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Lee, M, Park, JJ, Ko, YG and Lee, YS (2012) Cleavage of ST6Gal I by radiation-induced BACE1 inhibits golgi-anchored ST6Gal I-mediated sialylation of integrin β1 and migration in colon cancer cells. Radiat Oncol 7:47
Previously, we found that β-galactoside α2,6-sialyltransferase (ST6Gal I), an enzyme that adds sialic acids to N-linked oligosaccharides of glycoproteins and is frequently overexpressed in cancer cells, is up-regulated by ionizing radiation (IR) and cleaved to a form possessing catalytic activity comparable to that of the Golgi-localized enzyme. Moreover, this soluble form is secreted into the culture media. Induction of ST6Gal I significantly increased the migration of colon cancer cells via sialylation of integrin β1. Here, we further investigated the mechanisms underlying ST6Gal I cleavage, solubilization and release from cells, and addressed its functions, focusing primarily on cancer cell migration.
Amyloid Precursor Protein Secretases/metabolism; Antigens, CD29/metabolism; Aspartic Acid Endopeptidases/metabolism; Cell Line, Tumor; Cell Movement/radiation effects; Colonic Neoplasms/metabolism; Enzyme-Linked Immunosorbent Assay; Flow Cytometry; Golgi Apparatus/metabolism; Humans; Immunoblotting; Immunoprecipitation; N-Acetylneuraminic Acid/metabolism; Radiation, Ionizing; Sialyltransferases/metabolism
|Gene product||Qualifier||GO Term||Evidence Code||with/from||Aspect||Extension||Notes||Status|
|GO:0008233: peptidase activity||
Figure 1 shows that the activity of BACE-1 is actively involved in the cleave of ST6Gal I from the Golgi membrane inducing secretion. Mutants without BACE-1 activity could not induce the cleavage of ST6Gal I and no secretion occurred.
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