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SFTPD  -  surfactant protein D

Bos taurus

Synonyms: COLEC7, SP-D
 
 
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Disease relevance of SFTPD

 

High impact information on SFTPD

  • The CDM bound mannose-Sepharose and phosphatidylinositol (PI) as well as SP-D, but the binding to mannosyl bovine serum albumin and glucosylceramide was diminished by approximately 60% [3].
  • Surfactant protein D (SP-D) is a member of the C-type lectin superfamily with four distinct structural domains: an amino terminus involved in forming intermolecular disulfides, a collagen-like domain, a neck region, and a carbohydrate recognition domain [3].
  • The N-terminal sequence (27 amino acids) showed 56% identity with bovine SP-D and 44% identity to bovine conglutinin [4].
  • Surfactant protein D (SP-D) is a carbohydrate-binding glycoprotein containing a collagen-like domain that is synthesized by alveolar type II epithelial cells [5].
  • There are 6 cysteine residues present in rat SP-D: 2 in the NH2-terminal noncollagenous segment and 4 in the COOH-terminal carbohydrate-binding domain [5].
 

Biological context of SFTPD

  • The derived amino acid sequence for bovine SP-D shows a higher (78%) level of identity to the sequence of conglutinin than to the sequence of human or rat SP-D (67 and 65% respectively) [6].
  • With the perspective of being able to identify surfactant protein D (SP-D) polymorphisms associated with immune-compromised phenotypes in cattle, we have characterized the gene encoding bovine SP-D and its proximal promoter [7].
  • In addition, SP-D inhibits the generation of radical oxygen species or the propagation of lipid peroxidation [2].
  • Using a set of IAV strains that differed in the level and site of glycosylation, and a panel of recombinant collectins, we found that binding of SP-D to the globular domain of the HA was critical in mediating the inhibition of viral haemagglutination activity and infectivity [8].
  • Specific binding to FA chains was also demonstrated by solution phase competition for FA binding to acrylodan-labeled FA binding protein (ADIFAB), and by overlay of thin layer chromatograms with SP-D [9].
 

Anatomical context of SFTPD

 

Associations of SFTPD with chemical compounds

  • The most efficient inhibitors of SP-D binding were alpha-glucosyl-containing saccharides (e.g. isomaltose, maltose, malotriose) [10].
  • SP-D showed quantitative binding to maltosyl-agarose and was specifically eluted with maltose or EDTA [10].
 

Other interactions of SFTPD

  • Since SP-D appears to be a lung-specific protein, it seems probable that the liver is the primary site of synthesis of conglutinin [6].
  • Of interest, the expression of the BC mRNA, as determined by RNase protection assay, is restricted to liver, unlike bovine SP-D, a lung-surfactant protein [11].
  • CL-43, lung surfactant protein D (SP-D) and conglutinin showed no complement-activating properties under the same conditions [12].
 

Analytical, diagnostic and therapeutic context of SFTPD

  • The use of a polymerase chain reaction (PCR)-derived DNA probe for bovine SP-D in Northern blotting studies yielded a signal from bovine liver mRNA as well as the expected signal from bovine lung mRNA [6].
  • On gel-filtration, a proportion of the SP-D preparation behaved, as expected, as a molecule with an apparent molecular mass of 600 kDa [13].
  • A collagen domain deletion mutant (CDM) of SP-D was created by site-directed mutagenesis [3].
  • Saccharide-substituted bovine serum albumins (BSA neoglycoproteins) were adsorbed to plastic wells, and binding of purified SP-D was quantified with monospecific antibodies to SP-D using an indirect immunoassay [10].

References

  1. Structure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus. Eda, S., Suzuki, Y., Kawai, T., Ohtani, K., Kase, T., Fujinaga, Y., Sakamoto, T., Kurimura, T., Wakamiya, N. Biochem. J. (1997) [Pubmed]
  2. Lung surfactant protein D (SP-D) and the molecular diverted descendants: conglutinin, CL-43 and CL-46. Hansen, S., Holmskov, U. Immunobiology (2002) [Pubmed]
  3. The role of the amino-terminal domain and the collagenous region in the structure and the function of rat surfactant protein D. Ogasawara, Y., Voelker, D.R. J. Biol. Chem. (1995) [Pubmed]
  4. Purification and characterization of a bovine serum lectin (CL-43) with structural homology to conglutinin and SP-D and carbohydrate specificity similar to mannan-binding protein. Holmskov, U., Teisner, B., Willis, A.C., Reid, K.B., Jensenius, J.C. J. Biol. Chem. (1993) [Pubmed]
  5. Primary structure of rat pulmonary surfactant protein D. cDNA and deduced amino acid sequence. Shimizu, H., Fisher, J.H., Papst, P., Benson, B., Lau, K., Mason, R.J., Voelker, D.R. J. Biol. Chem. (1992) [Pubmed]
  6. Structural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutinin. Lim, B.L., Lu, J., Reid, K.B. Immunology (1993) [Pubmed]
  7. Genomic and molecular characterization of bovine surfactant protein D (SP-D). Gjerstorff, M., Madsen, J., Bendixen, C., Holmskov, U., Hansen, S. Mol. Immunol. (2004) [Pubmed]
  8. Mechanism of binding of surfactant protein D to influenza A viruses: importance of binding to haemagglutinin to antiviral activity. Hartshorn, K.L., White, M.R., Voelker, D.R., Coburn, J., Zaner, K., Crouch, E.C. Biochem. J. (2000) [Pubmed]
  9. Interactions of surfactant protein D with fatty acids. DeSilva, N.S., Ofek, I., Crouch, E.C. Am. J. Respir. Cell Mol. Biol. (2003) [Pubmed]
  10. Surfactant protein D is a divalent cation-dependent carbohydrate-binding protein. Persson, A., Chang, D., Crouch, E. J. Biol. Chem. (1990) [Pubmed]
  11. Bovine conglutinin (BC) mRNA expressed in liver: cloning and characterization of the BC cDNA reveals strong homology to surfactant protein-D. Liou, L.S., Sastry, R., Hartshorn, K.L., Lee, Y.M., Okarma, T.B., Tauber, A.I., Sastry, K.N. Gene (1994) [Pubmed]
  12. Comparative study of the structural and functional properties of a bovine plasma C-type lectin, collectin-43, with other collectins. Holmskov, U., Laursen, S.B., Malhotra, R., Wiedemann, H., Timpl, R., Stuart, G.R., Tornøe, I., Madsen, P.S., Reid, K.B., Jensenius, J.C. Biochem. J. (1995) [Pubmed]
  13. Structural similarity between lung surfactant protein D and conglutinin. Two distinct, C-type lectins containing collagen-like sequences. Lu, J., Wiedemann, H., Holmskov, U., Thiel, S., Timpl, R., Reid, K.B. Eur. J. Biochem. (1993) [Pubmed]
 
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