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164Ile allele in the beta2-Adrenergic receptor gene is associated with risk of elevated blood pressure in women. The Copenhagen City Heart Study.

https://arctichealth.org/en/permalink/ahliterature173671
Source
Pharmacogenet Genomics. 2005 Sep;15(9):633-45
Publication Type
Article
Date
Sep-2005
Author
Amar A Sethi
Anne Tybjaerg-Hansen
Gorm B Jensen
Børge G Nordestgaard
Author Affiliation
Department of Clinical Biochemistry, Herlev University Hospital, Herlev, Denmark.
Source
Pharmacogenet Genomics. 2005 Sep;15(9):633-45
Date
Sep-2005
Language
English
Publication Type
Article
Keywords
Alleles
Arginine - chemistry
Blood pressure
Body mass index
Denmark
Female
Gene Expression Regulation
Gene Frequency
Genetic Variation
Genotype
Glutamic Acid - chemistry
Glutamine - chemistry
Glycine - chemistry
Haplotypes
Heart rate
Heterozygote
Humans
Hypertension - genetics
Isoleucine - chemistry
Linkage Disequilibrium
Male
Receptors, Adrenergic, beta-2 - genetics
Risk
Risk factors
Sequence Analysis, DNA
Sex Factors
Time Factors
Abstract
Since beta2-adrenergic receptors are important regulators of blood pressure, genetic variation in this receptor could explain risk of elevated blood pressure in selected individuals. We tested the hypothesis that Gly16Arg, Gln27Glu, and Thr164Ile in the beta2-adrenergic receptor gene associated with elevated blood pressure.
We genotyped 9185 individuals from the adult Danish general population.
Allele frequencies of 16Arg, 27Glu, and 164Ile were 0.38, 0.44, and 0.01, respectively. Among women never treated with antihypertensive medication those heterozygous for Thr164Ile versus non-carriers had increased diastolic blood pressure (P=0.02). Women heterozygous for Thr164Ile versus non-carriers had an odds ratio for elevated blood pressure of 1.93 (95% CI: 1.30-2.86). Finally, women double heterozygous for Thr164Ile and Gln27Glu or Gly16Arg versus non-carriers at all 3 loci had an odds ratio for elevated blood pressure of 2.49 (1.28-4.85) or 3.19 (1.46-6.97). In men, blood pressure was not influenced by this genetic variation.
In women Thr164Ile heterozygosity is associated with increased diastolic blood pressure, and represent a risk factor for elevated blood pressure in women in the general population. This was most pronounced in those women also heterozygous for Gln27Glu or Gly16Arg.
PubMed ID
16041242 View in PubMed
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The basis of prostaglandin synthesis in coral: molecular cloning and expression of a cyclooxygenase from the Arctic soft coral Gersemia fruticosa.

https://arctichealth.org/en/permalink/ahliterature3964
Source
J Biol Chem. 2001 Mar 9;276(10):7033-40
Publication Type
Article
Date
Mar-9-2001
Author
R. Koljak
I. Järving
R. Kurg
W E Boeglin
K. Varvas
K. Valmsen
M. Ustav
A R Brash
N. Samel
Author Affiliation
Department of Bioorganic Chemistry, Institute of Chemistry, Tallinn Technical University, Akadeemia tee 15, Tallinn 12618, Estonia.
Source
J Biol Chem. 2001 Mar 9;276(10):7033-40
Date
Mar-9-2001
Language
English
Publication Type
Article
Keywords
Alanine - chemistry
Amino Acid Sequence
Animals
Arginine - chemistry
Blotting, Northern
COS Cells
Chromatography, Thin Layer
Cloning, Molecular
Cnidaria - metabolism
Cyclooxygenase 1
Cyclooxygenase 2
DNA, Complementary - metabolism
Hela Cells
Histidine - chemistry
Humans
Isoenzymes - chemistry
Isoleucine - chemistry
Membrane Proteins
Microscopy, Fluorescence
Models, Genetic
Molecular Sequence Data
Phylogeny
Plasmids - metabolism
Polymerase Chain Reaction
Prostaglandin-Endoperoxide Synthases - biosynthesis - chemistry - genetics
Prostaglandins - biosynthesis
Protein Binding
RNA, Messenger - metabolism
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.
Sequence Analysis, DNA
Sequence Homology, Amino Acid
Serine - chemistry
Tyrosine - chemistry
Abstract
In vertebrates, the synthesis of prostaglandin hormones is catalyzed by cyclooxygenase (COX)-1, a constitutively expressed enzyme with physiological functions, and COX-2, induced in inflammation and cancer. Prostaglandins have been detected in high concentrations in certain corals, and previous evidence suggested their biosynthesis through a lipoxygenase-allene oxide pathway. Here we describe the discovery of an ancestor of cyclooxygenases that is responsible for prostaglandin biosynthesis in coral. Using a homology-based polymerase chain reaction cloning strategy, the cDNA encoding a polypeptide with approximately 50% amino acid identity to both mammalian COX-1 and COX-2 was cloned and sequenced from the Arctic soft coral Gersemia fruticosa. Nearly all the amino acids essential for substrate binding and catalysis as determined in the mammalian enzymes are represented in coral COX: the arachidonate-binding Arg(120) and Tyr(355) are present, as are the heme-coordinating His(207) and His(388); the catalytic Tyr(385); and the target of aspirin attack, Ser(530). A key amino acid that determines the sensitivity to selective COX-2 inhibitors (Ile(523) in COX-1 and Val(523) in COX-2) is present in coral COX as isoleucine. The conserved Glu(524), implicated in the binding of certain COX inhibitors, is represented as alanine. Expression of the G. fruticosa cDNA afforded a functional cyclooxygenase that converted exogenous arachidonic acid to prostaglandins. The biosynthesis was inhibited by indomethacin, whereas the selective COX-2 inhibitor nimesulide was ineffective. We conclude that the cyclooxygenase occurs widely in the animal kingdom and that vertebrate COX-1 and COX-2 are evolutionary derivatives of the invertebrate precursor.
PubMed ID
11085996 View in PubMed
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Relationship between glutathione S-transferase P1 polymorphism and bronchial asthma and atopic dermatitis.

https://arctichealth.org/en/permalink/ahliterature15226
Source
Bull Exp Biol Med. 2003 Jul;136(1):73-5
Publication Type
Article
Date
Jul-2003
Author
O G Safronova
V A Vavilin
A A Lyapunova
S I Makarova
V V Lyakhovich
L F Kaznacheeva
N A Manankin
O A Batychko
S M Gavalov
Author Affiliation
Institute of Molecular Biology and Biophysics, Siberian Division of the Russian Academy of Medical Sciences, Novosibirsk. drugsmet@.cyber.ma.nsc.ru
Source
Bull Exp Biol Med. 2003 Jul;136(1):73-5
Date
Jul-2003
Language
English
Publication Type
Article
Keywords
Alleles
Asthma - genetics
Child
Dermatitis, Atopic - genetics
Female
Genotype
Glutathione Transferase - genetics
Homozygote
Humans
Isoleucine - chemistry
Male
Odds Ratio
Polymorphism, Genetic
Risk
Russia
Valine - chemistry
Xenobiotics - pharmacology
Abstract
We determined the prevalence of GSTP1-Ile105 and GSTP1-Val105 alleles in patients with bronchial asthma and atopic dermatitis and healthy children of 2 groups (randomized and nonatopic control). The GSTP1-Ile105/Val105 genotype determines the resistance to atopic dermatitis (odds ratio=0.51; 95% confidence interval: 0.28-0.92; p=0.023). However, both homozygotes are at high risk of developing atopic dermatitis (near-significant differences).
PubMed ID
14534616 View in PubMed
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Substitution of Ile-172 to Asn in the steroid 21-hydroxylase B (P450c21B) gene in a Finnish patient with the simple virilizing form of congenital adrenal hyperplasia.

https://arctichealth.org/en/permalink/ahliterature225595
Source
Hum Genet. 1991 Oct;87(6):716-20
Publication Type
Article
Date
Oct-1991
Author
J. Partanen
R D Campbell
Author Affiliation
Department of Biochemistry, University of Oxford, UK.
Source
Hum Genet. 1991 Oct;87(6):716-20
Date
Oct-1991
Language
English
Publication Type
Article
Keywords
Adrenal Hyperplasia, Congenital - enzymology - genetics
Asparagine - chemistry
Base Sequence
Child
Cloning, Molecular
DNA
Finland
Humans
Isoleucine - chemistry
Male
Molecular Sequence Data
Mutation
Polymerase Chain Reaction
Steroid 21-Hydroxylase - chemistry - genetics
Abstract
The steroid 21-hydroxylase enzyme (P450c21) is a member of the cytochrome P450 gene superfamily and is essential in the synthesis of cortisol and aldosterone. Defects in the P450c21B gene cause congenital adrenal hyperplasia (CAH), a common genetic disorder leading to virilization of newborn females. To avoid the standard cloning of mutant P450c21 genes from genomic libraries, we amplified the full-length genomic P450c21 genes by polymerase chain reaction (PCR). The amplification was followed by cloning and sequencing of a defective P450c21B gene. The strategy described here is generally applicable, thus making a simple characterization of the complete P450c21B gene possible. The method was tested in one patient suffering from the simple virilizing form of CAH. The sequence of three independent clones originating from the defective P450c21B showed that Ile at position 172 in exon 4 was substituted by Asn. The identical mutation also has been found in other patients with CAH.
PubMed ID
1937474 View in PubMed
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