L-Ascorbate Biosynthesis Involves Carbon Skeleton Rearrangement in the Nematode Caenorhabditis elegans
Ascorbate (AsA) is required as a cofactor and is widely distributed in plants and animals. Recently, it has been suggested that the nematode Caenorhabditis elegans also synthesizes AsA. However, its biosynthetic pathway is still unknown. To further understand AsA biosynthesis in C. elegans, we analy...
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| Published in | Metabolites Vol. 10; no. 8; p. 334 |
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| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
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17.08.2020
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| ISSN | 2218-1989 2218-1989 |
| DOI | 10.3390/metabo10080334 |
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| Abstract | Ascorbate (AsA) is required as a cofactor and is widely distributed in plants and animals. Recently, it has been suggested that the nematode Caenorhabditis elegans also synthesizes AsA. However, its biosynthetic pathway is still unknown. To further understand AsA biosynthesis in C. elegans, we analyzed the incorporation of the 13C atom into AsA using gas chromatography-mass spectrometry (GC-MS) in worms fed with D-Glc (1-13C)-labeled Escherichia coli. GC-MS analysis revealed that AsA biosynthesis in C. elegans, similarly to that in mammalian systems, involves carbon skeleton rearrangement. The addition of L-gulono-1,4-lactone, an AsA precursor in the mammalian pathway, significantly increased AsA level in C. elegans, whereas the addition of L-galactono-1,4-lactone, an AsA precursor in the plant and Euglena pathway, did not affect AsA level. The suppression of E03H4.3 (an ortholog of gluconolactonase) or the deficiency of F54D5.12 (an ortholog of L-gulono-1,4-lactone oxidase) significantly decreased AsA level in C. elegans. Although N2- and AsA-deficient F54D5.12 knockout mutant worm (tm6671) morphologies and the ratio of collagen to non-collagen protein did not show any significant differences, the mutant worms exhibited increased malondialdehyde levels and reduced lifespan compared with the N2 worms. In conclusion, our findings indicate that the AsA biosynthetic pathway is similar in C. elegans and mammals. |
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| AbstractList | Ascorbate (AsA) is required as a cofactor and is widely distributed in plants and animals. Recently, it has been suggested that the nematode Caenorhabditis elegans also synthesizes AsA. However, its biosynthetic pathway is still unknown. To further understand AsA biosynthesis in C. elegans, we analyzed the incorporation of the 13C atom into AsA using gas chromatography-mass spectrometry (GC-MS) in worms fed with D-Glc (1-13C)-labeled Escherichia coli. GC-MS analysis revealed that AsA biosynthesis in C. elegans, similarly to that in mammalian systems, involves carbon skeleton rearrangement. The addition of L-gulono-1,4-lactone, an AsA precursor in the mammalian pathway, significantly increased AsA level in C. elegans, whereas the addition of L-galactono-1,4-lactone, an AsA precursor in the plant and Euglena pathway, did not affect AsA level. The suppression of E03H4.3 (an ortholog of gluconolactonase) or the deficiency of F54D5.12 (an ortholog of L-gulono-1,4-lactone oxidase) significantly decreased AsA level in C. elegans. Although N2- and AsA-deficient F54D5.12 knockout mutant worm (tm6671) morphologies and the ratio of collagen to non-collagen protein did not show any significant differences, the mutant worms exhibited increased malondialdehyde levels and reduced lifespan compared with the N2 worms. In conclusion, our findings indicate that the AsA biosynthetic pathway is similar in C. elegans and mammals. Ascorbate (AsA) is required as a cofactor and is widely distributed in plants and animals. Recently, it has been suggested that the nematode Caenorhabditis elegans also synthesizes AsA. However, its biosynthetic pathway is still unknown. To further understand AsA biosynthesis in C. elegans , we analyzed the incorporation of the 13 C atom into AsA using gas chromatography-mass spectrometry (GC-MS) in worms fed with D-Glc (1- 13 C)-labeled Escherichia coli . GC-MS analysis revealed that AsA biosynthesis in C. elegans , similarly to that in mammalian systems, involves carbon skeleton rearrangement. The addition of L-gulono-1,4-lactone, an AsA precursor in the mammalian pathway, significantly increased AsA level in C. elegans , whereas the addition of L-galactono-1,4-lactone, an AsA precursor in the plant and Euglena pathway, did not affect AsA level. The suppression of E03H4.3 (an ortholog of gluconolactonase) or the deficiency of F54D5.12 (an ortholog of L-gulono-1,4-lactone oxidase) significantly decreased AsA level in C. elegans . Although N2- and AsA-deficient F54D5.12 knockout mutant worm (tm6671) morphologies and the ratio of collagen to non-collagen protein did not show any significant differences, the mutant worms exhibited increased malondialdehyde levels and reduced lifespan compared with the N2 worms. In conclusion, our findings indicate that the AsA biosynthetic pathway is similar in C. elegans and mammals. Ascorbate (AsA) is required as a cofactor and is widely distributed in plants and animals. Recently, it has been suggested that the nematode Caenorhabditis elegans also synthesizes AsA. However, its biosynthetic pathway is still unknown. To further understand AsA biosynthesis in C. elegans, we analyzed the incorporation of the 13C atom into AsA using gas chromatography-mass spectrometry (GC-MS) in worms fed with D-Glc (1-13C)-labeled Escherichia coli. GC-MS analysis revealed that AsA biosynthesis in C. elegans, similarly to that in mammalian systems, involves carbon skeleton rearrangement. The addition of L-gulono-1,4-lactone, an AsA precursor in the mammalian pathway, significantly increased AsA level in C. elegans, whereas the addition of L-galactono-1,4-lactone, an AsA precursor in the plant and Euglena pathway, did not affect AsA level. The suppression of E03H4.3 (an ortholog of gluconolactonase) or the deficiency of F54D5.12 (an ortholog of L-gulono-1,4-lactone oxidase) significantly decreased AsA level in C. elegans. Although N2- and AsA-deficient F54D5.12 knockout mutant worm (tm6671) morphologies and the ratio of collagen to non-collagen protein did not show any significant differences, the mutant worms exhibited increased malondialdehyde levels and reduced lifespan compared with the N2 worms. In conclusion, our findings indicate that the AsA biosynthetic pathway is similar in C. elegans and mammals.Ascorbate (AsA) is required as a cofactor and is widely distributed in plants and animals. Recently, it has been suggested that the nematode Caenorhabditis elegans also synthesizes AsA. However, its biosynthetic pathway is still unknown. To further understand AsA biosynthesis in C. elegans, we analyzed the incorporation of the 13C atom into AsA using gas chromatography-mass spectrometry (GC-MS) in worms fed with D-Glc (1-13C)-labeled Escherichia coli. GC-MS analysis revealed that AsA biosynthesis in C. elegans, similarly to that in mammalian systems, involves carbon skeleton rearrangement. The addition of L-gulono-1,4-lactone, an AsA precursor in the mammalian pathway, significantly increased AsA level in C. elegans, whereas the addition of L-galactono-1,4-lactone, an AsA precursor in the plant and Euglena pathway, did not affect AsA level. The suppression of E03H4.3 (an ortholog of gluconolactonase) or the deficiency of F54D5.12 (an ortholog of L-gulono-1,4-lactone oxidase) significantly decreased AsA level in C. elegans. Although N2- and AsA-deficient F54D5.12 knockout mutant worm (tm6671) morphologies and the ratio of collagen to non-collagen protein did not show any significant differences, the mutant worms exhibited increased malondialdehyde levels and reduced lifespan compared with the N2 worms. In conclusion, our findings indicate that the AsA biosynthetic pathway is similar in C. elegans and mammals. |
| Author | Yanagimoto, Ayako Okamoto, Naho Yoshida, Shinichi Aoki, Yuka Yabuta, Yukinori Bito, Tomohiro Hara, Hiroka Ishihara, Atsushi Watanabe, Fumio Nagata, Ryuta Kariya, Ayumi Wada, Kousuke |
| AuthorAffiliation | 3 Electronic and Organic Material Laboratory, Tottori Institute of Industrial Technology, 7-1-1 Wakabadai-minami, Tottori 689-1112, Japan; syoshida@tiit.or.jp 2 The United Graduate School of Agricultural Sciences, Tottori University, 4-101 Koyama-Minami, Tottori 680-8553, Japan; d18a2005y@edu.tottoir-u.ac.jp 1 Department of Agricultural, Life and Environmental Sciences, Faculty of Agriculture, Tottori University, 4-101 Koyama-Minami, Tottori 680-8553, Japan; b17a5143u@edu.tottori-u.ac.jp (R.N.); koromimi.love.0703@gmail.com (Y.A.); kariyaayumi11@gmail.com (A.K.); vitaminc198.11@gmail.com (K.W.); ascorbate250@gmail.com (A.Y.); a3416341@yahoo.co.jp (H.H.); bito@tottori-u.ac.jp (T.B.); aishihara@tottori-u.ac.jp (A.I.); watanabe@tottori-u.ac.jp (F.W.) |
| AuthorAffiliation_xml | – name: 2 The United Graduate School of Agricultural Sciences, Tottori University, 4-101 Koyama-Minami, Tottori 680-8553, Japan; d18a2005y@edu.tottoir-u.ac.jp – name: 1 Department of Agricultural, Life and Environmental Sciences, Faculty of Agriculture, Tottori University, 4-101 Koyama-Minami, Tottori 680-8553, Japan; b17a5143u@edu.tottori-u.ac.jp (R.N.); koromimi.love.0703@gmail.com (Y.A.); kariyaayumi11@gmail.com (A.K.); vitaminc198.11@gmail.com (K.W.); ascorbate250@gmail.com (A.Y.); a3416341@yahoo.co.jp (H.H.); bito@tottori-u.ac.jp (T.B.); aishihara@tottori-u.ac.jp (A.I.); watanabe@tottori-u.ac.jp (F.W.) – name: 3 Electronic and Organic Material Laboratory, Tottori Institute of Industrial Technology, 7-1-1 Wakabadai-minami, Tottori 689-1112, Japan; syoshida@tiit.or.jp |
| Author_xml | – sequence: 1 givenname: Yukinori orcidid: 0000-0002-6982-8522 surname: Yabuta fullname: Yabuta, Yukinori – sequence: 2 givenname: Ryuta surname: Nagata fullname: Nagata, Ryuta – sequence: 3 givenname: Yuka surname: Aoki fullname: Aoki, Yuka – sequence: 4 givenname: Ayumi surname: Kariya fullname: Kariya, Ayumi – sequence: 5 givenname: Kousuke surname: Wada fullname: Wada, Kousuke – sequence: 6 givenname: Ayako surname: Yanagimoto fullname: Yanagimoto, Ayako – sequence: 7 givenname: Hiroka surname: Hara fullname: Hara, Hiroka – sequence: 8 givenname: Tomohiro orcidid: 0000-0001-6654-4148 surname: Bito fullname: Bito, Tomohiro – sequence: 9 givenname: Naho surname: Okamoto fullname: Okamoto, Naho – sequence: 10 givenname: Shinichi surname: Yoshida fullname: Yoshida, Shinichi – sequence: 11 givenname: Atsushi surname: Ishihara fullname: Ishihara, Atsushi – sequence: 12 givenname: Fumio surname: Watanabe fullname: Watanabe, Fumio |
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| CitedBy_id | crossref_primary_10_7554_eLife_94181 crossref_primary_10_1128_msystems_00312_22 crossref_primary_10_2989_16085914_2023_2200853 crossref_primary_10_3390_ani13152502 crossref_primary_10_7554_eLife_94181_3 |
| Cites_doi | 10.1021/bi2019139 10.1074/jbc.M803930200 10.1042/bj3040385 10.1016/0304-4165(92)90108-7 10.1016/j.abb.2015.02.002 10.1007/978-1-4613-0325-1_2 10.1038/nbt777 10.1016/S0021-9258(19)36707-9 10.1016/S0021-9258(18)97021-3 10.1016/S0021-9258(18)55401-6 10.1038/30728 10.3177/jnsv.49.315 10.1186/1475-2891-2-7 10.1042/bj2920605 10.1016/S0076-6879(05)01005-0 10.1111/j.1440-1827.2003.01603.x 10.1104/pp.107.109934 10.1093/pcp/41.6.666 10.7554/eLife.06369 10.1042/bse0520113 10.1074/jbc.M203824200 10.1038/nature03809 10.1074/jbc.M200895200 10.1128/MCB.20.11.4084-4093.2000 10.1093/clinchem/36.10.1807 10.1093/ajcn/54.6.1147s 10.1073/pnas.0511225103 10.1016/S0021-9258(17)34915-3 10.1016/j.tig.2003.11.004 10.1016/j.redox.2016.10.013 10.1111/j.1749-6632.1985.tb51167.x 10.1074/jbc.272.48.30009 10.1104/pp.103.033936 10.1093/genetics/155.3.1139 10.3177/jnsv.25.299 10.3164/jcbn.34.61 10.1016/j.freeradbiomed.2018.03.033 10.1016/0006-291X(81)91300-0 10.1074/jbc.272.36.22607 10.1093/genetics/77.1.71 10.1038/ncomms10573 10.1016/0003-9861(76)90530-0 10.1073/pnas.97.9.4736 10.1016/S0021-9258(18)47082-2 10.1016/0891-5849(94)90019-1 10.1534/g3.117.300325 10.1074/jbc.M111.266692 10.1006/dbio.2000.9897 10.1016/S1097-2765(00)80003-9 10.1093/oxfordjournals.pcp.a029341 10.1074/jbc.273.44.28708 10.1016/j.biomaterials.2009.08.036 10.1194/jlr.M064808 10.1074/jbc.273.36.23039 10.1016/j.taap.2018.09.026 |
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| References | Winter (ref_30) 2000; 20 Agius (ref_22) 2003; 21 Friedman (ref_12) 1965; 240 Naidu (ref_1) 2003; 2 Shi (ref_34) 2016; 57 Jurgensen (ref_7) 2011; 286 Ishikawa (ref_29) 2008; 283 Mori (ref_16) 2004; 54 Wells (ref_48) 1990; 265 Zhang (ref_24) 2008; 146 Bhadriraju (ref_6) 2009; 30 Matsunaga (ref_55) 2016; 7 Wheeler (ref_20) 1998; 393 Bito (ref_56) 2017; 11 Rebouche (ref_11) 1991; 54 Yabuta (ref_27) 2000; 41 Hudson (ref_9) 2012; 51 ref_21 Lorence (ref_23) 2004; 134 Flavel (ref_57) 2018; 8 Ishii (ref_41) 2004; 34 Chen (ref_8) 2019; 362 Shigeoka (ref_28) 1979; 25 Veijola (ref_31) 1994; 269 Inai (ref_19) 2003; 49 Persiau (ref_25) 1997; 272 Nishikimi (ref_17) 1976; 175 Kondo (ref_14) 2006; 103 Hill (ref_37) 2000; 55 Vanfleteren (ref_40) 1993; 292 Bode (ref_45) 1990; 36 Myllyharju (ref_3) 2004; 20 Norman (ref_35) 2000; 227 Smirnoff (ref_42) 2018; 122 ref_33 Ito (ref_43) 1981; 101 Winkler (ref_46) 1994; 17 Yamauchi (ref_4) 2012; 52 Vogel (ref_5) 1997; 1 Riihimaa (ref_39) 2002; 277 Friedman (ref_36) 2000; 97 Hulse (ref_10) 1978; 253 Whitbread (ref_49) 2005; 401 Sieburth (ref_54) 2005; 436 Nishikimi (ref_13) 1996; 25 Ishikawa (ref_47) 1998; 273 Fujita (ref_15) 1992; 1116 Nishikimi (ref_18) 1992; 267 Kivirikko (ref_2) 1985; 460 May (ref_52) 1997; 272 Maellaro (ref_51) 1994; 304 Brenner (ref_53) 1974; 77 Myllyharju (ref_38) 2002; 277 Patananan (ref_32) 2015; 569 May (ref_44) 1998; 273 Imai (ref_26) 1998; 39 Du (ref_50) 2012; 1826 |
| References_xml | – volume: 51 start-page: 2417 year: 2012 ident: ref_9 article-title: Peptidyl 3-hydroxyproline binding properties of type I collagen suggest a function in fibril supramolecular assembly publication-title: Biochemistry doi: 10.1021/bi2019139 – volume: 283 start-page: 31133 year: 2008 ident: ref_29 article-title: The pathway via D-galacturonate/L-galactonate is significant for ascorbate biosynthesis in Euglena gracilis: Identification and functional characterization of aldonolactonase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M803930200 – volume: 304 start-page: 385 year: 1994 ident: ref_51 article-title: Purification of NADPH-dependent dehydroascorbate reductase from rat liver and its identification with 3α-hydroxysteroid dehydrogenase publication-title: Biochem. J. doi: 10.1042/bj3040385 – volume: 1116 start-page: 122 year: 1992 ident: ref_15 article-title: Purification of senescence marker protein-30 (SMP30) and its androgen-independent decrease with age in the rat liver publication-title: Biochim. Biophys. Acta doi: 10.1016/0304-4165(92)90108-7 – volume: 569 start-page: 32 year: 2015 ident: ref_32 article-title: The invertebrate Caenorhabditis elegans biosynthesizes ascorbate publication-title: Arch. Biochem Biophys. doi: 10.1016/j.abb.2015.02.002 – volume: 25 start-page: 17 year: 1996 ident: ref_13 article-title: Biochemistry and molecular biology of ascorbic acid biosynthesis publication-title: Subcell. Biochem. doi: 10.1007/978-1-4613-0325-1_2 – volume: 21 start-page: 177 year: 2003 ident: ref_22 article-title: Engineering increased vitamin C levels in plants by overexpression of a D-galacturonic acid reductase publication-title: Nat. Biotechnol. doi: 10.1038/nbt777 – volume: 267 start-page: 21967 year: 1992 ident: ref_18 article-title: Guinea pigs possess a highly mutated gene for L-gulono-γ-lactone oxidase, the key enzyme for L-ascorbic acid biosynthesis missing in this species publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(19)36707-9 – volume: 240 start-page: 4763 year: 1965 ident: ref_12 article-title: 3,4-dihydroxyphenylethylamine ß-hydroxylase. physical properties, copper content, and role of copper in the catalytic activity publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)97021-3 – volume: 265 start-page: 15361 year: 1990 ident: ref_48 article-title: Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)55401-6 – volume: 393 start-page: 365 year: 1998 ident: ref_20 article-title: The biosynthetic pathway of vitamin C in higher plants publication-title: Nature doi: 10.1038/30728 – volume: 49 start-page: 315 year: 2003 ident: ref_19 article-title: The whole structure of the human nonfunctional L-gulono-γ-lactone oxidase gene—The gene responsible for scurvy--and the evolution of repetitive sequences thereon publication-title: J. Nutr. Sci Vitaminol. doi: 10.3177/jnsv.49.315 – volume: 2 start-page: 7 year: 2003 ident: ref_1 article-title: Vitamin C in human health and disease is still a mystery? An overview publication-title: Nutr. J. doi: 10.1186/1475-2891-2-7 – volume: 292 start-page: 605 year: 1993 ident: ref_40 article-title: Oxidative stress and ageing in Caenorhabditis elegans publication-title: Biochem. J. doi: 10.1042/bj2920605 – volume: 401 start-page: 78 year: 2005 ident: ref_49 article-title: Characterization of the omega class of glutathione transferases publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(05)01005-0 – volume: 54 start-page: 167 year: 2004 ident: ref_16 article-title: Senescence marker protein-30 knockout mouse as a novel murine model of senile lung publication-title: Pathol. Int. doi: 10.1111/j.1440-1827.2003.01603.x – volume: 146 start-page: 431 year: 2008 ident: ref_24 article-title: An Arabidopsis purple acid phosphatase with phytase activity increases foliar ascorbate publication-title: Plant Physiol. doi: 10.1104/pp.107.109934 – volume: 41 start-page: 666 year: 2000 ident: ref_27 article-title: Molecular characterization of tobacco mitochondrial L-galactono-γ-lactone dehydrogenase and its expression in Escherichia coli publication-title: Plant Cell Physiol. doi: 10.1093/pcp/41.6.666 – ident: ref_21 doi: 10.7554/eLife.06369 – volume: 1826 start-page: 443 year: 2012 ident: ref_50 article-title: Ascorbic acid: Chemistry, biology and the treatment of cancer publication-title: Biochim. Biophys. Acta – volume: 52 start-page: 113 year: 2012 ident: ref_4 article-title: Lysine post-translational modifications of collagen publication-title: Essays Biochem. doi: 10.1042/bse0520113 – volume: 277 start-page: 29187 year: 2002 ident: ref_38 article-title: The exoskeleton collagens in Caenorhabditis elegans are modified by prolyl 4-hydroxylases with unique combinations of subunits publication-title: J. Biol. Chem. doi: 10.1074/jbc.M203824200 – volume: 436 start-page: 510 year: 2005 ident: ref_54 article-title: Systematic analysis of genes required for synapse structure and function publication-title: Nature doi: 10.1038/nature03809 – volume: 277 start-page: 18238 year: 2002 ident: ref_39 article-title: Egg shell collagen formation in Caenorhabditis elegans involves a novel prolyl 4-hydroxylase expressed in spermatheca and embryos and possessing many unique properties publication-title: J. Biol. Chem. doi: 10.1074/jbc.M200895200 – volume: 20 start-page: 4084 year: 2000 ident: ref_30 article-title: Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans publication-title: Mol. Cell Biol. doi: 10.1128/MCB.20.11.4084-4093.2000 – volume: 36 start-page: 1807 year: 1990 ident: ref_45 article-title: Spontaneous decay of oxidized ascorbic acid (dehydro-L-ascorbic acid) evaluated by high-pressure liquid chromatography publication-title: Clin. Chem. doi: 10.1093/clinchem/36.10.1807 – volume: 54 start-page: 1147S year: 1991 ident: ref_11 article-title: Ascorbic acid and carnitine biosynthesis publication-title: Am. J. Clin. Nutr. doi: 10.1093/ajcn/54.6.1147s – volume: 103 start-page: 5723 year: 2006 ident: ref_14 article-title: Senescence marker protein 30 functions as gluconolactonase in L-ascorbic acid biosynthesis, and its knockout mice are prone to scurvy publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.0511225103 – volume: 253 start-page: 1654 year: 1978 ident: ref_10 article-title: Carnitine biosynthesis. β-hydroxylation of trimethyllysine by an α-ketoglutarate-dependent mitochondrial dioxygenase publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(17)34915-3 – volume: 20 start-page: 33 year: 2004 ident: ref_3 article-title: Collagens, modifying enzymes and their mutations in humans, flies and worms publication-title: Trends Genet. doi: 10.1016/j.tig.2003.11.004 – volume: 11 start-page: 21 year: 2017 ident: ref_56 article-title: Vitamin B12 deficiency results in severe oxidative stress, leading to memory retention impairment in Caenorhabditis elegans publication-title: Redox Biol. doi: 10.1016/j.redox.2016.10.013 – volume: 460 start-page: 187 year: 1985 ident: ref_2 article-title: Post-translational processing of procollagens publication-title: Ann. N. Y. Acad. Sci. doi: 10.1111/j.1749-6632.1985.tb51167.x – volume: 272 start-page: 30009 year: 1997 ident: ref_25 article-title: Isolation of a cDNA coding for L-galactono-γ-lactone dehydrogenase, an enzyme involved in the biosynthesis of ascorbic acid in plants. Purification, characterization, cDNA cloning, and expression in yeast publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.48.30009 – volume: 134 start-page: 1200 year: 2004 ident: ref_23 article-title: myo-inositol oxygenase offers a possible entry point into plant ascorbate biosynthesis publication-title: Plant Physiol. doi: 10.1104/pp.103.033936 – volume: 55 start-page: 1139 year: 2000 ident: ref_37 article-title: dpy-18 encodes an α-subunit of prolyl-4-hydroxylase in Caenorhabditis elegans publication-title: Genetics doi: 10.1093/genetics/155.3.1139 – volume: 25 start-page: 299 year: 1979 ident: ref_28 article-title: The biosynthetic pathway of L-ascorbic acid in Euglena gracilis Z publication-title: J. Nutr. Sci. Vitaminol. doi: 10.3177/jnsv.25.299 – volume: 34 start-page: 61 year: 2004 ident: ref_41 article-title: Life span and oxidative stress in nematode publication-title: J. Clin. Biochem. Nutr. doi: 10.3164/jcbn.34.61 – volume: 122 start-page: 116 year: 2018 ident: ref_42 article-title: Ascorbic acid metabolism and functions: A comparison of plants and mammals publication-title: Free Radic. Biol. Med. doi: 10.1016/j.freeradbiomed.2018.03.033 – volume: 101 start-page: 591 year: 1981 ident: ref_43 article-title: Participation of a cytochrome b5-like hemoprotein of outer mitochondrial membrane (OM cytochrome b) in NADH-semidehydroascorbic acid reductase activity of rat liver publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/0006-291X(81)91300-0 – volume: 272 start-page: 22607 year: 1997 ident: ref_52 article-title: Reduction of dehydroascorbate to ascorbate by the selenoenzyme thioredoxin reductase publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.36.22607 – volume: 77 start-page: 71 year: 1974 ident: ref_53 article-title: The genetics of Caenorhabditis elegans publication-title: Genetics doi: 10.1093/genetics/77.1.71 – volume: 7 start-page: 10573 year: 2016 ident: ref_55 article-title: Diapause is associated with a change in the polarity of secretion of insulin-like peptides publication-title: Nat. Commun. doi: 10.1038/ncomms10573 – volume: 175 start-page: 427 year: 1976 ident: ref_17 article-title: Purification and characterization of L-gulono-γ-lactone oxidase from rat and goat liver publication-title: Arch. Biochem. Biophys. doi: 10.1016/0003-9861(76)90530-0 – volume: 97 start-page: 4736 year: 2000 ident: ref_36 article-title: Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegans publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.97.9.4736 – volume: 269 start-page: 26746 year: 1994 ident: ref_31 article-title: Cloning, baculovirus expression, and characterization of the α subunit of prolyl 4-hydroxylase from the nematode Caenorhabditis elegans. This α subunit forms an active αβ dimer with the human protein disulfide isomerase/β subunit publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)47082-2 – volume: 17 start-page: 333 year: 1994 ident: ref_46 article-title: The redox couple between glutathione and ascorbic acid: A chemical and physiological perspective publication-title: Free Radic. Biol. Med. doi: 10.1016/0891-5849(94)90019-1 – volume: 8 start-page: 567 year: 2018 ident: ref_57 article-title: Growth of Caenorhabditis elegans in defined media is dependent on presence of particulate matter publication-title: G3 doi: 10.1534/g3.117.300325 – volume: 286 start-page: 32736 year: 2011 ident: ref_7 article-title: A novel functional role of collagen glycosylation: Interaction with the endocytic collagen receptor uparap/ENDO180 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.266692 – volume: 227 start-page: 690 year: 2000 ident: ref_35 article-title: The let-268 locus of Caenorhabditis elegans encodes a procollagen lysyl hydroxylase that is essential for type IV collagen secretion publication-title: Dev. Biol. doi: 10.1006/dbio.2000.9897 – volume: 1 start-page: 13 year: 1997 ident: ref_5 article-title: The discoidin domain receptor tyrosine kinases are activated by collagen publication-title: Mol. Cell doi: 10.1016/S1097-2765(00)80003-9 – ident: ref_33 – volume: 39 start-page: 1350 year: 1998 ident: ref_26 article-title: L-galactono-γ-lactone dehydrogenase from sweet potato: Purification and cDNA sequence analysis publication-title: Plant Cell Physiol. doi: 10.1093/oxfordjournals.pcp.a029341 – volume: 273 start-page: 28708 year: 1998 ident: ref_47 article-title: Molecular cloning and functional expression of rat liver glutathione-dependent dehydroascorbate reductase publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.44.28708 – volume: 30 start-page: 6687 year: 2009 ident: ref_6 article-title: The relative roles of collagen adhesive receptor DDR2 activation and matrix stiffness on the downregulation of focal adhesion kinase in vascular smooth muscle cells publication-title: Biomaterials doi: 10.1016/j.biomaterials.2009.08.036 – volume: 57 start-page: 265 year: 2016 ident: ref_34 article-title: A Caenorhabditis elegans model for ether lipid biosynthesis and function publication-title: J. Lipid Res. doi: 10.1194/jlr.M064808 – volume: 273 start-page: 23039 year: 1998 ident: ref_44 article-title: Reduction of the ascorbyl free radical to ascorbate by thioredoxin reductase publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.36.23039 – volume: 362 start-page: 9 year: 2019 ident: ref_8 article-title: Effect of N-(2-aminoethyl) ethanolamine on hypertrophic scarring changes in vitro: Finding novel anti-fibrotic therapies publication-title: Toxicol. Appl. Pharmacol. doi: 10.1016/j.taap.2018.09.026 |
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| Snippet | Ascorbate (AsA) is required as a cofactor and is widely distributed in plants and animals. Recently, it has been suggested that the nematode Caenorhabditis... Ascorbate (AsA) is required as a cofactor and is widely distributed in plants and animals. Recently, it has been suggested that the nematode Caenorhabditis... |
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| SubjectTerms | antioxidant Ascorbic acid Biosynthesis biosynthetic pathway Caenorhabditis elegans Carbon Collagen Dopamine E coli Enzymes Gas chromatography Gene expression Gluconolactonase Kidneys L-ascorbate (AsA) Life span Malondialdehyde Mammals Mass spectroscopy Mutants Nematodes Proteins reactive oxygen species redox Worms |
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| Title | L-Ascorbate Biosynthesis Involves Carbon Skeleton Rearrangement in the Nematode Caenorhabditis elegans |
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