Sialylation by β‑galactoside α‑2,6‑sialyltransferase and N‑glycans regulate cell adhesion and invasion in human anaplastic large cell lymphoma.

Sialylation by β‑galactoside α‑2,6‑sialyltransferase and N‑glycans regulate cell adhesion and invasion in human anaplastic large cell lymphoma. Int J Oncol. 2015 Jan 7; Authors: Suzuki O, Abe M, Hashimoto Y Abstract The interaction between cell surface glycans and extracellular matrix (ECM) including galectins is known to be closely associated with tumor cell adhesion, invasion and metastasis. We analyzed the roles of cell surface sialylation or glycosylation in galectin or ECM‑mediated cell adhesion and invasion of human malignant lymphoma cells. Neuraminidase from Arthrobacter ureafaciens (AU) treatment resulted in reduction of cell adhesion to galectin‑8 in human anaplastic large cell lymphoma (H‑ALCL) which was established in our laboratory. The knockdown of β‑galactoside α‑2,6‑sialyltrans-ferase (ST6Gal1) by siRNA showed inhibition of ST6Gal1 expression in the cytoplasm of H‑ALCL cells on immunohistochemical findings, and showed dramatic enhancement of cell adhesion to galectin‑8. On the other hand, α‑2,3‑specific neuraminidase treatment resulted in moderate enhancement of cell adhesion to galectin‑8. We performed chemically artificial modification of cell surface O‑glycans by treatment of benzyl 2‑acetamido‑2‑deoxy‑α‑D‑galactopyranoside (Bz‑α‑GalNAc) in H‑ALCL. Cell adhesion to galectin‑8 was enhanced by treatment of Bz‑α‑GalNAc suggesting that inhibition of e...
Source: International Journal of Oncology - Category: Cancer & Oncology Authors: Tags: Int J Oncol Source Type: research