Chapter title |
Lectin Histochemistry for Metastasizing and Non-metastasizing Cancer Cells
|
---|---|
Chapter number | 8 |
Book title |
Histochemistry of Single Molecules
|
Published in |
Methods in molecular biology, February 2017
|
DOI | 10.1007/978-1-4939-6788-9_8 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6787-2, 978-1-4939-6788-9
|
Authors |
Gerrit Wolters-Eisfeld, Udo Schumacher |
Editors |
Carlo Pellicciari, Marco Biggiogera |
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. |
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Unknown | 6 | 43% |