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Relevance of βGal-βGalNAc-containing glycans and the enzymes involved in their synthesis for invasion and survival in breast cancer patients

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Relevance of βGal-βGalNAc-containing glycans and the enzymes involved in their synthesis for invasion and survival in breast cancer patients. / Milde-Langosch, Karin; Schütze, Dina; Oliveira-Ferrer, Leticia; Wikman-Kocher, Harriet; Müller, Volkmar; Lebok, Patrick; Pantel, Klaus; Schröder, Christine; Witzel, Isabell; Schumacher, Udo.

In: BREAST CANCER RES TR, Vol. 151, No. 3, 06.2015, p. 515-28.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Milde-Langosch, K, Schütze, D, Oliveira-Ferrer, L, Wikman-Kocher, H, Müller, V, Lebok, P, Pantel, K, Schröder, C, Witzel, I & Schumacher, U 2015, 'Relevance of βGal-βGalNAc-containing glycans and the enzymes involved in their synthesis for invasion and survival in breast cancer patients', BREAST CANCER RES TR, vol. 151, no. 3, pp. 515-28. https://doi.org/10.1007/s10549-015-3425-0

APA

Milde-Langosch, K., Schütze, D., Oliveira-Ferrer, L., Wikman-Kocher, H., Müller, V., Lebok, P., Pantel, K., Schröder, C., Witzel, I., & Schumacher, U. (2015). Relevance of βGal-βGalNAc-containing glycans and the enzymes involved in their synthesis for invasion and survival in breast cancer patients. BREAST CANCER RES TR, 151(3), 515-28. https://doi.org/10.1007/s10549-015-3425-0

Vancouver

Milde-Langosch K, Schütze D, Oliveira-Ferrer L, Wikman-Kocher H, Müller V, Lebok P et al. Relevance of βGal-βGalNAc-containing glycans and the enzymes involved in their synthesis for invasion and survival in breast cancer patients. BREAST CANCER RES TR. 2015 Jun;151(3):515-28. https://doi.org/10.1007/s10549-015-3425-0

Bibtex

@article{a54a8f792f06439b9f635969ae8ec6ff,
title = "Relevance of βGal-βGalNAc-containing glycans and the enzymes involved in their synthesis for invasion and survival in breast cancer patients",
abstract = "To study the influence of glycosylation on breast cancer progression by analyses on glycan, mRNA, and protein level. For detection of glycan structures, we performed lectin histochemistry with five lectins of different specificity (UEA-1, HPA, GNA, PNA, and PHA-L) on a tissue microarray with >400 breast cancer samples. For comparison, mRNA expression of glycosylation enzymes involved in the synthesis of HPA and PNA binding glycostructures (GALNT family members and C1GALT1) was analyzed in microarray data of 194 carcinomas. Additionally, C1GALT1 protein expression was analyzed by Western blot analysis in 106 tumors. Correlations with clinical and histological parameters including recurrence-free (RFS) and overall survival (OAS) were calculated. Positive binding of four lectins (HPA, GNA, PNA, and PHA-L) correlated significantly with parameters involved in tumor metastasis, namely lymphangiosis, vascular invasion, lymph node involvement, and presence of disseminated tumor cells in bone marrow. HPA and PNA binding also showed a negative prognostic impact in our cohort. Correspondingly, high expression of C1GALT1, GALNT1, GALNT8, or GALNT14 mRNA and C1GALT1 protein correlated significantly with shorter OAS. Notably, combined overexpression of C1GALT1/GALNT1 or C1GALT1/GALNT8 mRNA was associated with a significantly reduced OAS (HR 3.15 and 2.73) and RFS (HR 2.01 and 1.94), pointing to an additive influence of these enzymes. This prognostic impact retained significance in multivariate analysis including classical prognostic markers. Our data indicate that glycan structures containing βGal-βGalNAc residues and the enzymes involved in their synthesis play a role in breast cancer progression, at least partly by their promoting influence on haematogenic and lymphatic spread.",
author = "Karin Milde-Langosch and Dina Sch{\"u}tze and Leticia Oliveira-Ferrer and Harriet Wikman-Kocher and Volkmar M{\"u}ller and Patrick Lebok and Klaus Pantel and Christine Schr{\"o}der and Isabell Witzel and Udo Schumacher",
year = "2015",
month = jun,
doi = "10.1007/s10549-015-3425-0",
language = "English",
volume = "151",
pages = "515--28",
journal = "BREAST CANCER RES TR",
issn = "0167-6806",
publisher = "Springer New York",
number = "3",

}

RIS

TY - JOUR

T1 - Relevance of βGal-βGalNAc-containing glycans and the enzymes involved in their synthesis for invasion and survival in breast cancer patients

AU - Milde-Langosch, Karin

AU - Schütze, Dina

AU - Oliveira-Ferrer, Leticia

AU - Wikman-Kocher, Harriet

AU - Müller, Volkmar

AU - Lebok, Patrick

AU - Pantel, Klaus

AU - Schröder, Christine

AU - Witzel, Isabell

AU - Schumacher, Udo

PY - 2015/6

Y1 - 2015/6

N2 - To study the influence of glycosylation on breast cancer progression by analyses on glycan, mRNA, and protein level. For detection of glycan structures, we performed lectin histochemistry with five lectins of different specificity (UEA-1, HPA, GNA, PNA, and PHA-L) on a tissue microarray with >400 breast cancer samples. For comparison, mRNA expression of glycosylation enzymes involved in the synthesis of HPA and PNA binding glycostructures (GALNT family members and C1GALT1) was analyzed in microarray data of 194 carcinomas. Additionally, C1GALT1 protein expression was analyzed by Western blot analysis in 106 tumors. Correlations with clinical and histological parameters including recurrence-free (RFS) and overall survival (OAS) were calculated. Positive binding of four lectins (HPA, GNA, PNA, and PHA-L) correlated significantly with parameters involved in tumor metastasis, namely lymphangiosis, vascular invasion, lymph node involvement, and presence of disseminated tumor cells in bone marrow. HPA and PNA binding also showed a negative prognostic impact in our cohort. Correspondingly, high expression of C1GALT1, GALNT1, GALNT8, or GALNT14 mRNA and C1GALT1 protein correlated significantly with shorter OAS. Notably, combined overexpression of C1GALT1/GALNT1 or C1GALT1/GALNT8 mRNA was associated with a significantly reduced OAS (HR 3.15 and 2.73) and RFS (HR 2.01 and 1.94), pointing to an additive influence of these enzymes. This prognostic impact retained significance in multivariate analysis including classical prognostic markers. Our data indicate that glycan structures containing βGal-βGalNAc residues and the enzymes involved in their synthesis play a role in breast cancer progression, at least partly by their promoting influence on haematogenic and lymphatic spread.

AB - To study the influence of glycosylation on breast cancer progression by analyses on glycan, mRNA, and protein level. For detection of glycan structures, we performed lectin histochemistry with five lectins of different specificity (UEA-1, HPA, GNA, PNA, and PHA-L) on a tissue microarray with >400 breast cancer samples. For comparison, mRNA expression of glycosylation enzymes involved in the synthesis of HPA and PNA binding glycostructures (GALNT family members and C1GALT1) was analyzed in microarray data of 194 carcinomas. Additionally, C1GALT1 protein expression was analyzed by Western blot analysis in 106 tumors. Correlations with clinical and histological parameters including recurrence-free (RFS) and overall survival (OAS) were calculated. Positive binding of four lectins (HPA, GNA, PNA, and PHA-L) correlated significantly with parameters involved in tumor metastasis, namely lymphangiosis, vascular invasion, lymph node involvement, and presence of disseminated tumor cells in bone marrow. HPA and PNA binding also showed a negative prognostic impact in our cohort. Correspondingly, high expression of C1GALT1, GALNT1, GALNT8, or GALNT14 mRNA and C1GALT1 protein correlated significantly with shorter OAS. Notably, combined overexpression of C1GALT1/GALNT1 or C1GALT1/GALNT8 mRNA was associated with a significantly reduced OAS (HR 3.15 and 2.73) and RFS (HR 2.01 and 1.94), pointing to an additive influence of these enzymes. This prognostic impact retained significance in multivariate analysis including classical prognostic markers. Our data indicate that glycan structures containing βGal-βGalNAc residues and the enzymes involved in their synthesis play a role in breast cancer progression, at least partly by their promoting influence on haematogenic and lymphatic spread.

U2 - 10.1007/s10549-015-3425-0

DO - 10.1007/s10549-015-3425-0

M3 - SCORING: Journal article

C2 - 25975956

VL - 151

SP - 515

EP - 528

JO - BREAST CANCER RES TR

JF - BREAST CANCER RES TR

SN - 0167-6806

IS - 3

ER -