Lectin histochemistry of murine WAP-T mammary cancer reveals similar glycoconjugate changes to those in human breast cancer

TY - JOUR

T1 - Lectin histochemistry of murine WAP-T mammary cancer reveals similar glycoconjugate changes to those in human breast cancer

AU - Schreiber, Steffen

AU - Gocht, Andreas

AU - Wegwitz, Florian

AU - Deppert, Wolfgang

AU - Schumacher, Udo

N1 - Copyright© 2014 International Institute of Anticancer Research (Dr. John G. Delinassios), All rights reserved.

PY - 2014/12/1

Y1 - 2014/12/1

N2 - BACKGROUND: The WAP-T mouse model is an established clinically relevant model of breast cancer. Lectins have been used to study malignant progression in clinical studies. We investigated lectin binding sites to test for the clinical relevance of this model.MATERIALS AND METHODS: Samples of the WAP-T mouse mammary tissues, from normal tissues to undifferentiated higher tumor grades were stained using an indirect technique with nine different lectins for intensity of lectin binding.RESULTS: HPA bound to the luminal epithelium in higher tumor grades in a similar pattern to that in human breast cancer. BSA-IB4 bound to luminal epithelium in hyperplasia and increased towards higher grades, comparable to previous clinical studies. PHA-L-binding to myoepithelium and luminal epithelium increased from hyperplasia to higher grades, comparable to findings in human breast cancer.CONCLUSION: The results of our study support the hypothesis that lectin binding sites change similarly in WAP-T and human breast cancer, stressing the similarity of this model with the clinical setting.

AB - BACKGROUND: The WAP-T mouse model is an established clinically relevant model of breast cancer. Lectins have been used to study malignant progression in clinical studies. We investigated lectin binding sites to test for the clinical relevance of this model.MATERIALS AND METHODS: Samples of the WAP-T mouse mammary tissues, from normal tissues to undifferentiated higher tumor grades were stained using an indirect technique with nine different lectins for intensity of lectin binding.RESULTS: HPA bound to the luminal epithelium in higher tumor grades in a similar pattern to that in human breast cancer. BSA-IB4 bound to luminal epithelium in hyperplasia and increased towards higher grades, comparable to previous clinical studies. PHA-L-binding to myoepithelium and luminal epithelium increased from hyperplasia to higher grades, comparable to findings in human breast cancer.CONCLUSION: The results of our study support the hypothesis that lectin binding sites change similarly in WAP-T and human breast cancer, stressing the similarity of this model with the clinical setting.

M3 - SCORING: Journal article

C2 - 25503131

VL - 34

SP - 7045

EP - 7053

JO - ANTICANCER RES

JF - ANTICANCER RES

SN - 0250-7005

IS - 12

ER -