Skip to main content
SpringerLink
Log in

Immunohistochemical localization of peanut lectin binding sites on human brain tumors as determined by peroxidase-antiperoxidase technique in paraffin sections

  • Original Works
  • Published:
Acta Neuropathologica Aims and scope Submit manuscript

Summary

Peroxidase-antiperoxidase (PAP) technique was selected for visualizing the binding of peanut lectin (PNL) to the most frequent human brain tumors. The randomly selected material included neoplasms of neuroectodermal and mesenchymal origin.

We employed 1–5 μm sections of routinely processed and paraffin-embedded tissues. PNL receptors were detected to a variable extent on the cell surface of astrocytoma, glioblastoma multiforme, oligodendroglioma, ependymoma, meningotheliomatous meningeoma, and plexus papilloma. In gliomas an increase in malignancy seems to be associated with a decrease in PNL binding. Except for the plexus papillomas, neuraminidase pretreatment had neither a qualitative nor a quantitative influence on the binding behavior of PNL.

Intracellular PNL receptors could be detected in “granular cells” and in the perinuclear region of malignant gliomas.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Abrikossoff A (1926) Über Myome, ausgehend von der quergestreiften willkürlichen Muskulatur. Virchows Arch [Pathol Anat] 260:216–233

    Google Scholar 

  • Azzopardi JG (1956) Histogenesis of the granular-cell “myoblastoma”. J Pathol Bacteriol 71:85–94

    Google Scholar 

  • Bernhard W, Avrameas S (1971) Ultrastructural visualization of cellular carbohydrate components by means of Concanavalin A. Exp Cell Res 64:232–236

    Google Scholar 

  • Böck P, Jellinger K (1979) Nachweis sulfatierter Polysaccaride in menschlichen Gliomen. Curr Top Neuropathol 6:35–42

    Google Scholar 

  • Conatas NK, Avrameas W (1973) Detection of plasma membrane carbohydrates with lectin peroxidase conjugates. J Cell Biol 59:436–443

    Google Scholar 

  • Engelhardt A (1980) Detection of acid mucopolysaccharides in human brain tumors by histochemical methods. Acta Neuropathol (Berl) 49:199–203

    Google Scholar 

  • Engelhardt A, Bannasch P (1978) Histochemie saurer Mucopolysaccharide während der Genese Methylmitrosoharnstoff-induzierter Hirntumoren der Ratte. Acta Neuropathol (Berl) 42: 197–204

    Google Scholar 

  • Feyrter F (1952) Über die granulären Neurome (sog. Myoblastenmyome). Virchows Arch [Pathol Anat] 332:66–72

    Google Scholar 

  • Haisken W, Langer E (1962) Die submikroskopischen Strukturen des sog. Myoblastenmyoms (Lipidfibrom, granuläres Neurom). Frankf Z Pathol 71:600–616

    Google Scholar 

  • Hamperl H (1937) Über das Vorkommen von Onkocyten in verschiedenen Organen und ihren Geschwülsten (Mundspeicheldrüsen, Bauchspeicheldrüsen, Epithelkörperchen, Hypophyse, Schilddrüse, Eileiter). Virchows Arch [Pathol Anat] 298:328–375

    Google Scholar 

  • Hori T, Matsutani M, Terao H, Tamura A, Sano K, Nishiyama F, Hirano H (1978) Electron microscopic study of human pituitary tumors using phytohemagglutinin (lectin). Shinkei Geka 18:188–1992

    Google Scholar 

  • Hori T, Matsutani M, Terao H, Sano K, Nishiyama F, Fukuada M, Hirano H (1979) Electron microscopic and cytochemical studies of human pituitary adenomas. J Electron Microsc (Tokyo) 28:249–250

    Google Scholar 

  • Hori T, Nishiyama F, Matsutani M, Teramoto A, Takakura K, Sano K, Hirano H (1982) Lectin-binding sites of the human pituitary adenoma cells by means of the ferritin-labeling technique. Acta Neuropathol (Berl) 56:67–74

    Google Scholar 

  • Irle C (1977) Rapid purification of peanut agglutinin by sialic acidless fetuin-sepharose column. J Immunol Methods 17:117–121

    Google Scholar 

  • Katsuyama T, Spicer SS (1978) Histochemical differentiation of complex carbohydrates with variants of the concanavalin A-horseradish peroxidase method. J Histochem Cytochem 26: 233–250

    Google Scholar 

  • Kiernan JA (1975) Localization of -D-glycosyl and -D-mannosyl groups of mucosubstances with concanavalin A and horseradish peroxidase. Histochemistry 44:39–45

    Google Scholar 

  • Klein PJ, Newman RA, Müller P, Uhlenbruck G, Citoler P, Schaefer HE, Lennartz KJ, Fischer R (1979) The presence and significance of the Thomsen-Friedenreich antigen in mammary gland. J Cancer Res Clin Oncol 93:205–214

    Google Scholar 

  • Köttgen E, Bauer Ch, Reutter W, Gerok W (1979) Neue Ergebnisse zur biologischen und medizinischen Bedeutung von Glykoproteinen. 1. Grundlagen und interdisziplinäre Gesichtspunkte. Klin Wochenschr 57:151–159

    Google Scholar 

  • Köttgen E, Gerok W (1979) Pathobiochemische Aspekte der Wechselwirkung zwischen Glykoproteinen und Glykoproteinrezeptoren. Med Welt 30:20–29

    Google Scholar 

  • Lotan R, Skutelsky E, Danon D, Sharon N (1975) The purification, composition and specifity of the anti-T lectin from peanut (Arachis hypogaea). J Biol Chem 250:8518–8523

    Google Scholar 

  • Margolis RK, Preti G, Lai D, Margolis RU (1976) Developmental changes in brain glycoproteins. Brain Res 112:363–369

    Google Scholar 

  • Martin BJ, Spice SS (1974) Concanavalin A-iron dextran technique for staining cell surface mucosubstances. J Histochem Cytochem 22:206–207

    Google Scholar 

  • Micheau G, Rion G (1975) Oncocytes et oncocytomes (histoenzymologie, ultrastructure et description de l'ADN mitochondrial). Virchows Arch [Pathol Anat] 23:123–132

    Google Scholar 

  • Möller P (1982) Peanut lectin: a useful tool for detecting Hodgkin cells in paraffin sections. Virchows Arch [Pathol Anat] (in press)

  • Müller W, Klein PJ (1979) Über die Anwendung neuerer histochemischer Methoden zur nähreren Charakterisierung von Kohlenhydraten in der Neuropathologie. Curr Top Neuropathol 6:31–34

    Google Scholar 

  • Müller W, Klein PJ, Newman RA, Uhlenbruck G (1980) Histochemical methods for the further characterization of the tumourettes of the posterior lobe of the pituitary. Acta Neuropathol (Berl) 49:101–103

    Google Scholar 

  • Nicolson GL, Singer SJ (1971) Ferritin conjugated plant agglutinins as a specific saccharid stain for electron microscopy: application to saccharides bound to cell membranes. Proc Natl Acad Sci USA 68:942–945

    Google Scholar 

  • Novogrodsky A, Lotan R, Ravid A, Sharon N (1975) Peanut agglutinin, a new mitogen that binds to galactosyl sites exposed after neuraminidase treatment. J Immunol 115:1243–1248

    Google Scholar 

  • Pearse AGE (1956) The histogenesis of granular-cell myoblastoma (granular-cell perineural fibroblastoma). J Pathol Bacteriol 62:351–361

    Google Scholar 

  • Sato A, Spicer SS (1982) Ultrastructural visualization of galactose in the glycoprotein of gastric surface cells with a peanut lectin conjugate. Histochem J 14:125–138

    Google Scholar 

  • Schwechheimer K, Möller P, Schnabel P, Waldherr R (1983) Emphasis on peanut lectin as a marker for granular cells. Virchows Arch [Pathol Anat] 399:289–297

    Google Scholar 

  • Sharon N, Lis H (1972) Lectin cell-agglutinating and sugar-specific proteins. Science 177:949–959

    Google Scholar 

  • Sian CS, Ryan StF (1981) The ultrastructure of neurilemoma with emphasis on Antoni B tissue. Hum Pathol 12:145–160

    Google Scholar 

  • Skutelsky E, Lotan R, Sharon N, Danon D (1977) Distribution of the T-antigen on erythroid cell surfaces; studies with peanut agglutinin, an anti-T specific lectin. Biochim Biophys Acta 467: 165–174

    Google Scholar 

  • Sternberger LA, Hardy PH, Cuculis JJ, Meyer HG (1970) The unlabeled antibody enzyme method of immunohistochemistry: preparation and properties of soluble antigen-antibody complex (horseradish peroxidase antihorseradish peroxidase) and its use in identification of Spirochetes. J Histochem Cytochem 18:315–333

    Google Scholar 

  • Sutoh K, Rosenfeld L, Lee YG (1977) Isolation of peanut lectin affinity chromatography on polyacrylamide-entrapped guar beads and polyacrylamide (Co-allyl-α-D-galacto-pyranoside). Anal Biochem 79:329–337

    Google Scholar 

  • Yokoyama M, Nishiyama F, Kawai N, Hirano H (1980) Ricinus communis agglutinin. Horseradish peroxidase conjugate stains Golgi membranes in mice tissue cells. Exp Cell Res 125:47–53

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institut für Neuropathologie, Universität Heidelberg, Im Neuenheimer Feld 220-221, D-6900, Heidelberg, Germany

    K. Schwechheimer & P. Schnabel

  2. Institut für Allgemeine Pathologie und pathologische Anatomie, Universität Heidelberg, Im Neuenheimer Feld 220-221, D-6900, Heidelberg, Germany

    P. Möller

Authors
  1. K. Schwechheimer
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. P. Schnabel
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. P. Möller
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Schwechheimer, K., Schnabel, P. & Möller, P. Immunohistochemical localization of peanut lectin binding sites on human brain tumors as determined by peroxidase-antiperoxidase technique in paraffin sections. Acta Neuropathol 61, 21–26 (1983). https://doi.org/10.1007/BF00688382

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00688382

Key words

Search

Navigation