Two cell lines, derived from human T-cell acute leukemia, one glucocorticoid sensitive (CEM-C7) and the other glucocorticoid resistant (CEM-C1) were grown in the presence of 1 x 10-7 M dexamethasone and were analyzed for their dolichol content. After 24 hrs of incubation, dolichols became significantly elevated in the sensitive but not in the resistant line. Lovastatin, the specific inhibitor of cholesterol synthesis did not affect dolichol levels in either of the two cell lines. The results raise the possibility that dolichol accumulation might be involved in the early stages of the glucocorticoid-induced apoptosis (directed cell killing).
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Absence of the dolichol synthesis gene DHRSX leads to N-glycosylation defects in Lec5 and Lec9 Chinese hamster ovary cells.
J Biol Chem
December 2024
Laboratory for Molecular Diagnosis, Center for Human Genetics, KU Leuven, Leuven, Belgium. Electronic address:
Article Synopsis
- - Glycosylation-deficient CHO cell lines, specifically Lec5 and Lec9, have been key to understanding N-glycosylation, but the reasons behind their glycosylation defects remained unclear until now.
- - Dolichol synthesis from polyprenol was found to occur in three steps involving the enzymes DHRSX and SRD5A3, with Lec5 and Lec9 cells showing increased levels of polyprenol and decreased dolichol, indicating a deficiency in DHRSX.
- - Long-read genome sequencing revealed that the DHRSX gene was missing in Lec5 and Lec9 cells, while the SRD5A3 gene was intact, confirming that the glycosylation defects
Molecular characterization of Rft1, an ER membrane protein associated with congenital disorder of glycosylation RFT1-CDG.
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The oligosaccharide needed for protein N-glycosylation is assembled on a lipid carrier via a multistep pathway. Synthesis is initiated on the cytoplasmic face of the endoplasmic reticulum (ER) and completed on the luminal side after transbilayer translocation of a heptasaccharide lipid intermediate. More than 30 congenital disorders of glycosylation (CDGs) are associated with this pathway, including RFT1-CDG which results from defects in the membrane protein Rft1.
View Article and Find Full Text PDFMetabolic modulation: phosphoglucomutase is a target influencing host recognition.
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View Article and Find Full Text PDFThe N-glycosylation defect in Lec5 and Lec9 CHO cells is caused by absence of the DHRSX gene.
bioRxiv
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Laboratory for Molecular Diagnosis, Center for Human Genetics, KU Leuven, Leuven 3000, Belgium.
Glycosylation-deficient Chinese hamster ovary (CHO) cell lines have been instrumental in the discovery of N-glycosylation machinery. Yet, the molecular causes of the glycosylation defects in the Lec5 and Lec9 mutants have been elusive, even though for both cell lines a defect in dolichol formation from polyprenol was previously established. We recently found that dolichol synthesis from polyprenol occurs in three steps consisting of the conversion of polyprenol to polyprenal by DHRSX, the reduction of polyprenal to dolichal by SRD5A3 and the reduction of dolichal to dolichol, again by DHRSX.
View Article and Find Full Text PDFMolecular characterization of Rft1, an ER membrane protein associated with congenital disorder of glycosylation RFT1-CDG.
bioRxiv
June 2024
Department of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
The oligosaccharide needed for protein -glycosylation is assembled on a lipid carrier via a multi-step pathway. Synthesis is initiated on the cytoplasmic face of the endoplasmic reticulum (ER) and completed on the luminal side after transbilayer translocation of a heptasaccharide lipid intermediate. More than 30 Congenital Disorders of Glycosylation (CDGs) are associated with this pathway, including RFT1-CDG which results from defects in the membrane protein Rft1.
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