Lectin Histochemistry for Metastasizing and Non-metastasizing Cancer Cells

TY - JOUR

T1 - Lectin Histochemistry for Metastasizing and Non-metastasizing Cancer Cells

AU - Wolters-Eisfeld, Gerrit

AU - Schumacher, Udo

PY - 2017

Y1 - 2017

N2 - 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.

AB - 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.

U2 - 10.1007/978-1-4939-6788-9_8

DO - 10.1007/978-1-4939-6788-9_8

M3 - SCORING: Journal article

C2 - 28155149

VL - 1560

SP - 121

EP - 132

JO - Methods Mol Biol

JF - Methods Mol Biol

SN - 1064-3745

ER -