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Lectin Histochemistry for Metastasizing and Non-metastasizing Cancer Cells

  • Gerrit Wolters-EisfeldEmail author
  • Udo Schumacher
Protocol
Part of the Methods in Molecular Biology book series (MIMB, volume 1560)

Abstract

Changes in glycosylation of the cancer cell glycocalyx are a hallmark of metastasizing cancers and critically contribute to distant metastasis. In this chapter we concentrate on two lectins capable of specifically binding tumor-associated glycans in cryostat or formalin-fixed, paraffin-embedded tissue sections derived from primary clinical material, genetically engineered mouse models with endogenous cancer formation or xenograft mouse models. The snail lectin of Helix pomatia (HPA) binds N-acetylgalactosamine (GalNAc) that is expressed among others as Tn antigen (O-linked GalNAc) in primary tumors and metastases in several human adenocarcinomas. Another lectin, Phaseolus vulgaris leucoagglutinin (PHA-L) binds to complex β1-6 branched N-linked oligosaccharides associated with increased metastatic potential in breast, colon, and prostate cancer. Using these two lectins both O- and N-linked alterations in the glycocalyx of cancer cells can be monitored. As they are commercially available in a biotinylated or fluorescence-labeled form they can be readily used in cancer metastasis studies.

Key words

Cancer cell glycosylation Clinical studies Helix pomatia agglutin (HPA) Lectin histochemistry Metastasis formation Phaseolus vulgaris leucoagglutinin (PHA-L) Tn antigen Xenograft models 

Notes

Acknowledgment

This work was supported by the German Research Foundation (DFG) grant WO 1967/1-1 to G.W.-E.

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Copyright information

© Springer Science+Business Media LLC 2017

Authors and Affiliations

  1. 1.Medical Glycobiology Group, Department of General, Visceral and Thoracic SurgeryUniversity Medical Center Hamburg-EppendorfHamburgGermany
  2. 2.Department of Anatomy and Experimental MorphologyUniversity Medical Center Hamburg-EppendorfHamburgGermany

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