BIOMAT Database Logo BIOMAT Database Logo

Changes in mRNA expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol 7 alpha-hydroxylase in chickens. 2003

Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
Animal Nutrition, Division of Life Sciences, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan. kan@bios.tohoku.ac.jp

3-Hydroxy-3-methylglutaryl coenzyme A reductase (HMGR) and cholesterol 7 alpha-hydroxylase (CYP7A1), essential enzymes of cholesterol synthesis and excretion, respectively, were isolated from a chicken liver cDNA library. When their recombinant proteins were overexpressed in HNK293 cells, corresponding enzyme activities were observed. The complete open reading frames of MHGR and CYP7A1 contained (i) 2625 base pairs (bp), predicting a protein of 875 amino acids, and (ii) 1539 bp, predicting a protein of 513 amino acids, respectively. By Northern blot analysis, chicken HMGR mRNA expression was detected in most tissues examined, however, the highest levels were found in liver, brain and ileum. CYP7A1 mRNA was detected only in the liver. Changes in chicken HMGR and CYP7A1 mRNA expression with nutritional state were examined and were shown to respond to certain nutritional treatments, i.e. fast refeeding and cholesterol supplementation. HMGR and CYP7A1 mRNA levels were significantly increased with maturation (i.e. egg producing), when compared to immature chickens. However, these stimulations were not associated with estrogen, although this does enhance triacylglycerol and very low density lipoprotein secretion by the chicken liver. The present study is the first to report the molecular characterization of HMGR and CYP7A1, key enzymes of cholesterol metabolism in avian species.

UI MeSH Term Description Entries
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009928 Organ Specificity Characteristic restricted to a particular organ of the body, such as a cell type, metabolic response or expression of a particular protein or antigen. Tissue Specificity,Organ Specificities,Specificities, Organ,Specificities, Tissue,Specificity, Organ,Specificity, Tissue,Tissue Specificities
D002645 Chickens Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA. Gallus gallus,Gallus domesticus,Gallus gallus domesticus,Chicken
D002784 Cholesterol The principal sterol of all higher animals, distributed in body tissues, especially the brain and spinal cord, and in animal fats and oils. Epicholesterol
D002790 Cholesterol 7-alpha-Hydroxylase A membrane-bound cytochrome P450 enzyme that catalyzes the 7-alpha-hydroxylation of CHOLESTEROL in the presence of molecular oxygen and NADPH-FERRIHEMOPROTEIN REDUCTASE. This enzyme, encoded by CYP7, converts cholesterol to 7-alpha-hydroxycholesterol which is the first and rate-limiting step in the synthesis of BILE ACIDS. CYP7,CYP7A,Cytochrome P-450 CYP7,CYP 7,CYP 7A,Cholesterol 7-alpha-Monooxygenase,Cholesterol 7alpha-Hydroxylase,Cholesterol-7-Hydroxylase,Cytochrome P450 7,Cholesterol 7 Hydroxylase,Cholesterol 7 alpha Hydroxylase,Cholesterol 7 alpha Monooxygenase,Cholesterol 7alpha Hydroxylase,Cytochrome P 450 CYP7
D004958 Estradiol The 17-beta-isomer of estradiol, an aromatized C18 steroid with hydroxyl group at 3-beta- and 17-beta-position. Estradiol-17-beta is the most potent form of mammalian estrogenic steroids. 17 beta-Estradiol,Estradiol-17 beta,Oestradiol,17 beta-Oestradiol,Aerodiol,Delestrogen,Estrace,Estraderm TTS,Estradiol Anhydrous,Estradiol Hemihydrate,Estradiol Hemihydrate, (17 alpha)-Isomer,Estradiol Monohydrate,Estradiol Valerate,Estradiol Valeriante,Estradiol, (+-)-Isomer,Estradiol, (-)-Isomer,Estradiol, (16 alpha,17 alpha)-Isomer,Estradiol, (16 alpha,17 beta)-Isomer,Estradiol, (17-alpha)-Isomer,Estradiol, (8 alpha,17 beta)-(+-)-Isomer,Estradiol, (8 alpha,17 beta)-Isomer,Estradiol, (9 beta,17 alpha)-Isomer,Estradiol, (9 beta,17 beta)-Isomer,Estradiol, Monosodium Salt,Estradiol, Sodium Salt,Estradiol-17 alpha,Estradiol-17beta,Ovocyclin,Progynon-Depot,Progynova,Vivelle,17 beta Estradiol,17 beta Oestradiol,Estradiol 17 alpha,Estradiol 17 beta,Estradiol 17beta,Progynon Depot
D005260 Female Females
D006903 Hydroxymethylglutaryl CoA Reductases Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID. HMG CoA Reductases,3-Hydroxy-3-methylglutaryl CoA Reductase,HMG CoA Reductase,Hydroxymethylglutaryl CoA Reductase,3 Hydroxy 3 methylglutaryl CoA Reductase,CoA Reductase, 3-Hydroxy-3-methylglutaryl,Reductase, 3-Hydroxy-3-methylglutaryl CoA

Related Publications

Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
Hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase activity and cholesterol 7 alpha-hydroxylase activity in neonatal guinea pig.
July 1979, Steroids,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
Post-transcriptional regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol 7 alpha-hydroxylase in rats with subtotal nephrectomy.
August 1994, Kidney international,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
Development of hepatic microsomal activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase and cholesterol 7 alpha-hydroxylase in the young chick.
October 1992, Comparative biochemistry and physiology. Comparative physiology,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
Cholesterol regulation of hepatic 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
June 1972, The Biochemical journal,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
The submicrosomal localization of 3-hydroxy-3-methylglutaryl-coenzyme-A reductase, cholesterol 7alpha-hydroxylase and cholesterol in rat liver.
January 1978, European journal of biochemistry,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
In vivo and in vitro studies on the regulatory link between 3-hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol 7 alpha-hydroxylase in rat liver.
January 1999, Zeitschrift fur Naturforschung. C, Journal of biosciences,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
Phosphorylation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by microsomal 3-hydroxy-3-methylglutaryl coenzyme A reductase kinase.
April 1984, Archives of biochemistry and biophysics,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
Structure and expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase.
January 1986, Annals of the New York Academy of Sciences,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
3-hydroxy-3-methylglutaryl-coenzyme A reductase mRNA in Alzheimer and control brain.
September 2001, Neuroreport,
Kan Sato, and Aya Ohuchi, and Seol Hyang Sook, and Masaaki Toyomizu, and Yukio Akiba
Regulation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and cholesterol synthesis.
May 1971, The Journal of biological chemistry,
Copied contents to your clipboard!