1984
DOI: 10.1016/0092-8674(84)90007-2
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Translocation across golgi vesicle membranes: A CHO glycosylation mutant deficient in CMP-sialic acid transport

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Cited by 258 publications
(178 citation statements)
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“…The biochemical characterisation (Deutscher et al, 1984) strongly suggested that the gene defective in these cells encodes the Golgi CMP-Sia-Tr. Recently, we were able to confirm this hypothesis by cloning the gene defective in Lec2 cells .…”
Section: Discussionmentioning
confidence: 99%
“…The biochemical characterisation (Deutscher et al, 1984) strongly suggested that the gene defective in these cells encodes the Golgi CMP-Sia-Tr. Recently, we were able to confirm this hypothesis by cloning the gene defective in Lec2 cells .…”
Section: Discussionmentioning
confidence: 99%
“…The stained cells were subjected to FACS analysis as described above. CHO mutant Lec2 cells lack a functional Golgi CMP-sialic acid transporter; and therefore, sialylation is absent in Lec2 cells (34). The absence of sialylation facilitates core 1 extension because core 1 extension and sialylation compete with each other for the same acceptor, Gal␤133GalNAc␣13 R.…”
Section: Expression Of I Antigen In Hela Cells By Different ␤3glcnactmentioning
confidence: 99%
“…To further validate our system, we acquired the comparative lectin binding profiles of two additional Lec mutants: Lec1, which is deficient in GlcNAcT1, the enzyme necessary for hybrid and complex N-linked glycans; and Lec2, a mutant lacking CMP-sialic acid transport (24,25). Biological replicates of Lec1 clustered very tightly (R ϭ 0.98, n ϭ 9, P Ͻ 0.001) and displayed a marked increase in exposed mannose residues when compared with Pro-5 as reflected by differences in ConA and GNA binding (Fig.…”
Section: Hierarchical Clustering Of Lec Mutants Reveals Subtle Differmentioning
confidence: 99%