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Cellular glycosylation affects Herceptin binding and sensitivity of breast cancer cells to doxorubicin and growth factors.


ABSTRACT: Alterations in protein glycosylation are a key feature of oncogenesis and have been shown to affect cancer cell behaviour perturbing cell adhesion, favouring cell migration and metastasis. This study investigated the effect of N-linked glycosylation on the binding of Herceptin to HER2 protein in breast cancer and on the sensitivity of cancer cells to the chemotherapeutic agent doxorubicin (DXR) and growth factors (EGF and IGF-1). The interaction between Herceptin and recombinant HER2 protein and cancer cell surfaces (on-rate/off-rate) was assessed using a quartz crystal microbalance biosensor revealing an increase in the accessibility of HER2 to Herceptin following deglycosylation of cell membrane proteins (deglycosylated cells Bmax: 6.83?Hz; glycosylated cells Bmax: 7.35?Hz). The sensitivity of cells to DXR and to growth factors was evaluated using an MTT assay. Maintenance of SKBR-3 cells in tunicamycin (an inhibitor of N-linked glycosylation) resulted in an increase in sensitivity to DXR (0.1??M DXR P?

SUBMITTER: Peiris D 

PROVIDER: S-EPMC5320443 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

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Cellular glycosylation affects Herceptin binding and sensitivity of breast cancer cells to doxorubicin and growth factors.

Peiris Diluka D   Spector Alexander F AF   Lomax-Browne Hannah H   Azimi Tayebeh T   Ramesh Bala B   Loizidou Marilena M   Welch Hazel H   Dwek Miriam V MV  

Scientific reports 20170222


Alterations in protein glycosylation are a key feature of oncogenesis and have been shown to affect cancer cell behaviour perturbing cell adhesion, favouring cell migration and metastasis. This study investigated the effect of N-linked glycosylation on the binding of Herceptin to HER2 protein in breast cancer and on the sensitivity of cancer cells to the chemotherapeutic agent doxorubicin (DXR) and growth factors (EGF and IGF-1). The interaction between Herceptin and recombinant HER2 protein and  ...[more]

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