https://www.ncbi.nlm.nih.gov/pubmed/30131986
Food Funct. 2018 Sep 19;9(9):4814-4821. doi: 10.1039/c8fo00740c.
The intervention effect of licorice in d-galactose induced aging rats by regulating the taurine metabolic pathway.Abstract
Licorice,
an edible and officinal plant material, has attracted considerable
attention for its wide range of pharmacological activities. Our previous
study showed that licorice can ameliorate cognitive damage and improve
oxidative stress and apoptosis in aging rats induced by d-galactose
(d-gal). In this study, in order to further explore the changes of the
metabolic profile during the aging process and the antiaging mechanism
of licorice, the 1H NMR-based metabolomics approach was used to analyze
serum and urine samples and identify a potential biomarker in d-gal
induced aging rats.
The results revealed that the taurine metabolic pathway was significantly correlated with the ageing process in d-gal induced rats. Furthermore, the taurine contents were significantly decreased in both the serum and urine samples of aging rats compared with the controls. At the same time, the levels of
The results revealed that the taurine metabolic pathway was significantly correlated with the ageing process in d-gal induced rats. Furthermore, the taurine contents were significantly decreased in both the serum and urine samples of aging rats compared with the controls. At the same time, the levels of
- cysteine dioxygenase type I (CDO1),
- cysteine sulfinic acid decarboxylase (CSAD) and
- glutamate decarboxylase type I (GAD1),
After licorice administration, the levels of taurine, CDO1 and CSAD were all significantly increased. These findings firstly demonstrated that the regulation of the taurine metabolic pathway is involved in the anti-aging effect of licorice in d-gal induced aging rats.
PMID: 30131986 DOI: 10.1039/c8fo00740c
[Indexed for MEDLINE]
Official
Symbol CSAD
Official
Full Name cysteine sulfinic acid decarboxylase
Gene type protein coding
Also known as CSD; PCAP
Summary: This gene encodes a member of the group 2 decarboxylase
family. A similar protein in rodents plays a role in multiple biological
processes as the rate-limiting enzyme in taurine biosynthesis,
catalyzing the decarboxylation of cysteinesulfinate to hypotaurine.
Alternatively spliced transcript variants encoding multiple isoforms
have been observed for this gene. [provided by RefSeq, Sep 2011] Expression Ubiquitous expression in fat (RPKM 9.9), skin (RPKM 8.5) and 25 other tissues See more Orthologs mouse
all
https://www.ncbi.nlm.nih.gov/pubmed/26327310
Abstract
Variants in the gene encoding the enzyme glutamic acid decarboxylase like 1 (GADL1) have been associated with response to lithium therapy. Both GADL1 and the related enzyme cysteine sulfinic acid decarboxylase (CSAD) have been proposed to be involved in the pyridoxal-5'-phosphate (PLP)-dependent biosynthesis of taurine.
In the present study, we compared the catalytic properties, inhibitor sensitivity and expression profiles of GADL1 and CSAD in brain tissue.
In mouse and human brain we observed distinct patterns of expression of the PLP-dependent decarboxylases CSAD, GADL1 and glutamic acid decarboxylase 67 (GAD67).
CSAD levels were highest during prenatal and early postnatal development;
GADL1 peaked early in prenatal development,
while GAD67 increased rapidly after birth.
Both CSAD and GADL1 are being expressed in neurons,
whereas only CSAD mRNA was detected in astrocytes.
Cysteine sulfinic acid was the preferred substrate for both mouse CSAD and GADL1, although both enzymes also decarboxylated cysteic acid and aspartate. In silico screening and molecular docking using the crystal structure of CSAD and in vitro assays led to the discovery of eight new enzyme inhibitors with partial selectivity for either CSAD or GADL1. Lithium had minimal effect on their enzyme activities.
In conclusion, taurine biosynthesis in vertebrates involves two structurally related PLP-dependent decarboxylases (CSAD and GADL1) that have partially overlapping catalytic properties but different tissue distribution, indicating divergent physiological roles.
Development of selective enzyme inhibitors targeting these enzymes is important to further dissect their (patho)physiological roles.
- Preferred Names
- cysteine sulfinic acid decarboxylase (CSAD)
- Names
- P-selectin cytoplasmic tail-associated protein (PCAP)
- aspartate 1-decarboxylase (ADC)
- cysteine sulfinic acid decarboxylase-related protein
- cysteine-sulfinate decarboxylase
- sulfinoalanine decarboxylase
- Cloning of murine cysteine sulfinic acid decarboxylase and its mRNA expression in murine tissues. Park E, et al. Biochim Biophys Acta, 2002 Apr 12. PMID 11997111
- Mechanism of cysteine-dependent inactivation of aspartate/glutamate/cysteine sulfinic acid α-decarboxylases. Liu P, et al. Amino Acids, 2013 Feb. PMID 22718265
- Mammalian CSAD and GADL1 have distinct biochemical properties and patterns of brain expression. Winge I, et al. Neurochem Int, 2015 Nov. PMID 26327310
- Whole genome RNAi screens reveal a critical role of REV3 in coping with replication stress. Kotov IN, et al. Mol Oncol, 2014 Dec. PMID 25113059, Free PMC Article
- Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver. Xu XR, et al. Proc Natl Acad Sci U S A, 2001 Dec 18. PMID 11752456, Free PMC Article
Abstract
Variants in the gene encoding the enzyme glutamic acid decarboxylase like 1 (GADL1) have been associated with response to lithium therapy. Both GADL1 and the related enzyme cysteine sulfinic acid decarboxylase (CSAD) have been proposed to be involved in the pyridoxal-5'-phosphate (PLP)-dependent biosynthesis of taurine.
In the present study, we compared the catalytic properties, inhibitor sensitivity and expression profiles of GADL1 and CSAD in brain tissue.
In mouse and human brain we observed distinct patterns of expression of the PLP-dependent decarboxylases CSAD, GADL1 and glutamic acid decarboxylase 67 (GAD67).
CSAD levels were highest during prenatal and early postnatal development;
GADL1 peaked early in prenatal development,
while GAD67 increased rapidly after birth.
Both CSAD and GADL1 are being expressed in neurons,
whereas only CSAD mRNA was detected in astrocytes.
Cysteine sulfinic acid was the preferred substrate for both mouse CSAD and GADL1, although both enzymes also decarboxylated cysteic acid and aspartate. In silico screening and molecular docking using the crystal structure of CSAD and in vitro assays led to the discovery of eight new enzyme inhibitors with partial selectivity for either CSAD or GADL1. Lithium had minimal effect on their enzyme activities.
In conclusion, taurine biosynthesis in vertebrates involves two structurally related PLP-dependent decarboxylases (CSAD and GADL1) that have partially overlapping catalytic properties but different tissue distribution, indicating divergent physiological roles.
Development of selective enzyme inhibitors targeting these enzymes is important to further dissect their (patho)physiological roles.
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