Cellular UDP-Glucose Deficiency Caused by a Single Point Mutation in the UDP-Glucose Pyrophosphorylase Gene

Flores-Dı́az, Marietta; Alape-Girón, Alberto; Persson, Bengt; Pollesello, Piero; Moos, Michael; Eichel‐Streiber, Christoph von; Thelestam, Mónica; Florin, Inger

doi:10.1074/jbc.272.38.23784

Cited by 80 publications

(90 citation statements)

References 70 publications

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“…The UDP-Glcdeficient mutant cell, referred to here as Don Q, and the spontaneous revertant, referred to here as Don QR, and the transfectant clones QC, B9, and G3 were previously isolated (23,26). Chemicals were from Sigma unless otherwise stated.…”

Section: Materials-thementioning

confidence: 99%

“…Cell lysates (30 g of protein/lane) were subjected to electrophoresis under reducing conditions on a 10% (w/v) SDS-polyacrylamide gel, electroblotted onto 0.45-m nitrocellulose membranes, and subjected to Western blot analyses as described (23). Immunoreactive bands were detected and quantified with a densitometer using ImageQuant (Amersham Biosciences).…”

Section: Materials-thementioning

confidence: 99%

“…From Don Q we isolated a spontaneous revertant cell, Don QR, in which the mutation was reverted in one allele, partially compensating for the UDP-Glc deficiency (23). These cells provide a unique opportunity to investigate how mammalian cells are affected by fluctuations in the cellular UDP-Glc content.…”

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confidence: 99%

“…Furthermore, it is required in the quality control of newly synthesized glycoproteins within the ER (23). A low level of UDP-Glc occurs in mammalian cells exposed to hypoxia or glucose starvation (for references see Ref.…”

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confidence: 99%

“…We previously isolated a Chinese hamster mutant cell line, Don Q, having a permanent low level of UDP-Glc because of a recessive point mutation affecting the UDP-Glc pyrophosphorylase gene (UDPG:PP) (23). From Don Q we isolated a spontaneous revertant cell, Don QR, in which the mutation was reverted in one allele, partially compensating for the UDP-Glc deficiency (23).…”

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A Cellular UDP-glucose Deficiency Causes Overexpression of Glucose/Oxygen-regulated Proteins Independent of the Endoplasmic Reticulum Stress Elements

Flores-Dı́az

Higuita

Florin

et al. 2004

Journal of Biological Chemistry

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A low level of UDP-Glc occurs in cells exposed to hypoxia or glucose starvation. This work reveals that a 65% reduction in the cellular UDP-Glc level causes upregulation of the mitochondrial chaperone GRP75 and the endoplasmic reticulum (ER) resident chaperones GRP58, ERp72, GRP78, GRP94, GRP170, and calreticulin. Conditions that cause misfolding of proteins within the ER activate the transcription factors ATF6␣/␤ and induce translation of the transcription factors XBP-1/ TREB5 and ATF4/CREB2. These transcription factors induce the overexpression of ER chaperones and CHOP/ GADD153. However, the 65% decrease in the cellular UDP-Glc level does not cause activation of ATF6␣, splicing of XBP-1/TREB5, induction of ATF4/CREB2, or expression of CHOP/GADD153. The activity of the promoters of the ER chaperones is increased in UDP-Glcdeficient cells, but the activity of the CHOP/GADD153 promoter is not affected, in comparison with their respective activities in cells having compensated for the UDP-Glc deficiency. The results demonstrate that the unfolded protein response remains functionally intact in cells with a 65% decrease in the cellular UDP-Glc level and provide evidence that this decrease is a stress signal in mammalian cells, which triggers the coordinate overexpression of mitochondrial and ER chaperones, independently of the ER stress elements.

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Section: Materials-thementioning

confidence: 99%

Section: Materials-thementioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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A Cellular UDP-glucose Deficiency Causes Overexpression of Glucose/Oxygen-regulated Proteins Independent of the Endoplasmic Reticulum Stress Elements

Flores-Dı́az

Higuita

Florin

et al. 2004

Journal of Biological Chemistry

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Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase

et al. 2021

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Bacterial phospholipases and sphingomyelinases are lipolytic esterases that are structurally and evolutionarily heterogeneous. These enzymes play crucial roles as virulence factors in several human and animal infectious diseases. Some bacterial phospholipases C (PLCs) have both phosphatidylcholinesterase and sphingomyelinase C activities. Among them, Listeria monocytogenes PlcB, Clostridium perfringens PLC, and Pseudomonas aeruginosa PlcH are the most deeply understood. In silico predictions of substrates docking with these three bacterial enzymes provide evidence that they interact with different substrates at the same active site. This review discusses structural aspects, substrate specificity, and the mechanism of action of those bacterial enzymes on target cells and animal infection models to shed light on their roles in pathogenesis.

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Banana (Musa spp.) as a model to study the meristem proteome: Acclimation to osmotic stress

Carpentier¹,

Witters²,

Laukens³

et al. 2007

Proteomics

112

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Banana (Musa spp.) multiple shoot meristems are an excellent model to study the meristem proteome. Using a 2-DE protocol developed for small amounts of tissue and MS-based cross species polypeptide identification, we have revealed the meristem proteome and investigated the influence of sucrose-mediated osmotic stress in a dehydration-tolerant variety. Proteins that were significantly up- or down-regulated due to the high-sucrose treatment were classified using non-parametric univariate statistics. Our results suggest that the maintenance of an osmoprotective intracellular sucrose concentration, the enhanced expression of particular genes of the energy-conserving glycolysis and the conservation of the cell wall integrity are essential to maintain homeostasis, to acclimate and to survive dehydration. By comparing the dehydration-tolerant variety with a dehydration-sensitive variety, we were able to distinguish several genotype-specific proteins (isoforms), and could associate the dehydration-tolerant variety with proteins involved in energy metabolism (e.g., phosphoglycerate kinase, phosphoglucomutase, UDP-glucose pyrophosphorylase) and proteins that are associated with stress adaptation (e.g., OSR40-like protein, abscisic stress ripening protein-like protein). This work shows that proteome analysis can be used successfully to perform quantitative difference analysis and to characterize genetic variations in a recalcitrant crop.

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Cellular UDP-Glucose Deficiency Caused by a Single Point Mutation in the UDP-Glucose Pyrophosphorylase Gene

Cited by 80 publications

References 70 publications

A Cellular UDP-glucose Deficiency Causes Overexpression of Glucose/Oxygen-regulated Proteins Independent of the Endoplasmic Reticulum Stress Elements

A Cellular UDP-glucose Deficiency Causes Overexpression of Glucose/Oxygen-regulated Proteins Independent of the Endoplasmic Reticulum Stress Elements

Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase

Banana (Musa spp.) as a model to study the meristem proteome: Acclimation to osmotic stress

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