Implication of GnT-V in cancer metastasis: a glycomic approach for identification of a target protein and its unique function as an angiogenic cofactor.

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It is known that sugar chains have a variety of functions and play a key role in development, differentiation, cell adhesion and cell growth in cells [1,2]. Our group has focused on the underlying mechanism of the biosynthesis of N -glycan branchings in glycoproteins, and reported on various N -glycan branching enzymes that play a pivotal role in various steps [3]. A possible link between β1-6 branched structures of N glycans and cancer metastasis has been proposed by several authors [4–6]. However before the cloning of the UDP-GlcNAc α-mannoside β1-6-N -acetylglucosaminyltransferase (GnT-V) enzyme which catalyzes the formation of β1-6 branching was carried out, it was not clear whether or not β1-6 branching is actually related to the metastatic potential of cancer cells. The enzyme was independently purified from rat kidney [7] by Pierce’s group and from human cancer cells [8] by our group, and both groups subsequently cloned their cDNAs [9,10]. Using the cloned genes several studies have presented evidence for the presence of strong association between β1-6 branching and cancer metastasis [11–13]. Knock out mice developed by Dennis’s group confirmed that the gene is highly linked to cancer development [14]. However, in the case of glycosyl-

Journal

  • Glycoconjugate Journal

    Glycoconjugate Journal 18 (11/12), 859-865, 2001

    Springer Science and Business Media LLC

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