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Gene Review

Sftpd  -  surfactant protein D

Rattus norvegicus

Synonyms: CP4, Lung surfactant protein D, PSP-D, Pulmonary surfactant-associated protein D, SP-D, ...
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Disease relevance of Sftpd

  • Wild-type B. pertussis and B. bronchiseptica were both resistant to SP-D; however, LPS mutants of either strain lacking the terminal trisaccharide were aggregated and permeabilized by SP-D [1].
  • We conclude that the terminal trisaccharide protects Bordetella species from the bactericidal functions of SP-A and SP-D [1].
  • We hypothesized that SP-A and SP-D would respond to an acute stress, such as lung inflammation, in the same manner as does mannose-binding protein, with increased messenger ribonucleic acid (mRNA) and protein production [2].
  • We also found that the relative content of SP-D was significantly higher in PCP (24,249 +/- 4780 grey values) than that in the negative control (13,384 +/- 2887 grey values, P < 0.001) and that in bacterial pneumonia (11,989 +/- 2750 grey values, P < 0.001) [3].
  • Twenty-one hours after ischemia, axonal damage was reduced by 45% (P = 0.006) in the SPD 502-treated group compared with the vehicle [4].

Psychiatry related information on Sftpd

  • The REM (rapid eye movement) sleep stage was significantly shortened without a marked change of the Non-REM sleep from the 24th to the 32nd hr following injection of 40 microgram of SPD [5].

High impact information on Sftpd

  • Lastly, we show that SP-D augments binding of P. carinii to alveolar macrophages, but does not significantly enhance macrophage phagocytosis of the organism [6].
  • Accordingly, we evaluated the extent and localization of SP-D in the lower respiratory tract during Pneumocystis pneumonia in an immunosuppressed rat model and examined its role in modulating interaction of P. carinii with macrophages [6].
  • We report that SP-D is a major component of the alveolar exudates that typify P. carinii pneumonia and is present bound to the surface of P. carinii organisms in vivo [6].
  • The interaction of SP-D with gpA represents an additional important component of the host-parasite relationship during P. carinii pneumonia [6].
  • Surfactant protein D (SP-D) is a recently described component of the airspace lining material that possesses a calcium-dependent lectin domain capable of interacting with glycoconjugates present on microorganisms and leukocytes [6].

Chemical compound and disease context of Sftpd


Biological context of Sftpd


Anatomical context of Sftpd

  • Heterogeneous allele expression of pulmonary SP-D gene in rat large intestine and other tissues [9].
  • Immunoperoxidase localization of SP-D studies at 2 weeks after silica instillation showed intense staining of intra-alveolar exudates, and cytoplasmic staining of hypertrophic type II cells [10].
  • Immunoelectron microscopy showed that airspace SP-D was specifically associated with granular material, but not tubular myelin or other membranous structures [10].
  • Surfactant proteins A (SP-A) and D (SP-D) are lung collectins that are constituents of the innate immune system of the lung [14].
  • The opsonic activities of SP-A and SP-D for bacteria with different types of LPS and alveolar macrophages were investigated [13].

Associations of Sftpd with chemical compounds

  • SP-D decreased CD14 binding to both smooth and rough LPS, whereas SP-A enhanced CD14 binding to rough LPS and inhibited binding to smooth LPS [14].
  • Chimera A1A2D3D4 competed with iodinated SP-D in the solid phase binding assay to both PI and GlcCer [12].
  • Mannose and EDTA inhibited SP-D binding to CD14 but did not decrease SP-A binding [14].
  • Both proteins are composed of four characteristic domains which are: 1) an NH2-terminal domain involved in interchain disulfide formation (denoted A1 domain for SP-A or D1 for SP-D); 2) a collagenous domain (denoted A2 or D2); 3) a neck domain (denoted A3 or D3); and 4) a carbohydrate recognition domain (denoted A4 or D4) [12].
  • Here we report that newborn rats, which can adapt to even higher levels of hyperoxia (100% O(2)) than do adult rats, manifest changes in the lung surfactant proteins (SP), especially SP-A and SP-D [15].

Other interactions of Sftpd

  • In situ hybridization studies demonstrated increases in SP-D, and to a lesser extent in SP-A, in peripheral lung tissues from oxygen-exposed newborns [15].
  • This pattern of SP-D mRNA expression was compared with the expression of the other surfactant proteins and found to be most similar to that of SP-B [16].
  • By contrast, SP-C and SP-D mRNAs were maximally increased relative to values in simultaneously air-exposed control rats after 4 d of exposure [15].
  • We investigated the cellular and subcellular distribution of surfactant protein D (SP-D) by immunogold labeling in lungs of adult rats that had been given bovine serum albumin coupled to 5-nm gold (BSAG) for 2 hr to visualize the endocytotic pathway [17].

Analytical, diagnostic and therapeutic context of Sftpd

  • Within 2 weeks after silica instillation, there was a greater than 45-fold increase in lavage SP-D per lung compared with saline controls, including an almost ten-fold increase in the insoluble or surfactant-associated protein [10].
  • SP-D was quantified in bronchoalveolar lavage by immunoassay using antibodies specific for SP-D, and by reversephase HPLC after affinity purification of SP-D on maltosyl-agarose [10].
  • These studies indicate that the extracellular accumulation of SP-D is markedly increased in silica-induced lipoproteinosis, and that SP-D is associated with amorphous components identified by electron microscopy [10].
  • The authors examined the accumulation of SP-D using this animal model of alveolar proteinosis [10].
  • SP-D mRNA expression was evaluated by Northern blot analysis [16].


  1. Interactions of pulmonary collectins with Bordetella bronchiseptica and Bordetella pertussis lipopolysaccharide elucidate the structural basis of their antimicrobial activities. Schaeffer, L.M., McCormack, F.X., Wu, H., Weiss, A.A. Infect. Immun. (2004) [Pubmed]
  2. Surfactant proteins A and D increase in response to intratracheal lipopolysaccharide. McIntosh, J.C., Swyers, A.H., Fisher, J.H., Wright, J.R. Am. J. Respir. Cell Mol. Biol. (1996) [Pubmed]
  3. Alteration of surfactant proteins A and D in bronchoalveolar lavage fluid of Pneumocystis carinii pneumonia. Qu, J., He, L., Rong, Z., Pan, J., Chen, X., Morrison, D.C., Li, X. Chin. Med. J. (2001) [Pubmed]
  4. Grey matter and white matter ischemic damage is reduced by the competitive AMPA receptor antagonist, SPD 502. McCracken, E., Fowler, J.H., Dewar, D., Morrison, S., McCulloch, J. J. Cereb. Blood Flow Metab. (2002) [Pubmed]
  5. Effects of intraventricularly administered polyamines spermidine and spermine on sleep-wakefulness cycles in rats. Sakurada, T., Kisara, K. Jpn. J. Pharmacol. (1978) [Pubmed]
  6. Surfactant protein D interacts with Pneumocystis carinii and mediates organism adherence to alveolar macrophages. O'Riordan, D.M., Standing, J.E., Kwon, K.Y., Chang, D., Crouch, E.C., Limper, A.H. J. Clin. Invest. (1995) [Pubmed]
  7. Increased surfactant protein D in rat airway goblet and Clara cells during ovalbumin-induced allergic airway inflammation. Kasper, M., Sims, G., Koslowski, R., Kuss, H., Thuemmler, M., Fehrenbach, H., Auten, R.L. Clin. Exp. Allergy (2002) [Pubmed]
  8. The feeding value of soybeans fed to rats, chickens, catfish and dairy cattle is not altered by genetic incorporation of glyphosate tolerance. Hammond, B.G., Vicini, J.L., Hartnell, G.F., Naylor, M.W., Knight, C.D., Robinson, E.H., Fuchs, R.L., Padgette, S.R. J. Nutr. (1996) [Pubmed]
  9. Heterogeneous allele expression of pulmonary SP-D gene in rat large intestine and other tissues. Lin, Z., Floros, J. Physiol. Genomics (2002) [Pubmed]
  10. Surfactant protein D. Increased accumulation in silica-induced pulmonary lipoproteinosis. Crouch, E., Persson, A., Chang, D., Parghi, D. Am. J. Pathol. (1991) [Pubmed]
  11. Analysis of chimeric proteins identifies the regions in the carbohydrate recognition domains of rat lung collectins that are essential for interactions with phospholipids, glycolipids, and alveolar type II cells. Sano, H., Kuroki, Y., Honma, T., Ogasawara, Y., Sohma, H., Voelker, D.R., Akino, T. J. Biol. Chem. (1998) [Pubmed]
  12. Chimeras of surfactant proteins A and D identify the carbohydrate recognition domains as essential for phospholipid interaction. Ogasawara, Y., McCormack, F.X., Mason, R.J., Voelker, D.R. J. Biol. Chem. (1994) [Pubmed]
  13. Opsonic activities of surfactant proteins A and D in phagocytosis of gram-negative bacteria by alveolar macrophages. Pikaar, J.C., Voorhout, W.F., van Golde, L.M., Verhoef, J., Van Strijp, J.A., van Iwaarden, J.F. J. Infect. Dis. (1995) [Pubmed]
  14. Surfactant proteins A and D bind CD14 by different mechanisms. Sano, H., Chiba, H., Iwaki, D., Sohma, H., Voelker, D.R., Kuroki, Y. J. Biol. Chem. (2000) [Pubmed]
  15. Elevated expression of surfactant proteins in newborn rats during adaptation to hyperoxia. White, C.W., Greene, K.E., Allen, C.B., Shannon, J.M. Am. J. Respir. Cell Mol. Biol. (2001) [Pubmed]
  16. Regulation of surfactant protein D expression by glucocorticoids in vitro and in vivo. Deterding, R.R., Shimizu, H., Fisher, J.H., Shannon, J.M. Am. J. Respir. Cell Mol. Biol. (1994) [Pubmed]
  17. Immunocytochemical localization of surfactant protein D (SP-D) in type II cells, Clara cells, and alveolar macrophages of rat lung. Voorhout, W.F., Veenendaal, T., Kuroki, Y., Ogasawara, Y., van Golde, L.M., Geuze, H.J. J. Histochem. Cytochem. (1992) [Pubmed]
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