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. 1985 Feb;118(2):325–330.

Lectin binding in membranoproliferative glomerulonephritis. Evidence for N-acetylglucosamine in dense intramembranous deposits.

T E Nevins
PMCID: PMC1887868  PMID: 3838220

Abstract

Type II membranoproliferative glomerulonephritis (MPGN-II) is characterized by electron-dense intramembranous deposits (DIMD) in the basal laminae of the kidney. These deposits selectively bind the lectin wheat germ agglutinin (WGA) or its succinylated derivative. In renal tissue samples from normal controls, Type I membranoproliferative glomerulonephritis, and several other renal diseases, only a normal pattern of WGA binding was observed and no membrane-oriented deposits reacted with WGA. Additional attempts to stain the DIMD with any of eight other lectins or eight antisera to renal antigens were uniformly unsuccessful. Discrete WGA reactivity indicates that the deposits contain appreciable quantities of internally linked N-acetylglucosamine and may also provide a valuable adjunct in making the histologic diagnosis of MPGN-II.

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Selected References

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  1. BERGER J., GALLE P. [Unusual change of the basal membranes of the kidney]. J Urol Nephrol (Paris) 1962 Jan-Feb;68:116–122. [PubMed] [Google Scholar]
  2. Bhavanandan V. P., Katlic A. W. The interaction of wheat germ agglutinin with sialoglycoproteins. The role of sialic acid. J Biol Chem. 1979 May 25;254(10):4000–4008. [PubMed] [Google Scholar]
  3. Bog-Hansen T. C., Bjerrum O. J., Brogren C. H. Identification and quantification of glycoproteins by affinity electrophoresis. Anal Biochem. 1977 Jul;81(1):78–87. doi: 10.1016/0003-2697(77)90600-5. [DOI] [PubMed] [Google Scholar]
  4. Carlin B., Jaffe R., Bender B., Chung A. E. Entactin, a novel basal lamina-associated sulfated glycoprotein. J Biol Chem. 1981 May 25;256(10):5209–5214. [PubMed] [Google Scholar]
  5. Churg J., Duffy J. L., Bernstein J. Identification of dense deposit disease: a report for the International Study of Kidney Diseases in Children. Arch Pathol Lab Med. 1979 Feb;103(2):67–72. [PubMed] [Google Scholar]
  6. Date A., Neela P., Shastry J. C. Thioflavin T fluorescence in membranoproliferative glomerulonephritis. Nephron. 1982;32(1):90–92. doi: 10.1159/000182813. [DOI] [PubMed] [Google Scholar]
  7. Eddy A., Sibley R., Mauer S. M., Kim Y. Renal allograft failure due to recurrent dense intramembranous deposit disease. Clin Nephrol. 1984 Jun;21(6):305–313. [PubMed] [Google Scholar]
  8. Etzler M. E., Branstrator M. L. Differential localization of cell surface and secretory components in rat intestinal epithelium by use of lectins. J Cell Biol. 1974 Aug;62(2):329–343. doi: 10.1083/jcb.62.2.329. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Falk R. J., Dalmasso A. P., Kim Y., Tsai C. H., Scheinman J. I., Gewurz H., Michael A. F. Neoantigen of the polymerized ninth component of complement. Characterization of a monoclonal antibody and immunohistochemical localization in renal disease. J Clin Invest. 1983 Aug;72(2):560–573. doi: 10.1172/JCI111004. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Faraggiana T., Malchiodi F., Prado A., Churg J. Lectin-peroxidase conjugate reactivity in normal human kidney. J Histochem Cytochem. 1982 May;30(5):451–458. doi: 10.1177/30.5.7077075. [DOI] [PubMed] [Google Scholar]
  11. Freeman H. J., Lotan R., Kim Y. S. Application of lectins for detection of goblet cell glycoconjugate differences in proximal and distal colon of the rat. Lab Invest. 1980 Apr;42(4):405–412. [PubMed] [Google Scholar]
  12. Galle P., Mahieu P. Electron dense alteration of kidney basement membranes. A renal lesion specific of a systemic disease. Am J Med. 1975 Jun;58(6):749–764. doi: 10.1016/0002-9343(75)90631-2. [DOI] [PubMed] [Google Scholar]
  13. Goldstein I. J., Hayes C. E. The lectins: carbohydrate-binding proteins of plants and animals. Adv Carbohydr Chem Biochem. 1978;35:127–340. doi: 10.1016/s0065-2318(08)60220-6. [DOI] [PubMed] [Google Scholar]
  14. Habib R., Gubler M. C., Loirat C., Mäiz H. B., Levy M. Dense deposit disease: a variant of membranoproliferative glomerulonephritis. Kidney Int. 1975 Apr;7(4):204–215. doi: 10.1038/ki.1975.32. [DOI] [PubMed] [Google Scholar]
  15. Holthöfer H., Virtanen I., Pettersson E., Törnroth T., Alfthan O., Linder E., Miettinen A. Lectins as fluorescence microscopic markers for saccharides in the human kidney. Lab Invest. 1981 Nov;45(5):391–399. [PubMed] [Google Scholar]
  16. Jakobovits A., Eshdat Y., Sharon N. Plucking of lectin receptors from erythrocytes: isolation of cell surface components without the use of detergents. Biochem Biophys Res Commun. 1981 Jun;100(4):1484–1490. doi: 10.1016/0006-291x(81)90686-0. [DOI] [PubMed] [Google Scholar]
  17. Kahane I., Furthmayr H., Marchesi V. T. Isolation of membrane glycoproteins by affinity chromatography in the presence of detergents. Biochim Biophys Acta. 1976 Mar 19;426(3):464–476. doi: 10.1016/0005-2736(76)90391-6. [DOI] [PubMed] [Google Scholar]
  18. Kim Y., Vernier R. L., Fish A. J., Michael A. F. Immunofluorescence studies of dense deposit disease. The presence of railroad tracks and mesangial rings. Lab Invest. 1979 Apr;40(4):474–480. [PubMed] [Google Scholar]
  19. Lotan R., Nicolson G. L. Purification of cell membrane glycoproteins by lectin affinity chromatography. Biochim Biophys Acta. 1979 Dec 20;559(4):329–376. doi: 10.1016/0304-4157(79)90010-8. [DOI] [PubMed] [Google Scholar]
  20. Lyer P. N., Wilkinson K. D., Goldstein L. J. An -N-acetyl-D-glycosamine binding lectin from Bandeiraea simplicifolia seeds. Arch Biochem Biophys. 1976 Nov;177(1):330–333. doi: 10.1016/0003-9861(76)90444-6. [DOI] [PubMed] [Google Scholar]
  21. McGregor J. L., Clemetson K. J., James E., Greenland T., Dechavanne M. Identification of human platelet glycoproteins in SDS-polyacrylamide gels using 125I labelled lectins. Thromb Res. 1979;16(5-6):825–831. doi: 10.1016/0049-3848(79)90225-1. [DOI] [PubMed] [Google Scholar]
  22. Michael A. F., Yang J. Y., Falk R. J., Bennington M. J., Scheinman J. I., Vernier R. L., Fish A. J. Monoclonal antibodies to human renal basement membranes: heterogenic and ontogenic changes. Kidney Int. 1983 Jul;24(1):74–86. doi: 10.1038/ki.1983.128. [DOI] [PubMed] [Google Scholar]
  23. Miller K., Michael A. F. Immunopathology of renal extracellular membranes in diabetes mellitus. Specificity of tubular basement-membrane immunofluorescence. Diabetes. 1976 Aug;25(8):701–708. doi: 10.2337/diab.25.8.701. [DOI] [PubMed] [Google Scholar]
  24. Monsigny M., Roche A. C., Sene C., Maget-Dana R., Delmotte F. Sugar-lectin interactions: how does wheat-germ agglutinin bind sialoglycoconjugates? Eur J Biochem. 1980 Feb;104(1):147–153. doi: 10.1111/j.1432-1033.1980.tb04410.x. [DOI] [PubMed] [Google Scholar]
  25. Nagata Y., Burger M. M. Wheat germ agglutinin. Molecular characteristics and specificity for sugar binding. J Biol Chem. 1974 May 25;249(10):3116–3122. [PubMed] [Google Scholar]
  26. Peters B. P., Ebisu S., Goldstein I. J., Flashner M. Interaction of wheat germ agglutinin with sialic acid. Biochemistry. 1979 Nov 27;18(24):5505–5511. doi: 10.1021/bi00591a038. [DOI] [PubMed] [Google Scholar]
  27. Peters B. P., Goldstein I. J. The use of fluorescein-conjugated Bandeiraea simplicifolia B4-isolectin as a histochemical reagent for the detection of alpha-D-galactopyranosyl groups. Their occurrence in basement membranes. Exp Cell Res. 1979 May;120(2):321–334. doi: 10.1016/0014-4827(79)90392-6. [DOI] [PubMed] [Google Scholar]
  28. Pukel C. S., Lloyd K. O., Travassos L. R., Dippold W. G., Oettgen H. F., Old L. J. GD3, a prominent ganglioside of human melanoma. Detection and characterisation by mouse monoclonal antibody. J Exp Med. 1982 Apr 1;155(4):1133–1147. doi: 10.1084/jem.155.4.1133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Sharon N., Lis H. Lectins: cell-agglutinating and sugar-specific proteins. Science. 1972 Sep 15;177(4053):949–959. doi: 10.1126/science.177.4053.949. [DOI] [PubMed] [Google Scholar]
  30. Ueda R., Ogata S., Morrissey D. M., Finstad C. L., Szkudlarek J., Whitmore W. F., Oettgen H. F., Lloyd K. O., Old L. J. Cell surface antigens of human renal cancer defined by mouse monoclonal antibodies: identification of tissue-specific kidney glycoproteins. Proc Natl Acad Sci U S A. 1981 Aug;78(8):5122–5126. doi: 10.1073/pnas.78.8.5122. [DOI] [PMC free article] [PubMed] [Google Scholar]

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