L-Ascorbic Acid Synthesis in Birds: Phylogenetic Trend

Chaudhuri, Chanchal; Chatterjee, I. B.

doi:10.1126/science.164.3878.435

Cited by 102 publications

(45 citation statements)

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“…However, antioxidants used to counterbalance prooxidants may differ between birds and bats: two essential antioxidants, α-tocopherol and retinol, have been found in all Neotropical bat species investigated so far (Müller et al, 2007), while β-carotene and lutein, among the most important antioxidants in birds, were missing in five out of six bat species. Furthermore, in contrast to many birds (Chaudhuri and Chatterjee, 1969), batsjust like haplorhine primates, including humans (Homo sapiens), capybaras (Hydrochoerus hydrochaeris) and guinea pigs (Cavia porcellus) -are unable to synthesise vitamin C because they lack L-gulonolactone oxidase (Birney et al, 1976). Thus, it might not be feasible to extrapolate findings from birds to bats and other mammals.…”

Section: Introductionmentioning

confidence: 86%

Inflammatory challenge increases measures of oxidative stress in a free-ranging, long-lived mammal

Schneeberger

Czirják

Voigt

2013

Journal of Experimental Biology

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SUMMARYOxidative stress -the imbalance between reactive oxygen species (ROS) and neutralising antioxidants -has been under debate as the main cause of ageing in aerobial organisms. The level of ROS should increase during infection as part of the activation of an immune response, leading to oxidative damage to proteins, lipids and DNA. Yet, it is unknown how long-lived organisms, especially mammals, cope with oxidative stress. Bats are known to carry a variety of zoonotic pathogens and at the same time are, despite their high mass-specific basal metabolic rate, unusually long lived, which may be partly the result of low oxidative damage of organs. Here, we asked whether an immune challenge causes oxidative stress in free-ranging bats, measuring two oxidative stress markers. We injected 20 short-tailed fruit bats (Carollia perspicillata) with bacterially derived lipopolysaccharide (LPS) and 20 individuals with phosphate-buffered saline solution (PBS) as a control. Individuals injected with LPS showed an immune reaction by increased white blood cell count after 24 h, whereas there was no significant change in leukocyte count in control animals. The biological antioxidant potential (BAP) remained the same in both groups, but reactive oxygen metabolites (ROMs) increased after treatment with LPS, indicating a significant increase in oxidative stress in animals when mounting an immune reaction toward the inflammatory challenge. Control individuals did not show a change in oxidative stress markers. We conclude that in a long-lived mammal, even high concentrations of antioxidants do not immediately neutralise free radicals produced during a cellular immune response. Thus, fighting an infection may lead to oxidative stress in bats.

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Section: Introductionmentioning

confidence: 86%

Inflammatory challenge increases measures of oxidative stress in a free-ranging, long-lived mammal

Schneeberger

Czirják

Voigt

2013

Journal of Experimental Biology

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“…L-AA is synthesized by all higher plants and by nearly all higher animals except humans, other primates, guinea pigs, bats, and some birds (1)(2)(3). L-AA has also been reported to be present in a number of yeasts (4), but several reports suggest that L-AA analogues, rather than L-AA, are present in microorganisms (5)(6)(7).…”

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confidence: 99%

Isolation of a cDNA Coding forl-Galactono-γ-Lactone Dehydrogenase, an Enzyme involved in the Biosynthesis of Ascorbic Acid in Plants

Østergaard¹,

Persiau

Davey

et al. 1997

Journal of Biological Chemistry

140

127

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L-Galactono-␥-lactone dehydrogenase (EC 1.3.2.3; GLDase), an enzyme that catalyzes the final step in the biosynthesis of L-ascorbic acid was purified 1693-fold from a mitochondrial extract of cauliflower (Brassica oleracea, var. botrytis) to apparent homogeneity with an overall yield of 1.1%. The purification procedure consisted of anion exchange, hydrophobic interaction, gel filtration, and fast protein liquid chromatography. The enzyme had a molecular mass of 56 kDa estimated by gel filtration chromatography and SDS-polyacrylamide gel electrophoresis and showed a pH optimum for activity between pH 8.0 and 8.5, with an apparent K m of 3.3 mM for L-galactono-␥-lactone. Based on partial peptide sequence information, polymerase chain reaction fragments were isolated and used to screen a cauliflower cDNA library from which a cDNA encoding GLDase was isolated. The deduced mature GLDase contained 509 amino acid residues with a predicted molecular mass of 57,837 Da. Expression of the cDNA in yeast produced a biologically active protein displaying GLDase activity. Furthermore, we identified a substrate for the enzyme in cauliflower extract, which co-eluted with L-galactono-␥-lactone by high-performance liquid chromatography, suggesting that this compound is a naturally occurring precursor of L-ascorbic acid biosynthesis in vivo.

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“…Metaterian and eutherian mammals have GLO in their liver, but humans, monkeys, and guinea pigs lost the enzyme during their evolution. Birds have GLO in their kidney, in their liver, or in both; certain species of birds have no GLO at all (Chaudhuri and Chatterjee, 1969). Chatterjee (1973a;1973b) inferred that GLO appeared de novo when vertebrates started terrestrial life, based on the observation that GLO activity is absent in several bony fishes.…”

Section: Enzymology Of L-gulono-y-lactone Oxidase (Glo)mentioning

confidence: 97%