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• W2082325881 abstract "Polysialic acid (PSA) is a linear homopolymer of α-2,8-linked sialic acid residues whose expression is developmentally regulated and modulates the adhesive property of the neural adhesion molecule, N-CAM. Recently, hamster and human cDNAs encoding polysialyltransferase (PST-1 for the hamster enzyme and PST for the human enzyme) were cloned, and by using the human cDNA it was demonstrated that the expression of PSA in N-CAM facilitates neurite outgrowth (Nakayama, J., Fukuda, M.N., Fredette, B., Ranscht, B., and Fukuda, M.(1995) Proc. Natl. Acad. Sci. U. S. A., 92, 7031-7035; Eckhardt, M.A., Mühlenhoff, M., Bethe, A., Koopman, J., Frosch, M., and Gerardy-Schahn, R.(1995) Nature 373, 715-718.) Although these studies demonstrated that PST-1 and PST synthesize PSA in cultured cells, it was not shown that they could catalyze the polycondensation of α-2,8-linked sialic acid on a glycoconjugate template containing α-2,3-linked sialic acid. Here we demonstrate that PSA formation by PST is independent from the presence of N-CAM in vivo. We then develop an in vitro assay of PSA synthesis using glycoproteins other than N-CAM as acceptors and a soluble PST as an enzyme source. The soluble PST, produced as a chimeric protein fused with protein A, was incubated with rat α1-acid glycoprotein, fetuin or human α1-acid glycoprotein as acceptors together with the donor substrate CMP-[14C]NeuNAc. Incubation of fetuin with the soluble PST, in particular, resulted in a high molecular weight product that was susceptible to PSA-specific endoneuraminidase. Polysialylated products were not formed when α-2,3-linked sialic acid was removed from the acceptor fetuin before incubation. These results establish that a single enzyme, PST, alone can catalyze both the addition of the first α-2,8-linked sialic acid to α-2,3-linked sialic acid and the polycondensation of all α-2,8-linked sialic acids, yielding PSA. Polysialic acid (PSA) is a linear homopolymer of α-2,8-linked sialic acid residues whose expression is developmentally regulated and modulates the adhesive property of the neural adhesion molecule, N-CAM. Recently, hamster and human cDNAs encoding polysialyltransferase (PST-1 for the hamster enzyme and PST for the human enzyme) were cloned, and by using the human cDNA it was demonstrated that the expression of PSA in N-CAM facilitates neurite outgrowth (Nakayama, J., Fukuda, M.N., Fredette, B., Ranscht, B., and Fukuda, M.(1995) Proc. Natl. Acad. Sci. U. S. A., 92, 7031-7035; Eckhardt, M.A., Mühlenhoff, M., Bethe, A., Koopman, J., Frosch, M., and Gerardy-Schahn, R.(1995) Nature 373, 715-718.) Although these studies demonstrated that PST-1 and PST synthesize PSA in cultured cells, it was not shown that they could catalyze the polycondensation of α-2,8-linked sialic acid on a glycoconjugate template containing α-2,3-linked sialic acid. Here we demonstrate that PSA formation by PST is independent from the presence of N-CAM in vivo. We then develop an in vitro assay of PSA synthesis using glycoproteins other than N-CAM as acceptors and a soluble PST as an enzyme source. The soluble PST, produced as a chimeric protein fused with protein A, was incubated with rat α1-acid glycoprotein, fetuin or human α1-acid glycoprotein as acceptors together with the donor substrate CMP-[14C]NeuNAc. Incubation of fetuin with the soluble PST, in particular, resulted in a high molecular weight product that was susceptible to PSA-specific endoneuraminidase. Polysialylated products were not formed when α-2,3-linked sialic acid was removed from the acceptor fetuin before incubation. These results establish that a single enzyme, PST, alone can catalyze both the addition of the first α-2,8-linked sialic acid to α-2,3-linked sialic acid and the polycondensation of all α-2,8-linked sialic acids, yielding PSA." @default.
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• W2082325881 date "1996-01-01" @default.
• W2082325881 modified "2023-10-16" @default.
• W2082325881 title "A Human Polysialyltransferase Directs in Vitro Synthesis of Polysialic Acid" @default.
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• W2082325881 doi "https://doi.org/10.1074/jbc.271.4.1829" @default.
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