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Visar inlägg med etikett Csad. Visa alla inlägg

onsdag 19 juni 2019

(1) Cysteiiniaminohaposta kohti tauriinin tai sulfaatin muodostusta cys-dioxygenaasilla CDO1, joka tekee cysteiinisulfiinihappoa.

 Entsyymi cysteiinidioxygenaasi CDO1  (5q22.3)  on primäärinen cysteiiniä metaboloiva entsyymi ja tuote on  kysteiinisulfiinihappoa CSAD.

   (Tämä  CDO1 entsyymi on säätelyllinen alkukohta  sulfaatin  muodostuksessa. Sulfaattia tarvitaan detoksikaatiojärjestelmään ja  erilaisten rikkiä sisältävien kehomolekyylien luomiseen. Sulfotransferaaseja  ja arylsulfataasientsyymejä taas  avustaa kofaktorina k-vitamiini ja B6 vitamiini)

 CDO1  Cystein dioxygenase 1
https://www.ncbi.nlm.nih.gov/gene/1036
Official Symbol CDO1
Official Full Name cysteine dioxygenase type 1provided by HGNC
Also known as CDO-I
Expression Biased expression in liver (RPKM 94.6), fat (RPKM 66.8) and 8 other tissues See more
Orthologs mouse all

GeneRIFs: Gene References Into Functions

LOCUS       NP_001310494             219 aa            linear   PRI 01-JUN-2019
DEFINITION  cysteine dioxygenase type 1 isoform 1 [Homo sapiens].
ACCESSION   NP_001310494
VERSION     NP_001310494.1
DBSOURCE    REFSEQ: accession NM_001323565.2
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 219)
  AUTHORS   Tanaka Y, Kosaka Y, Waraya M, Yokota K, Harada H, Kaida T, Kikuchi
            M, Minatani N, Nishimiya H, Katoh H, Sengoku N, Watanabe M and
            Yamashita K.
  TITLE     Differential Prognostic Relevance of Promoter DNA Methylation of
            CDO1 and HOPX in Primary Breast Cancer
  JOURNAL   Anticancer Res. 39 (5), 2289-2298 (2019)
   PUBMED   31092420
  REMARK    GeneRIF: In the present study, we compared the 2 potential
            epigenetic prognostic markers of CDO1 hypermethylation and HOPX
            hypermethylation using the same breast cancer samples, and the
            final focus was given on CDO1 hypermethylation
REFERENCE   2  (residues 1 to 219)
  AUTHORS   Yokoi K, Harada H, Yokota K, Ishii S, Tanaka T, Nishizawa N,
            Shimazu M, Kojo K, Miura H, Yamanashi T, Sato T, Nakamura T,
            Watanabe M and Yamashita K.
  TITLE     Epigenetic Status of CDO1 Gene May Reflect Chemosensitivity in
            Colon Cancer with Postoperative Adjuvant Chemotherapy
  JOURNAL   Ann. Surg. Oncol. 26 (2), 406-414 (2019)
   PUBMED   30311169
  REMARK    GeneRIF: High expression of CDO1 gene increased chemoresistance in
            Colon Cancer.
REFERENCE   3  (residues 1 to 219)
  AUTHORS   Nakamoto S, Kumamoto Y, Igarashi K, Fujiyama Y, Nishizawa N, Ei S,
            Tajima H, Kaizu T, Watanabe M and Yamashita K.
  TITLE     Methylated promoter DNA of CDO1 gene and preoperative serum CA19-9
            are prognostic biomarkers in primary extrahepatic
            cholangiocarcinoma
  JOURNAL   PLoS ONE 13 (10), e0205864 (2018)
   PUBMED   30325974
  REMARK    GeneRIF: CDO1 hypermethylation, preoperative serum CA19-9 and
            perineural invasion were independent prognostic factors in primary
            extrahepatic cholangiocarcinoma
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 219)
  AUTHORS   Kojima K, Nakamura T, Ohbu M, Katoh H, Ooizumi Y, Igarashi K, Ishii
            S, Tanaka T, Yokoi K, Nishizawa N, Yokota K, Kosaka Y, Sato T,
            Watanabe M and Yamashita K.
  TITLE     Cysteine dioxygenase type 1 (CDO1) gene promoter methylation during
            the adenoma-carcinoma sequence in colorectal cancer
  JOURNAL   PLoS ONE 13 (5), e0194785 (2018)
   PUBMED   29746493
  REMARK    GeneRIF: High CDO1 methylation is associated with colorectal cancer
            progression.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 219)
  AUTHORS   Igarashi K, Yamashita K, Katoh H, Kojima K, Ooizumi Y, Nishizawa N,
            Nishiyama R, Kawamata H, Tajima H, Kaizu T, Kumamoto Y and Watanabe
            M.
  TITLE     Prognostic significance of promoter DNA hypermethylation of the
            cysteine dioxygenase 1 (CDO1) gene in primary gallbladder cancer
            and gallbladder disease
  JOURNAL   PLoS ONE 12 (11), e0188178 (2017)
   PUBMED   29161283
  REMARK    GeneRIF: Promoter NA methylation of CDO1 was demonstrated for the
            first time to be a cancer-associated methylation in primary
            gallbladder cancer(GBC), and it has the potential to be a
            prognostic biomarker of GBC for high-risk patients with stage II
            GBC.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 219)
  AUTHORS   Harrington JJ, Sherf B, Rundlett S, Jackson PD, Perry R, Cain S,
            Leventhal C, Thornton M, Ramachandran R, Whittington J, Lerner L,
            Costanzo D, McElligott K, Boozer S, Mays R, Smith E, Veloso N,
            Klika A, Hess J, Cothren K, Lo K, Offenbacher J, Danzig J and Ducar
            M.
  TITLE     Creation of genome-wide protein expression libraries using random
            activation of gene expression
  JOURNAL   Nat. Biotechnol. 19 (5), 440-445 (2001)
   PUBMED   11329013
REFERENCE   7  (residues 1 to 219)
  AUTHORS   Qusti S, Parsons RB, Abouglila KD, Waring RH, Williams AC and
            Ramsden DB.
  TITLE     Development of an in vitro model for cysteine dioxygenase
            expression in the brain
  JOURNAL   Cell Biol. Toxicol. 16 (4), 243-255 (2000)
   PUBMED   11101006  The development of an in vitro model for cysteine dioxygenase (CDO) 
expression in the brain would provide a useful model for determining the
 mechanisms for the regulation of CDO expression that does not involve 
the use of animals. Here we demonstrate the screening and 
characterization of a cell line that expresses CDO, the primary 
metabolizing enzyme of cysteine and the regulatory point of sulfate 
production. A panel of four commercially available tumor-derived human 
brain cell lines, each representing one major class of brain cell, were 
screened using western blotting and activity assay for cysteine 
dioxygenase expression. One cell line, TE 671 (human medulloblastoma) 
was found to express both a protein of approximately 70 kDa and CDO 
activity. Nuclease protection assay (NPA) of mRNA isolated from TE 671 
showed the expression of a CDO mRNA. Reverse transcription-polymerase 
chain reaction of this mRNA and sequencing of the cDNA obtained showed 
that this was indeed CDO. Treatment of TE 671 cells with cysteine 
resulted in the upregulation of CDO mRNA, whereas treatment with tumor 
necrosis factor alpha resulted in the downregulation of CDO mRNA, as 
evidenced using NPA. The characterization of an in vitro model for CDO 
expression provides a useful tool for the investigation of this 
important enzyme, which may have an etiological role in the pathogenesis
 of Parkinson's disease.
REFERENCE   8  (residues 1 to 219)
  AUTHORS   Ramsden DB, Kapadi A, Fitch NJ, Farmer MJ, Bennett P and Williams
            AC.
  TITLE     Human cysteine dioxygenase type I (CDO-I; EC 1.13.11.20): 5'
            flanking region and intron-exon structure of the gene
  JOURNAL   MP, Mol. Pathol. 50 (5), 269-271 (1997)
   PUBMED   9497919
REFERENCE   9  (residues 1 to 219)
  AUTHORS   Jeremiah S, McCann KP, Williams AC, Ramsden DB, Pilz AJ, Fox MF and
            Povey S.
  TITLE     Chromosomal localisation of genes coding for human and mouse liver
            cytosolic cysteine dioxygenase
  JOURNAL   Ann. Hum. Genet. 60 (1), 29-33 (1996)
   PUBMED   8835096
REFERENCE   10 (residues 1 to 219)
  AUTHORS   McCann KP, Akbari MT, Williams AC and Ramsden DB.
  TITLE     Human cysteine dioxygenase type I: primary structure derived from
            base sequencing of cDNA
  JOURNAL   Biochim. Biophys. Acta 1209 (1), 107-110 (1994)
   PUBMED   7524679
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC026449.6, DA849625.1, AK130357.1 and BC024241.2.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR5189664.60540.1,
                                           SRR1803613.237389.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2467146, SAMEA2467147
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..219
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q22.3"
     Protein         1..219
                     /product="cysteine dioxygenase type 1 isoform 1"
                     /EC_number="1.13.11.20"
                     /note="cysteine dioxygenase, type I"
                     /calculated_mol_wt=24700
     CDS             1..219
                     /gene="CDO1"
                     /gene_synonym="CDO-I"
                     /coded_by="NM_001323565.2:263..922"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:1036"
                     /db_xref="HGNC:HGNC:1795"
                     /db_xref="MIM:603943"
ORIGIN      
        1 meqtevlkpr tladlirilh qlfagdevnv eevqaimeay esdptewamy akfdqysrgr
       61 glqfvvgggs gggwlwytrn lvdqgngkfn lmilcwgegh gssihdhtns hcflkmlqgn
      121 lketlfawpd kksnemvkks ervlrenqca yindsiglhr venishtepa vslhlysppf
      181 dtchafdqrt ghknkvtmtf hskfgirtpn atsgslenn
//
Seuraaksi CSAD- molekyylistä cysteinsulphinic acid , kysteiinisulfiinihappo.

lördag 24 november 2012

CSAD entsyymi aivoissa ( 10 löytöä PubMed)

Results: 10

1.
Chang YC, Ding ST, Lee YH, Wang YC, Huang MF, Liu IH.
Amino Acids. 2012 Aug 21. [Epub ahead of print]
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Wu JY, Tang XW, Schloss JV, Faiman MD.
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Tang XW, Hsu CC, Schloss JV, Faiman MD, Wu E, Yang CY, Wu JY.
J Neurosci. 1997 Sep 15;17(18):6947-51.
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Tang XW, Hsu CC, Sun Y, Wu E, Yang CY, Wu JY.
J Biomed Sci. 1996 Nov-Dec;3(6):442-453.
PMID:
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[PubMed - as supplied by publisher]
5.
Taber KH, Lin CT, Liu JW, Thalmann RH, Wu JY.
Brain Res. 1986 Oct 29;386(1-2):113-21.
PMID:
2430674
[PubMed - indexed for MEDLINE]
6.
Wu H, Song GX, Liu SD.
Zhongguo Yi Xue Ke Xue Yuan Xue Bao. 1986 Oct;8(5):391-3. Chinese. No abstract available.
PMID:
2952314
[PubMed - indexed for MEDLINE]
7.
Heinämäki AA, Malila SI, Tolonen KM, Valkonen KH, Piha RS.
Neurochem Res. 1983 Feb;8(2):207-18.
PMID:
6856026
[PubMed - indexed for MEDLINE]
9.
Sturman JA.
J Neurochem. 1981 Jan;36(1):304-6.
PMID:
7193241
[PubMed - indexed for MEDLINE]
10.
Staines WA, Benjamin AM, McGeer EG.
J Neurosci Res. 1980;5(6):555-62.
PMID:
7205993
[PubMed - indexed for MEDLINE]

Tauriinin homeostaasi vaatii de novo synteesin

Amino Acids. 2012 Aug 21. [Epub ahead of print]  Taurine homeostasis requires de novo synthesis via cysteine sulfinic acid decarboxylase during zebrafish early embryogenesis.

Source

Department of Animal Science and Technology, National Taiwan University, Taipei, 106, Taiwan.

Abstract

Cysteine sulfinic acid decarboxylase (Csad) is the rate-limiting enzyme in the de novo biosynthesis of taurine. There are a number of physiological roles of taurine, such as bile salt synthesis, osmoregulation, lipid metabolism, and oxidative stress inhibition. To investigate the role of de novo synthesis of taurine during embryonic development, zebrafish csad was cloned and functionally analyzed. Semi-quantitative RT-PCR showed that csad transcripts are maternally deposited, while whole-mount in situ hybridization demonstrated that csad is expressed in yolk syncytial layer and various embryonic tissues such as notochord, brain, retina, pronephric duct, liver, and pancreas. Knockdown of csad significantly reduced the embryonic taurine level, and the affected embryos had increased early mortality and cardiac anomalies. mRNA coinjection and taurine supplementation rescued the cardiac phenotypes suggesting that taurine originating from the de novo synthesis pathway plays a role in cardiac development. Our findings indicated that the de novo synthesis pathway via Csad plays a critical role in taurine homeostasis and cardiac development in zebrafish early embryos.

  • ONKO AIVOISSA tätä csad entsyymiä, jota aivo voi tehdä tauriinia ?Tästä on vastaus vuodelta 1996.  On.
J Biomed Sci. 1996 Nov-Dec;3(6):442-453. Multiplicity of Brain Cysteine Sulfinic Acid Decarboxylase - Purification, Characterization and Subunit Structure.

Source

Department of Physiology and Cell Biology, University of Kansas, Lawrence, Kans., USA.

Abstract

Cysteine sulfinic acid decarboxylase (CSAD), the rate-limiting enzyme in taurine biosynthesis, appears to be present in the brain in multiple isoforms. Two distinct forms of CSAD, referred to as CSAD I and CSAD II, were obtained on Sephadex G-100 column. CSAD I and CSAD II differ in: (1) the elution profile on Sephadex G-100 column; (2) the sensitivity towards Mn(2+), methione, and other sulfur-containing amino acids, and (3) their immunologic properties. CSAD II has been purified to about 2,500-fold by a combination of column chromatographies and polyacrylamide gel electrophoresis (PAGE). The purity of the enzyme preparation was established as judged from the following observations: (1) a single protein band was observed under various electrophoretic conditions, e.g., 5-20% nondenaturing PAGE, 7% nondenaturing PAGE and 10% SDS-PAGE, and (2) in nondenaturing PAGE, the protein band comigrated with CSAD activity. CSAD II has a molecular weight of 90 kDa and is a homodimer consisting of two 43 +/- 2 kDa subunits. CSAD appears to require Mn(2+) for its maximum activity. Other divalent cations fail to replace Mn(2+) in activation of CSAD activity. However, the precise role of Mn(2+) in the action of CSAD remains to be determined. Copyright 1996 S. Karger AG, Basel