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Gene Review

Sftpa1  -  surfactant associated protein A1

Mus musculus

Synonyms: PSAP, PSP-A, Pulmonary surfactant-associated protein A, SFTPA1, SP-A, ...
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Disease relevance of Sftpa1

  • Lungs of SP-A (-/-) mice have markedly decreased tubular myelin figures and clear Group B streptococci and Pseudomonas aeruginosa less efficiently than SP-A wild type mice [1].
  • In contrast, in the absence of SP-A, bacterial killing was decreased and associated with increased lung inflammation, decreased oxidant production, and decreased macrophage phagocytosis [2].
  • The collectins, SP-A and SP-D, play distinct roles during bacterial infection of the lung [2].
  • Mice lacking surfactant protein (SP)-A (SP-A-/-) or SP-D (SP-D-/-) and wild-type mice were infected with group B streptococcus or Haemophilus influenzae by intratracheal instillation [2].
  • Cyclic AMP stimulation of expression of the SP-A-1766:hGH, SP-A-991:hGH, and SP-A-378:hGH fusion genes was limited to type II pneumonocytes in primary culture and was absent in two lung adenocarcinoma cell lines (NCl-H358 and A549), which do not express SP-A, and in cAMP-responsive adrenal Y1 cells [3].

Psychiatry related information on Sftpa1


High impact information on Sftpa1

  • 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 [5].
  • Pulmonary infiltration with polymorphonuclear leukocytes was greater in the SP-A-/- mice [5].
  • 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 [5].
  • SP-A, -B, and -C mRNAs were unaltered in lungs from GM-CSF-deficient and -replete mice [6].
  • In this review we examine the evidence from in vitro systems and gene-targeted mice that two surfactant-associated collectins (SP-A and SP-D) may serve in these roles and help modify surfactant homeostasis as part of a coordinated host response to environmental challenges [7].

Chemical compound and disease context of Sftpa1


Biological context of Sftpa1

  • Neither SP-A nor NH2-terminal domains of SP-A can substitute for SP-D in regulation of alveolar homeostasis [12].
  • We suggest that SP-A secreted by the fetal lung serves as a hormone of parturition [13].
  • Lung morphology, surfactant proteins B-D, lung tissue, alveolar phospholipid pool sizes and composition, and lung compliance in SP-A(-/-) mice were unaltered [14].
  • Moreover, in vitro inhibition of sPLA(2)-IIA-induces surfactant phospholipid hydrolysis correlates with the concentration of SP-A in surfactant [15].
  • Mutations of a putative cAMP-responsive element (TGACCTCA) at -261 bp revealed its functional importance in mediating cAMP regulation of SP-A gene expression [3].

Anatomical context of Sftpa1

  • As surfactant protein A (SP-A), a member of the collectin family, inhibits LPS-induced in vitro IL-10 formation by bone marrow-derived macrophages, we studied its effect on MP under in vivo inflammatory conditions [16].
  • The earlier phase (embryonic days 13-15; E13-E15) was characterized by CGRP, CC10, and SP-A immunostaining in all epithelial cells of the distal airways, with the three patterns being virtually identical in adjacent sections [17].
  • These studies of SP-A (-/-) mice demonstrate that SP-A has an important role in the innate immune system of the lung in vivo [1].
  • In the mouse, secretion of the major lung surfactant protein, surfactant protein A (SP-A), was first detected in amniotic fluid (AF) at 17 days postcoitum, rising progressively to term (19 days postcoitum) [13].
  • The surfactant protein A (SP-A) gene was disrupted by homologous recombination in embryonic stem cells that were used to generate homozygous SP-A-deficient mice [14].

Associations of Sftpa1 with chemical compounds

  • Tissue levels of saturated phosphatidylcholine were slightly reduced in the SP-A(-/-,rSP-A) mice compared with SP-A(-/-) littermates [18].
  • Cyclic AMP analogs and glucocorticoids stimulate transcriptional activity of the SP-A gene in fetal rabbit lung tissue in culture; an additive effect is observed when the agents are added in combination [3].
  • Wild-type and SP-A-deficient mice were conditioned with cyclophosphamide and lethal irradiation and then given allogeneic donor bone marrow plus inflammation-inducing spleen T cells [19].
  • Using a murine model to mimic occupational exposures to endotoxin, we hypothesized that SP-A gene expression and protein would be elevated in response to repeat exposure to inhaled grain dust and to purified lipopolysaccharide (LPS) [8].
  • Like surfactant protein A (SP-A), SP-D is a collagen-like glycoprotein belonging to the "collectin" class of C-type lectins that may play an important role in pulmonary host defense [20].

Enzymatic interactions of Sftpa1


Regulatory relationships of Sftpa1


Other interactions of Sftpa1

  • In normal mouse lung, the messenger RNAs (mRNAs) for SP-A, SP-B, and SP-D were expressed in both type II cells and Clara cells [23].
  • In contrast to IL-10 production, SP-A concentrations during LPS-induced inflammation decreased with a nadir at Day 3, and then increased significantly within 24 h [16].
  • SP-B and SP-C, but not SP-A, localized predominantly to the glycogen stores [24].
  • Surfactant proteins-A and -D (SP-A and SP-D) are members of the collectin protein family [25].
  • In addition, FGF-7 stimulates epithelial differentiation, stimulating expression of SP-A and SP-B mRNA throughout the explant, and inducing formation of focal areas of highly differentiated cells [26].

Analytical, diagnostic and therapeutic context of Sftpa1


  1. Surfactant protein A (SP-A) gene targeted mice. Korfhagen, T.R., LeVine, A.M., Whitsett, J.A. Biochim. Biophys. Acta (1998) [Pubmed]
  2. Distinct effects of surfactant protein A or D deficiency during bacterial infection on the lung. LeVine, A.M., Whitsett, J.A., Gwozdz, J.A., Richardson, T.R., Fisher, J.H., Burhans, M.S., Korfhagen, T.R. J. Immunol. (2000) [Pubmed]
  3. Genomic elements involved in transcriptional regulation of the rabbit surfactant protein-A gene. Alcorn, J.L., Gao, E., Chen, Q., Smith, M.E., Gerard, R.D., Mendelson, C.R. Mol. Endocrinol. (1993) [Pubmed]
  4. Dense-core plaques in Tg2576 and PSAPP mouse models of Alzheimer's disease are centered on vessel walls. Kumar-Singh, S., Pirici, D., McGowan, E., Serneels, S., Ceuterick, C., Hardy, J., Duff, K., Dickson, D., Van Broeckhoven, C. Am. J. Pathol. (2005) [Pubmed]
  5. Surfactant protein-A enhances respiratory syncytial virus clearance in vivo. LeVine, A.M., Gwozdz, J., Stark, J., Bruno, M., Whitsett, J., Korfhagen, T. J. Clin. Invest. (1999) [Pubmed]
  6. Pulmonary epithelial cell expression of GM-CSF corrects the alveolar proteinosis in GM-CSF-deficient mice. Huffman, J.A., Hull, W.M., Dranoff, G., Mulligan, R.C., Whitsett, J.A. J. Clin. Invest. (1996) [Pubmed]
  7. The pulmonary collectins and surfactant metabolism. Hawgood, S., Poulain, F.R. Annu. Rev. Physiol. (2001) [Pubmed]
  8. Altered surfactant protein A gene expression and protein metabolism associated with repeat exposure to inhaled endotoxin. George, C.L., White, M.L., O'Neill, M.E., Thorne, P.S., Schwartz, D.A., Snyder, J.M. Am. J. Physiol. Lung Cell Mol. Physiol. (2003) [Pubmed]
  9. Murine pulmonary surfactant SP-A gene: cloning, sequence, and transcriptional activity. Korfhagen, T.R., Bruno, M.D., Glasser, S.W., Ciraolo, P.J., Whitsett, J.A., Lattier, D.L., Wikenheiser, K.A., Clark, J.C. Am. J. Physiol. (1992) [Pubmed]
  10. Statin therapy for Alzheimer's disease: will it work? Petanceska, S.S., DeRosa, S., Olm, V., Diaz, N., Sharma, A., Thomas-Bryant, T., Duff, K., Pappolla, M., Refolo, L.M. J. Mol. Neurosci. (2002) [Pubmed]
  11. Characteristics of surfactant from SP-A-deficient mice. Ikegami, M., Korfhagen, T.R., Whitsett, J.A., Bruno, M.D., Wert, S.E., Wada, K., Jobe, A.H. Am. J. Physiol. (1998) [Pubmed]
  12. Neither SP-A nor NH2-terminal domains of SP-A can substitute for SP-D in regulation of alveolar homeostasis. Zhang, L., Ikegami, M., Korfhagen, T.R., McCormack, F.X., Yoshida, M., Senior, R.M., Shipley, J.M., Shapiro, S.D., Whitsett, J.A. Am. J. Physiol. Lung Cell Mol. Physiol. (2006) [Pubmed]
  13. Surfactant protein secreted by the maturing mouse fetal lung acts as a hormone that signals the initiation of parturition. Condon, J.C., Jeyasuria, P., Faust, J.M., Mendelson, C.R. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  14. Altered surfactant function and structure in SP-A gene targeted mice. Korfhagen, T.R., Bruno, M.D., Ross, G.F., Huelsman, K.M., Ikegami, M., Jobe, A.H., Wert, S.E., Stripp, B.R., Morris, R.E., Glasser, S.W., Bachurski, C.J., Iwamoto, H.S., Whitsett, J.A. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  15. Inhibitory effects of surfactant protein A on surfactant phospholipid hydrolysis by secreted phospholipases A2. Chabot, S., Koumanov, K., Lambeau, G., Gelb, M.H., Balloy, V., Chignard, M., Whitsett, J.A., Touqui, L. J. Immunol. (2003) [Pubmed]
  16. Surfactant protein A inhibits lipopolysaccharide-induced in vivo production of interleukin-10 by mononuclear phagocytes during lung inflammation. Chabot, S., Salez, L., McCormack, F.X., Touqui, L., Chignard, M. Am. J. Respir. Cell Mol. Biol. (2003) [Pubmed]
  17. Embryonic mouse lung epithelial progenitor cells co-express immunohistochemical markers of diverse mature cell lineages. Wuenschell, C.W., Sunday, M.E., Singh, G., Minoo, P., Slavkin, H.C., Warburton, D. J. Histochem. Cytochem. (1996) [Pubmed]
  18. The collagen-like region of surfactant protein A (SP-A) is required for correction of surfactant structural and functional defects in the SP-A null mouse. Ikegami, M., Elhalwagi, B.M., Palaniyar, N., Dienger, K., Korfhagen, T., Whitsett, J.A., McCormack, F.X. J. Biol. Chem. (2001) [Pubmed]
  19. Surfactant protein A decreases lung injury and mortality after murine marrow transplantation. Yang, S., Milla, C., Panoskaltsis-Mortari, A., Hawgood, S., Blazar, B.R., Haddad, I.Y. Am. J. Respir. Cell Mol. Biol. (2002) [Pubmed]
  20. Localization and developmental expression of surfactant proteins D and A in the respiratory tract of the mouse. Wong, C.J., Akiyama, J., Allen, L., Hawgood, S. Pediatr. Res. (1996) [Pubmed]
  21. Surfactant protein D binds genomic DNA and apoptotic cells, and enhances their clearance, in vivo. Palaniyar, N., Clark, H., Nadesalingam, J., Hawgood, S., Reid, K.B. Ann. N. Y. Acad. Sci. (2003) [Pubmed]
  22. Surfactant protein A inhibits alveolar macrophage cytokine production by CD14-independent pathway. Alcorn, J.F., Wright, J.R. Am. J. Physiol. Lung Cell Mol. Physiol. (2004) [Pubmed]
  23. Surfactant protein C expression in urethane-induced murine pulmonary tumors. Mason, R.J., Kalina, M., Nielsen, L.D., Malkinson, A.M., Shannon, J.M. Am. J. Pathol. (2000) [Pubmed]
  24. Surfactant lipid synthesis and lamellar body formation in glycogen-laden type II cells. Ridsdale, R., Post, M. Am. J. Physiol. Lung Cell Mol. Physiol. (2004) [Pubmed]
  25. Sequential targeted deficiency of SP-A and -D leads to progressive alveolar lipoproteinosis and emphysema. Hawgood, S., Ochs, M., Jung, A., Akiyama, J., Allen, L., Brown, C., Edmondson, J., Levitt, S., Carlson, E., Gillespie, A.M., Villar, A., Epstein, C.J., Poulain, F.R. Am. J. Physiol. Lung Cell Mol. Physiol. (2002) [Pubmed]
  26. FGF-1 and FGF-7 induce distinct patterns of growth and differentiation in embryonic lung epithelium. Cardoso, W.V., Itoh, A., Nogawa, H., Mason, I., Brody, J.S. Dev. Dyn. (1997) [Pubmed]
  27. Surfactant protein-A mRNA expression by human fetal membranes is increased in histological chorioamnionitis but not in spontaneous labour at term. Han, Y.M., Romero, R., Kim, Y.M., Kim, J.S., Richani, K., Friel, L.A., Kusanovic, J.P., Jeanty, C., Vitale, S., Nien, J.K., Espinoza, J., Kim, C.J. J. Pathol. (2007) [Pubmed]
  28. Pulmonary alveolar proteinosis in SCID mice. Jennings, V.M., Dillehay, D.L., Webb, S.K., Brown, L.A. Am. J. Respir. Cell Mol. Biol. (1995) [Pubmed]
  29. Surfactant proteins A and D enhance pulmonary clearance of Pseudomonas aeruginosa. Giannoni, E., Sawa, T., Allen, L., Wiener-Kronish, J., Hawgood, S. Am. J. Respir. Cell Mol. Biol. (2006) [Pubmed]
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