Translocation across golgi vesicle membranes: A CHO glycosylation mutant deficient in CMP-sialic acid transport

Susan L. Deutscher, Naziha Nuwayhid, Pamela Stanley, Eve Ida Barak Briles, Carlos B. Hirschberg

Research output: Contribution to journalArticle

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Abstract

Golgi vesicle membranes from the Lec2 CHO glycosylation mutant translocate CMP-sialic acid at only 2% the rate of vesicles from wild-type CHO cells. The deficiency is specific, because vesicles from Lec2 cells can translocate UDP-N-acetylglucosamine, adenosine 3′-phosphate 5′-phosphosulfate, and UDP-galactose at rates comparable to those of vesicles from wild-type cells. Complementation analyses show that Lec2 mutants belong to the same genetic complementation group as clone 1021, a CHO mutant of similar phenotype. Both mutants have previously been shown to have a 90% reduction in the sialylation of glycoproteins and gangliosides compared with wild-type cells. However, 1021 cells appear to have normal levels of CMP-sialic acid, sialyltransferase activity, and endogenous acceptors for sialylation. It seems likely that the primary defect in Lec2 and 1021 cells is their inability to translocate CMP-sialic acid across Golgi vesicle membranes.

Original languageEnglish (US)
Pages (from-to)295-299
Number of pages5
JournalCell
Volume39
Issue number2 PART 1
DOIs
StatePublished - 1984

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Cytidine Monophosphate N-Acetylneuraminic Acid
Glycosylation
Membranes
Phosphoadenosine Phosphosulfate
Uridine Diphosphate Galactose
Sialyltransferases
Uridine Diphosphate
Acetylglucosamine
Gangliosides
Uridine Diphosphate N-Acetylglucosamine
Glycoproteins
CHO Cells
Defects
Clone Cells
Phenotype

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

Translocation across golgi vesicle membranes : A CHO glycosylation mutant deficient in CMP-sialic acid transport. / Deutscher, Susan L.; Nuwayhid, Naziha; Stanley, Pamela; Briles, Eve Ida Barak; Hirschberg, Carlos B.

In: Cell, Vol. 39, No. 2 PART 1, 1984, p. 295-299.

Research output: Contribution to journalArticle

Deutscher, Susan L. ; Nuwayhid, Naziha ; Stanley, Pamela ; Briles, Eve Ida Barak ; Hirschberg, Carlos B. / Translocation across golgi vesicle membranes : A CHO glycosylation mutant deficient in CMP-sialic acid transport. In: Cell. 1984 ; Vol. 39, No. 2 PART 1. pp. 295-299.
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abstract = "Golgi vesicle membranes from the Lec2 CHO glycosylation mutant translocate CMP-sialic acid at only 2{\%} the rate of vesicles from wild-type CHO cells. The deficiency is specific, because vesicles from Lec2 cells can translocate UDP-N-acetylglucosamine, adenosine 3′-phosphate 5′-phosphosulfate, and UDP-galactose at rates comparable to those of vesicles from wild-type cells. Complementation analyses show that Lec2 mutants belong to the same genetic complementation group as clone 1021, a CHO mutant of similar phenotype. Both mutants have previously been shown to have a 90{\%} reduction in the sialylation of glycoproteins and gangliosides compared with wild-type cells. However, 1021 cells appear to have normal levels of CMP-sialic acid, sialyltransferase activity, and endogenous acceptors for sialylation. It seems likely that the primary defect in Lec2 and 1021 cells is their inability to translocate CMP-sialic acid across Golgi vesicle membranes.",
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AU - Hirschberg, Carlos B.

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AB - Golgi vesicle membranes from the Lec2 CHO glycosylation mutant translocate CMP-sialic acid at only 2% the rate of vesicles from wild-type CHO cells. The deficiency is specific, because vesicles from Lec2 cells can translocate UDP-N-acetylglucosamine, adenosine 3′-phosphate 5′-phosphosulfate, and UDP-galactose at rates comparable to those of vesicles from wild-type cells. Complementation analyses show that Lec2 mutants belong to the same genetic complementation group as clone 1021, a CHO mutant of similar phenotype. Both mutants have previously been shown to have a 90% reduction in the sialylation of glycoproteins and gangliosides compared with wild-type cells. However, 1021 cells appear to have normal levels of CMP-sialic acid, sialyltransferase activity, and endogenous acceptors for sialylation. It seems likely that the primary defect in Lec2 and 1021 cells is their inability to translocate CMP-sialic acid across Golgi vesicle membranes.

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