A Novel Cysteine Sulfinic Acid Decarboxylase Knock-Out Mouse: Taurine Distribution in Various Tissues With and Without Taurine Supplementation

2017 ◽  
pp. 461-474 ◽  
Author(s):  
Eunkyue Park ◽  
Seung Yong Park ◽  
In Soo Cho ◽  
Bo Sook Kim ◽  
Georgia Schuller-Levis
Keyword(s):  
Acid Decarboxylase ◽  
Sulfinic Acid ◽  
Taurine Supplementation ◽  
Cysteine Sulfinic Acid ◽  
Knock Out ◽  
Cysteine Sulfinic Acid Decarboxylase ◽  
Knock Out Mouse

scholarly journals Development of a Novel Cysteine Sulfinic Acid Decarboxylase Knockout Mouse: Dietary Taurine Reduces Neonatal Mortality

2014 ◽  
Vol 2014 ◽  
pp. 1-12 ◽  
Author(s):  
Eunkyue Park ◽  
Seung Yong Park ◽  
Carl Dobkin ◽  
Georgia Schuller-Levis
Keyword(s):  
Knockout Mouse ◽  
Prolactin Receptor ◽  
Survival Rates ◽  
Acid Decarboxylase ◽  
Sulfinic Acid ◽  
Taurine Supplementation ◽  
Cysteine Sulfinic Acid ◽  
Taurine Concentration ◽  
Taurine Deficiency ◽  
Cysteine Sulfinic Acid Decarboxylase

We engineered a CSAD KO mouse to investigate the physiological roles of taurine. The disruption of the CSAD gene was verified by Southern, Northern, and Western blotting. HPLC indicated an 83% decrease of taurine concentration in the plasma of CSAD-/-. Although CSAD-/- generation (G)1 and G2 survived, offspring from G2 CSAD-/- had low brain and liver taurine concentrations and most died within 24 hrs of birth. Taurine concentrations in G3 CSAD-/- born from G2 CSAD-/- treated with taurine in the drinking water were restored and survival rates of G3 CSAD-/- increased from 15% to 92%. The mRNA expression of CDO, ADO, and TauT was not different in CSAD-/- compared to WT and CSAD mRNA was not expressed in CSAD-/-. Expression of Gpx 1 and 3 was increased significantly in CSAD-/- and restored to normal levels with taurine supplementation. Lactoferrin and the prolactin receptor were significantly decreased in CSAD-/-. The prolactin receptor was restored with taurine supplementation. These data indicated that CSAD KO is a good model for studying the effects of taurine deficiency and its treatment with taurine supplementation.

scholarly journals Analysis of Antibody Reactivity against Cysteine Sulfinic Acid Decarboxylase, A Pyridoxal Phosphate-Dependent Enzyme, in Endocrine Autoimmune Disease

2004 ◽  
Vol 89 (4) ◽  
pp. 1636-1640 ◽  
Author(s):  
Filip Sköldberg ◽  
Fredrik Rorsman ◽  
Jaakko Perheentupa ◽  
Mona Landin-Olsson ◽  
Eystein S. Husebye ◽  
...  
Keyword(s):  
Amino Acid ◽  
Autoimmune Disease ◽  
Pyridoxal Phosphate ◽  
Acid Decarboxylase ◽  
Endocrine Disorders ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Gad 65 ◽  
Cysteine Sulfinic Acid Decarboxylase ◽  
Group Ii

Abstract The structurally related group II pyridoxal phosphate (PLP)-dependent amino acid decarboxylases glutamic acid decarboxylase (GAD), aromatic l-amino acid decarboxylase (AADC), and histidine decarboxylase (HDC) are known autoantigens in endocrine disorders. We report, for the first time, the prevalence of serum autoantibody reactivity against cysteine sulfinic acid decarboxylase (CSAD), an enzyme that shares 50% amino acid identity with the 65- and 67-kDa isoforms of GAD (GAD-65 and GAD-67), in endocrine autoimmune disease. Three of 83 patients (3.6%) with autoimmune polyendocrine syndrome type 1 (APS1) were anti-CSAD positive in a radioimmunoprecipitation assay. Anti-CSAD antibodies cross-reacted with GAD-65, and the anti-CSAD-positive sera were also reactive with AADC and HDC. The low frequency of anti-CSAD reactivity is in striking contrast to the prevalence of antibodies against GAD-65, AADC, and HDC in APS1 patients, suggesting that different mechanisms control the immunological tolerance toward CSAD and the other group II decarboxylases. Moreover, CSAD may be a useful mold for the construction of recombinant chimerical antigens in attempts to map conformational epitopes on other group II PLP-dependent amino acid decarboxylases.

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