» Articles » PMID: 8573067

Relationship of Human Liver Dihydrodiol Dehydrogenases to Hepatic Bile-acid-binding Protein and an Oxidoreductase of Human Colon Cells

Overview
Journal Biochem J
Specialty Biochemistry
Date 1996 Jan 15
PMID 8573067
Citations 27
Authors
Affiliations
Soon will be listed here.
Abstract

We previously isolated three monomeric dihydrodiol dehydrogenases, DD1, DD2 and DD4, from human liver, and cloned a cDNA (C9) thought to encode DD2, which is identical with those for human bile-acid-binding protein and an oxidoreductase of human colon carcinoma HT29 cells. In the present study we have provided evidence that the C9 cDNA clone encodes DD1, not DD2. A recombinant enzyme expressed from the cDNA in a bacterial system was purified, and its catalytic properties, bile-acid-binding ability and primary sequence were compared with those of the hepatic dihydrodiol dehydrogenases. The results show that DD1 encoded by C9 possesses prostaglandin F synthase activity but low affinity for lithocholic acid, whereas DD2, showing differences of six amino acid residues from the DD1 sequence, exhibited high-affinity binding for the bile acid. Refined relationship between dihydrodiol dehydrogenases and their related proteins of human tissues is proposed.

Citing Articles

Long read sequencing characterises a novel structural variant, revealing underactive AKR1C1 with overactive AKR1C2 as a possible cause of severe chronic fatigue.

Oakley J, Hill M, Giess A, Tanguy M, Elgar G J Transl Med. 2023; 21(1):825.

PMID: 37978513 PMC: 10655400. DOI: 10.1186/s12967-023-04711-5.


Genomic adaptations to cereal-based diets contribute to mitigate metabolic risk in some human populations of East Asian ancestry.

Landini A, Yu S, Gnecchi-Ruscone G, Abondio P, Ojeda-Granados C, Sarno S Evol Appl. 2021; 14(2):297-313.

PMID: 33664777 PMC: 7896717. DOI: 10.1111/eva.13090.


The SIRT2-mediated deacetylation of AKR1C1 is required for suppressing its pro-metastasis function in Non-Small Cell Lung Cancer.

Zhu H, Hu Y, Zeng C, Chang L, Ge F, Wang W Theranostics. 2020; 10(5):2188-2200.

PMID: 32104503 PMC: 7019158. DOI: 10.7150/thno.39151.


Role of Human Aldo-Keto Reductases in the Metabolic Activation of the Carcinogenic Air Pollutant 3-Nitrobenzanthrone.

Murray J, Mesaros C, Arlt V, Seidel A, Blair I, Penning T Chem Res Toxicol. 2018; 31(11):1277-1288.

PMID: 30406992 PMC: 6319660. DOI: 10.1021/acs.chemrestox.8b00250.


Structural and Functional Biology of Aldo-Keto Reductase Steroid-Transforming Enzymes.

Penning T, Wangtrakuldee P, Auchus R Endocr Rev. 2018; 40(2):447-475.

PMID: 30137266 PMC: 6405412. DOI: 10.1210/er.2018-00089.


References
1.
Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

2.
Bohren K, Bullock B, Wermuth B, GABBAY K . The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem. 1989; 264(16):9547-51. View

3.
Hara A, Deyashiki Y, Nakagawa M, Nakayama T, Sawada H . Isolation of proteins with carbonyl reductase activity and prostaglandin-9-ketoreductase activity from chicken kidney. J Biochem. 1982; 92(6):1753-62. DOI: 10.1093/oxfordjournals.jbchem.a134105. View

4.
Sugiyama Y, Stolz A, Sugimoto M, Kaplowitz N . Evidence for a common high affinity binding site on glutathione S-transferase B for lithocholic acid and bilirubin. J Lipid Res. 1984; 25(11):1177-83. View

5.
Winters C, Molowa D, Guzelian P . Isolation and characterization of cloned cDNAs encoding human liver chlordecone reductase. Biochemistry. 1990; 29(4):1080-7. DOI: 10.1021/bi00456a034. View