surfactant protein B processing and lamellar body genesis. Am J Respir Cell Mol Biol. 2003;28:69–79
  13. Foster CD, Zhang PX, Gonzales LW, et al. In vitro surfactant protein B deficiency inhibits lamellar body formation. Am J Respir Cell Mol Biol. 2003;29:259–266
  14. Nogee LM, Garnier G, Dietz HC, et al. A Mutation in the surfactant protein B gene responsible for fatal neonatal respiratory disease in multiple kindreds. J Clin Invest. 1994;93:1860–1863
  15. Clark JC, Wert SE, Bachurski CJ, et al. Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis causing respiratory failure in newborn mice. Proc Natl Acad Sci USA. 1995;92:7794–7798
  16. Stahlman MT, Gray MP, Falconieri MW, et al. Lamellar body formation in normal and surfactant protein B-deficient fetal mice. Lab Invest. 2000;80:395–403
  17. Weaver TE, Na CL, Stahlman M. Biogenesis of lamellar bodies (Lysosome-related organelles involved in storage and secretion of pulmonary surfactant). Semin Cell Dev Biol. 2002;13:263–270
  18. Zhai Y, Saier MH. The Amoebapore superfamily. Biochim Biophys Acta. 2000;1469:87–99
  19. Zaltash S, Johansson J. Secondary structure and limited proteolysis give experimental evidence that the precursor of pulmonary surfactant protein B contains three saposin-like domains. FEBS Lett. 1998;423:1–4
  20. Beck DC, Na CL, Whitsett JA, et al. Ablation of a critical surfactant protein B intramolecular disulfide bond in transgenic mice. J Biol Chem. 2000;275:3371–3376
  21. Lin Z, Pearson C, Chinchilli V, et al. Polymorphisms of human Sp-a, Sp-B, and Sp-D genes: association of Sp-B Thr131ile with ARDS. Clin Genet. 2000;58:181–191
  22. Lin Z, deMello DE, Wallot M, et al. An Sp-B gene mutation responsible for Sp-B deficiency in fatal congenital alveolar proteinosis: evidence for a mutation hotspot in Exon 4. Mol Genet Metab. 1998;64:25–35
  23. Marttila R, Haataja R, Guttentag S, et al. Surfactant protein A and B genetic variants in respiratory distress syndrome in singletons and twins. Am J Respir Crit Care Med. 2003;168:1216–1222
  24. Leonova T, Xiaoyang Q, Bencosme A, et al. Proteolytic processing patterns of prosaposin in insect and mammalian cells. J Biol Chem. 1996;271:17312–17320
  25. Guttentag SH, Beers MF, Bieler BM, et al. Surfactant protein B processing in human fetal lung. Am J Physiol. 1998;275:L559–L566
  26. Tatnell PJ, Powell DJ, Hill J, et al. Napsins: new human aspartic proteinases (Distinction between two closely related genes). FEBS Lett. 1998;441:43–48
  27. Schauer-Vukasinovic V, Bur D, Kling D, et al. Human napsin A: expression (immunochemical detection, and tissue localization). FEBS Lett. 1999;462:135–139
  28. Brasch F, Ochs M, Kahne T, et al. Involvement of napsin a in the C- and N-terminal processing of surfactant protein B in Type-Ii pneumocytes of the human lung. J Biol Chem. 2003;278:49006–49014
  29. Ueno T, Linder S, Na CL, et al. Processing of pulmonary surfactant protein B by napsin and cathepsin H. J Biol Chem. 2004;279:16178–16184
  30. Foster C, Aktar A, Kopf D, et al. Pepsinogen C: a Type 2 cell-specific protease. Am J Physiol Lung Cell Mol Physiol. 2004;286:L382–L387
  31. Gerson KD, Foster CD, Zhang P, et al. Pepsinogen C proteolytic processing of surfactant protein B. J Biol Chem. 2008;283:10330–10338
  32. Otto H, Schirmeister T. Cysteine proteases and their inhibitors. Chem Rev. 1997;97:133–171
  33. Brasch F, Ten Brinke A, Johnen G, et al. Involvement of Cathepsin H in the processing of the hydrophobic surfactant-associated protein C in Type Ii pneumocytes. Am J Respir Cell Mol Biol. 2002;26:659–670
  34. Korimilli A, Gonzales LW, Guttentag SH. Intracellular localization of processing events in human surfactant protein B biosynthesis. J Biol Chem. 2000;275:8672–8679
  35. Dinter A, Berger EG. Golgi-disturbing agents. Histochem Cell Biol. 1998;109:571–590
  36. Beck DC, Ikegami M, Na CL, et al. The role of homodimers in surfactant protein B function in vivo. J Biol Chem. 2000;275:3365–3370
  37. Beers MF, Shuman H, Liley HG, et al. Surfactant protein B in human fetal lung: developmental and glucocorticoid regulation. Pediatr Res. 1995;38:668–675
  38. Liley HG, White RT, Warr RG, et al. Regulation of messenger RNAs for the hydrophobic surfactant proteins in human lung. J Clin Invest. 1989;83:1191–1197

PII: S0146-0005(08)00088-8

doi: 10.1053/j.semperi.2008.08.003

Seminars in Perinatology
Volume 32, Issue 5 , Pages 367-370 , October 2008