Glycol-Cleavage Oxidation

Perlin, Arthur S.

doi:10.1016/s0065-2318(06)60005-x

Cited by 86 publications

(73 citation statements)

References 381 publications

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“…1C). To investigate this further, we adducted RCs to a second model Ag, the glycoprotein OVA, by aldehyde treatment (2 or 20 mM FA or GA) or by NaIO 4 oxidation of the glycan (16,27,29). After adjuvantfree immunization of BALB/c mice, OVA-specific total IgG responses, pooled irrespective of the method of modification, correlated robustly with the moles of adducted RCs on OVA (r = 0.71, p = 0.036; Fig.…”

Section: Rc Adduction To Proteins By Common Aldehyde By-products Of Omentioning

confidence: 96%

Reactive Carbonyls Are a Major Th2-Inducing Damage-Associated Molecular Pattern Generated by Oxidative Stress

Moghaddam

Gartlan

Kong

et al. 2011

The Journal of Immunology

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Oxidative stress is widespread and entwined with pathological processes, yet its linkage to adaptive immunity remains elusive. Reactive carbonyl (RC) adduction, a common feature of oxidative stress, has been shown to target proteins to the adaptive immune system. Because aldehydes are important mediators of carbonylation, we explored the immunomodulatory properties of model Ags modified by common bioactive aldehyde by-products of oxidative stress: 4-hydroxy-2-nonenal, malondialdehyde, and glycolaldehyde. Ag modification with all three aldehydes resulted in Ag-specific IgG1-dominated responses in adjuvant-free murine immunizations in an RC-dependent manner. The central role of RCs was confirmed, as their reduction into nonreactive groups abrogated all adaptive responses, despite the presence of other well-known aldehyde-driven adducts such as Nε-carboxymethyllysine and glycolaldehyde–pyridine. Moreover, Ag-specific Ab responses robustly correlated with the extent of RC adduction, regardless of the means of their generation. T cell responses mirrored the Th2-biased Ab isotypes by Ag-specific splenocyte production of IL-4, IL-5, and IL-13, but not IFN-γ. The RC-induced Th2 response was in sharp contrast to that induced by Th1/Th2 balanced or Th1-biasing adjuvants and was maintained in a range of mouse strains. In vitro studies revealed that RC adduction enhanced Ag presentation with Th2 polarization in the absence of conventional dendritic cell activation. Taken together, these data implicate commonly occurring RC as an important oxidation-derived Th2 immunomodulatory damage-associated molecular pattern with potentially important roles in health and disease.

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Section: Rc Adduction To Proteins By Common Aldehyde By-products Of Omentioning

confidence: 96%

Reactive Carbonyls Are a Major Th2-Inducing Damage-Associated Molecular Pattern Generated by Oxidative Stress

Moghaddam

Gartlan

Kong

et al. 2011

The Journal of Immunology

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“…depolymerization, and preserves both the pattern and degree of sulfation [98,99]. Periodate can selectively oxidize adjacent carbons bearing unsubstituted hydroxyl and /or amino groups [100], leading, in heparins, to the splitting of C(2)-C(3) bonds of un-sulfated uronic acids including the glucuronic acid, within the ATBR, essential for high anticoagulant activity [101]. Subsequent borohydride reduction leads to the "glycol-split" (gs) derivatives, also named reduced oxyheparins (ROHs), as shown in Fig.…”

Section: Glycol-split Heparins (Gs-heparins)mentioning

confidence: 99%

Old and new applications of non-anticoagulant heparin

Cassinelli

Naggi

2016

International Journal of Cardiology

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“…To analyze further the reactions catalyzed by the three isomerases, we examined the nature of the successively formed tetrose-4-Ps by taking advantage of the fact that reduction of erythrose-4-P, erythrulose-4-P, and 3-tetrulose-4-P with tritiated borohydride leads to specific incorporation of tritium on their C1, C2, and C3, respectively. Oxidation with periodate breaks down polyols according to well-known rules (20) predicting that the first carbon of tetritol-4-P will be converted to formaldehyde, the second one to formate, and the third and fourth ones to phosphoglycolaldehyde (see the expected patterns in Fig. S5).…”

Section: Identification Of the Intermediates With Tritiated Borohydrimentioning

confidence: 99%

Erythritol feeds the pentose phosphate pathway via three new isomerases leading to D-erythrose-4-phosphate in Brucella

Barbier

Collard

Zúñiga-Ripa

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Erythritol is an important nutrient for several α-2 Proteobacteria, including N 2-fixing plant endosymbionts and Brucella, a worldwide pathogen that finds this four-carbon polyol in genital tissues. Erythritol metabolism involves phosphorylation to L-erythritol-4-phosphate by the kinase EryA and oxidation of the latter to L-3-tetrulose 4-phosphate by the dehydrogenase EryB. It is accepted that further steps involve oxidation by the putative dehydrogenase EryC and subsequent decarboxylation to yield triose-phosphates. Accordingly, growth on erythritol as the sole C source should require aldolase and fructose-1,6-bisphosphatase to produce essential hexose-6-monophosphate. However, we observed that a mutant devoid of fructose-1,6-bisphosphatases grew normally on erythritol and that EryC, which was assumed to be a dehydrogenase, actually belongs to the xylose isomerase superfamily. Moreover, we found that TpiA2 and RpiB, distant homologs of triose phosphate isomerase and ribose 5-phosphate isomerase B, were necessary, as previously shown for Rhizobium. By using purified recombinant enzymes, we demonstrated that L-3-tetrulose-4-phosphate was converted to D-erythrose 4-phosphate through three previously unknown isomerization reactions catalyzed by EryC (tetrulose-4-phosphate racemase), TpiA2 (D-3-tetrulose-4-phosphate isomerase; renamed EryH), and RpiB (D-erythrose-4-phosphate isomerase; renamed EryI), a pathway fully consistent with the isotopomer distribution of the erythrose-4-phosphate-derived amino acids phenylalanine and tyrosine obtained from bacteria grown on 13 C-labeled erythritol. D-Erythrose-4-phosphate is then converted by enzymes of the pentose phosphate pathway to glyceraldehyde 3-phosphate and fructose 6-phosphate, thus bypassing fructose-1,6-bisphosphatase. This is the first description to our knowledge of a route feeding carbohydrate metabolism exclusively via D-erythrose 4-phosphate, a pathway that may provide clues to the preferential metabolism of erythritol by Brucella and its role in pathogenicity.rucellosis is a widespread bacterial zoonosis caused by the facultative intracellular pathogens Brucella spp. Domestic ruminants and swine, which altogether represent more than 4 billion animals worldwide, are highly susceptible, and in this livestock, the brucellae characteristically target the genital organs and cause abortion and infertility (1). Close to parturition, these bacteria reach exceedingly high numbers (up to 10 14 bacteria per conceptus) (2), thus making brucellosis abortion a highly contagious condition.It is accepted that this tropism and extensive multiplication relate to the high erythritol concentration in the genital organs of those animals (3, 4). In vitro, this four-carbon polyol is a preferential carbon source of Brucella, promotes growth, and up-regulates the expression of major virulence factors and key enzymes of central metabolism (5-9). In vivo, it has been observed that parenteral injections of erythritol increase the numbers of Brucella in the spleens of intraperitoneally...

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Glycol-Cleavage Oxidation

Cited by 86 publications

References 381 publications

Reactive Carbonyls Are a Major Th2-Inducing Damage-Associated Molecular Pattern Generated by Oxidative Stress

Reactive Carbonyls Are a Major Th2-Inducing Damage-Associated Molecular Pattern Generated by Oxidative Stress

Old and new applications of non-anticoagulant heparin

Erythritol feeds the pentose phosphate pathway via three new isomerases leading to D-erythrose-4-phosphate in Brucella

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