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. 1993 Jan;78(1):159–165.

Structural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutinin.

B L Lim 1, J Lu 1, K B Reid 1
PMCID: PMC1421780  PMID: 8436402

Abstract

Conglutinin is a Ca(2+)-dependent, carbohydrate-binding, serum protein which contains an N-terminal collagen-like region and a C-terminal, C-type lectin domain. To date, conglutinin, which appears to play an important role in defence mechanisms, has been fully described, by protein sequence analysis, only in the bovine system. To allow comparison of lung surfactant protein D (SP-D) with conglutinin, within one species, a full-length cDNA clone for SP-D has been isolated from a bovine lung library. 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). However, SP-D and conglutinin are known to have different carbohydrate-binding specificities, therefore some of the 16 residues conserved in the C-type lectin domains of all three species of SP-D, but which are not conserved in conglutinin, appear likely to be involved in determination of specificity. 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. Since SP-D appears to be a lung-specific protein, it seems probable that the liver is the primary site of synthesis of conglutinin.

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Selected References

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  1. Baatrup G., Thiel S., Isager H., Svehag S. E., Jensenius J. C. Demonstration in human plasma of a lectin activity analogous to that of bovine conglutinin. Scand J Immunol. 1987 Oct;26(4):355–361. doi: 10.1111/j.1365-3083.1987.tb02267.x. [DOI] [PubMed] [Google Scholar]
  2. Barondes S. H. Bifunctional properties of lectins: lectins redefined. Trends Biochem Sci. 1988 Dec;13(12):480–482. doi: 10.1016/0968-0004(88)90235-6. [DOI] [PubMed] [Google Scholar]
  3. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem. 1987 Apr;162(1):156–159. doi: 10.1006/abio.1987.9999. [DOI] [PubMed] [Google Scholar]
  4. Crouch E., Rust K., Persson A., Mariencheck W., Moxley M., Longmore W. Primary translation products of pulmonary surfactant protein D. Am J Physiol. 1991 Apr;260(4 Pt 1):L247–L253. doi: 10.1152/ajplung.1991.260.4.L247. [DOI] [PubMed] [Google Scholar]
  5. Dedhar S., Ruoslahti E., Pierschbacher M. D. A cell surface receptor complex for collagen type I recognizes the Arg-Gly-Asp sequence. J Cell Biol. 1987 Mar;104(3):585–593. doi: 10.1083/jcb.104.3.585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Drickamer K., Dordal M. S., Reynolds L. Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein. J Biol Chem. 1986 May 25;261(15):6878–6887. [PubMed] [Google Scholar]
  7. Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J Biol Chem. 1988 Jul 15;263(20):9557–9560. [PubMed] [Google Scholar]
  8. Friis-Christiansen P., Thiel S., Svehag S. E., Dessau R., Svendsen P., Andersen O., Laursen S. B., Jensenius J. C. In vivo and in vitro antibacterial activity of conglutinin, a mammalian plasma lectin. Scand J Immunol. 1990 Apr;31(4):453–460. doi: 10.1111/j.1365-3083.1990.tb02792.x. [DOI] [PubMed] [Google Scholar]
  9. Glasser S. W., Korfhagen T. R., Weaver T., Pilot-Matias T., Fox J. L., Whitsett J. A. cDNA and deduced amino acid sequence of human pulmonary surfactant-associated proteolipid SPL(Phe). Proc Natl Acad Sci U S A. 1987 Jun;84(12):4007–4011. doi: 10.1073/pnas.84.12.4007. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Haagsman H. P., Sargeant T., Hauschka P. V., Benson B. J., Hawgood S. Binding of calcium to SP-A, a surfactant-associated protein. Biochemistry. 1990 Sep 25;29(38):8894–8900. doi: 10.1021/bi00490a003. [DOI] [PubMed] [Google Scholar]
  11. Hawgood S., Benson B. J., Schilling J., Damm D., Clements J. A., White R. T. Nucleotide and amino acid sequences of pulmonary surfactant protein SP 18 and evidence for cooperation between SP 18 and SP 28-36 in surfactant lipid adsorption. Proc Natl Acad Sci U S A. 1987 Jan;84(1):66–70. doi: 10.1073/pnas.84.1.66. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hawgood S., Clements J. A. Pulmonary surfactant and its apoproteins. J Clin Invest. 1990 Jul;86(1):1–6. doi: 10.1172/JCI114670. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Heery D. M., Gannon F., Powell R. A simple method for subcloning DNA fragments from gel slices. Trends Genet. 1990 Jun;6(6):173–173. doi: 10.1016/0168-9525(90)90158-3. [DOI] [PubMed] [Google Scholar]
  14. Holmskov U., Teisner B., Pedersen N. T., Laursen S. B., Rasmussen H. B., Jensenius J. C. Tissue localization of conglutinin, a bovine C-type lectin. Immunology. 1992 May;76(1):169–173. [PMC free article] [PubMed] [Google Scholar]
  15. Kuan S. F., Rust K., Crouch E. Interactions of surfactant protein D with bacterial lipopolysaccharides. Surfactant protein D is an Escherichia coli-binding protein in bronchoalveolar lavage. J Clin Invest. 1992 Jul;90(1):97–106. doi: 10.1172/JCI115861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Lee Y. M., Leiby K. R., Allar J., Paris K., Lerch B., Okarma T. B. Primary structure of bovine conglutinin, a member of the C-type animal lectin family. J Biol Chem. 1991 Feb 15;266(5):2715–2723. [PubMed] [Google Scholar]
  17. Loveless R. W., Feizi T., Childs R. A., Mizuochi T., Stoll M. S., Oldroyd R. G., Lachmann P. J. Bovine serum conglutinin is a lectin which binds non-reducing terminal N-acetylglucosamine, mannose and fucose residues. Biochem J. 1989 Feb 15;258(1):109–113. doi: 10.1042/bj2580109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Lu J., Willis A. C., Reid K. B. Purification, characterization and cDNA cloning of human lung surfactant protein D. Biochem J. 1992 Jun 15;284(Pt 3):795–802. doi: 10.1042/bj2840795. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Malhotra R., Thiel S., Reid K. B., Sim R. B. Human leukocyte C1q receptor binds other soluble proteins with collagen domains. J Exp Med. 1990 Sep 1;172(3):955–959. doi: 10.1084/jem.172.3.955. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Persson A., Chang D., Crouch E. Surfactant protein D is a divalent cation-dependent carbohydrate-binding protein. J Biol Chem. 1990 Apr 5;265(10):5755–5760. [PubMed] [Google Scholar]
  21. Persson A., Chang D., Rust K., Moxley M., Longmore W., Crouch E. Purification and biochemical characterization of CP4 (SP-D), a collagenous surfactant-associated protein. Biochemistry. 1989 Jul 25;28(15):6361–6367. doi: 10.1021/bi00441a031. [DOI] [PubMed] [Google Scholar]
  22. Persson A., Rust K., Chang D., Moxley M., Longmore W., Crouch E. CP4: a pneumocyte-derived collagenous surfactant-associated protein. Evidence for heterogeneity of collagenous surfactant proteins. Biochemistry. 1988 Nov 15;27(23):8576–8584. doi: 10.1021/bi00423a011. [DOI] [PubMed] [Google Scholar]
  23. Possmayer F. A proposed nomenclature for pulmonary surfactant-associated proteins. Am Rev Respir Dis. 1988 Oct;138(4):990–998. doi: 10.1164/ajrccm/138.4.990. [DOI] [PubMed] [Google Scholar]
  24. Ruoslahti E., Pierschbacher M. D. New perspectives in cell adhesion: RGD and integrins. Science. 1987 Oct 23;238(4826):491–497. doi: 10.1126/science.2821619. [DOI] [PubMed] [Google Scholar]
  25. Rust K., Grosso L., Zhang V., Chang D., Persson A., Longmore W., Cai G. Z., Crouch E. Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain. Arch Biochem Biophys. 1991 Oct;290(1):116–126. doi: 10.1016/0003-9861(91)90597-c. [DOI] [PubMed] [Google Scholar]
  26. Sano K., Fisher J., Mason R. J., Kuroki Y., Schilling J., Benson B., Voelker D. Isolation and sequence of a cDNA clone for the rat pulmonary surfactant-associated protein (PSP-A). Biochem Biophys Res Commun. 1987 Apr 14;144(1):367–374. doi: 10.1016/s0006-291x(87)80519-3. [DOI] [PubMed] [Google Scholar]
  27. Shimizu H., Fisher J. H., Papst P., Benson B., Lau K., Mason R. J., Voelker D. R. Primary structure of rat pulmonary surfactant protein D. cDNA and deduced amino acid sequence. J Biol Chem. 1992 Jan 25;267(3):1853–1857. [PubMed] [Google Scholar]
  28. Strang C. J., Slayter H. S., Lachmann P. J., Davis A. E., 3rd Ultrastructure and composition of bovine conglutinin. Biochem J. 1986 Mar 1;234(2):381–389. doi: 10.1042/bj2340381. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Warr R. G., Hawgood S., Buckley D. I., Crisp T. M., Schilling J., Benson B. J., Ballard P. L., Clements J. A., White R. T. Low molecular weight human pulmonary surfactant protein (SP5): isolation, characterization, and cDNA and amino acid sequences. Proc Natl Acad Sci U S A. 1987 Nov;84(22):7915–7919. doi: 10.1073/pnas.84.22.7915. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Weis W. I., Kahn R., Fourme R., Drickamer K., Hendrickson W. A. Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing. Science. 1991 Dec 13;254(5038):1608–1615. doi: 10.1126/science.1721241. [DOI] [PubMed] [Google Scholar]

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