Inactivation of cystathionase and of cysteine sulfinic acid decarboxylase by proteolytic enzymes: Effect of pyridoxal phosphate

1970 ◽  
Vol 26 (6) ◽  
pp. 602-604 ◽  
Author(s):  
Fernande Chatagner ◽  
Yveline Gicquel ◽  
Christiane Portemer ◽  
Michèle Tixier
Keyword(s):  
Pyridoxal Phosphate ◽  
Proteolytic Enzymes ◽  
Acid Decarboxylase ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Cysteine Sulfinic Acid Decarboxylase

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.

Cloning and characterization of rat cysteine sulfinic acid decarboxylase

1995 ◽  
Vol 1262 (1) ◽  
pp. 79-82 ◽  
Author(s):  
Pamela J. Kaisakia ◽  
Ann A. Jerkins ◽  
David C. Goodspeed ◽  
Robert D. Steele
Keyword(s):  
Acid Decarboxylase ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Cysteine Sulfinic Acid Decarboxylase

Cloning of murine cysteine sulfinic acid decarboxylase and its mRNA expression in murine tissues

2002 ◽  
Vol 1574 (3) ◽  
pp. 403-406 ◽  
Author(s):  
Eunkyue Park ◽  
Seung Yong Park ◽  
Chuanhua Wang ◽  
Jiliu Xu ◽  
Giuseppe LaFauci ◽  
...  
Keyword(s):  
Mrna Expression ◽  
Acid Decarboxylase ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Cysteine Sulfinic Acid Decarboxylase

Dietary sulfur amino acid modulation of cysteine sulfinic acid decarboxylase

1991 ◽  
Vol 261 (5) ◽  
pp. E551-E555 ◽  
Author(s):  
A. A. Jerkins ◽  
R. D. Steele
Keyword(s):  
Amino Acid ◽  
Basal Diet ◽  
Male Rats ◽  
Acid Decarboxylase ◽  
Dependent Manner ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Immunochemical Detection ◽  
Significant Depression ◽  
Cysteine Sulfinic Acid Decarboxylase

Male rats were fed sulfur and nonsulfur amino acid-supplemented diets, and the response of cysteine sulfinic acid decarboxylase (CSAD) activity was determined. After adaptation to a casein-based basal diet, rats were fed diets containing additions of L-methionine. Hepatic CSAD activity decreased in a dose-dependent manner. Significant depression of CSAD activity in liver was evident within 24 h of feeding rats a methionine-supplemented diet. Depression of enzyme activity was reversed upon refeeding the basal diet. After rats were fed diets supplemented with methionine, cystine, homocystine, S-methyl-L-cysteine, phenylalanine, leucine, or ethionine for 14 days, hepatic CSAD activity in rats fed S-methyl-L-cysteine-, phenylalanine-, or leucine-supplemented diets was not depressed compared with activity in rats fed a basal diet. In contrast, CSAD activity in livers of rats fed cystine-, homocystine-, methionine-, or ethionine-supplemented diets was 60, 40, 40, and 8%, respectively, of the activity in livers from control rats. Immunochemical detection and quantification of CSAD protein in rat liver indicated that CSAD protein concentration was correlated to CSAD activity. CSAD activity may be specifically regulated by sulfur amino acids metabolized by the S-adenosylmethionine-dependent pathway of methionine metabolism.

Estradiol decreases taurine level by reducing cysteine sulfinic acid decarboxylase via the estrogen receptor-α in female mice liver

2015 ◽  
Vol 308 (4) ◽  
pp. G277-G286 ◽  
Author(s):  
Qiwang Ma ◽  
Jianjun Zhao ◽  
Wei Cao ◽  
Jiali Liu ◽  
Sheng Cui
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Acid Decarboxylase ◽  
Sulfinic Acid ◽  
Cysteine Sulfinic Acid ◽  
Female Mice ◽  
Ovariectomized Mice ◽  
Taurine Level ◽  
Cysteine Sulfinic Acid Decarboxylase ◽  
Mice Liver

Cysteine sulfinic acid decarboxylase (CSAD) and cysteine dioxygenase (CDO) are two rate-limiting enzymes in taurine de novo synthesis, and their expressions are associated with estrogen concentration. The present study was designed to determine the relationship between 17β-estradiol (E2) and taurine in female mice liver. We initially observed the mice had lower levels of CSAD, CDO, and taurine during estrus than diestrus. We then, respectively, treated the ovariectomized mice, the cultured hepatocytes, and Hep G2 cells with different doses of E2, and the CSAD and CDO expressions and taurine levels were analyzed. The results showed that E2 decreased taurine level in the serum and the cultured cells by inhibiting CSAD and CDO expressions. Furthermore, we identified the molecular receptor types through which E2 plays its role in regulating taurine synthesis, and our results showed that estrogen receptor-α (ERα) expression was much higher than estrogen receptor-β (ERβ) in the liver and hepatocytes, and the inhibiting effects of E2 on CSAD, CDO, and taurine level were partially abrogated in the ICI-182,780-pretreated liver and hepatocytes, and in ERα knockout mice. These results indicate that estradiol decreases taurine content by reducing taurine biosynthetic enzyme expression in mice liver.

Sign in / Sign up

Export Citation Format

Share Document