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A functional polymorphism in the monoamine oxidase A gene promoter

Sue Z. Sabol, +2 more
- 01 Sep 1998 - 
- Vol. 103, Iss: 3, pp 273-279
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TLDR
A new polymorphism upstream of the gene for monoamine oxidase A, which consists of a 30-bp repeated sequence present in 3, 3.5, 4, or 5 copies, may be useful as both a functional and an anonymous genetic marker for MAOA.
Abstract
We describe a new polymorphism upstream of the gene for monoamine oxidase A (MAOA), an important enzyme in human physiology and behavior. The polymorphism, which is located 1.2 kb upstream of the MAOA coding sequences, consists of a 30-bp repeated sequence present in 3, 3.5, 4, or 5 copies. The polymorphism is in linkage disequilibrium with other MAOA and MAOB gene markers and displays significant variations in allele frequencies across ethnic groups. The polymorphism has been shown to affect the transcriptional activity of the MAOA gene promoter by gene fusion and transfection experiments involving three different cell types. Alleles with 3.5 or 4 copies of the repeat sequence are transcribed 2–10 times more efficiently than those with 3 or 5 copies of the repeat, suggesting an optimal length for the regulatory region. This promoter region polymorphism may be useful as both a functional and an anonymous genetic marker for MAOA.

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Citations
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References
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Journal ArticleDOI

Assignment of genes for human monoamine oxidases A and B to the X chromosome.

TL;DR: Monoclonal antibodies that immunoprecipitate human monoamine oxidase (MAO) A or human MAO B, but not the corresponding mouse enzymes, were used to assay for the presence of immunopRecipitable MAO A orMAO B in mouse‐human hybrid somatic cell lines containing small numbers of human chromosomes.
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Evidence for a genetic association between alleles of monoamine oxidase a gene and bipolar affective disorder

TL;DR: Evidence of a genetic association between bipolar disorder and alleles at 3 monoamine oxidase A (MAOA) markers, but not with alleles of a monoamines oxidase B (MAOB) polymorphism is presented.
Journal ArticleDOI

Differences in the structure of A and B forms of human monoamine oxidase.

TL;DR: Findings indicate that distinct enzyme molecules are associated with the A and B types of human MAO activity.
Journal ArticleDOI

Properties of monoamine oxidase (MAO) in human blood platelets, plasma, lymphocytes and granulocytes

TL;DR: The properties of monoamine oxidase in plasma, platelets, lymphocytes and granulocytes have been studied using cells prepared from a single small sample of blood and the three substrates, 5-hydroxytryptamine, tyramine and benzylamine, have been used to obtain a more complete picture of blood monoamines oxidase than was previously possible.
Journal ArticleDOI

Characterization of a highly polymorphic region near the first exon of the human MAOA gene containing a GT dinucleotide and a novel VNTR motif.

TL;DR: The characterization of a highly informative polymorphic region within a 2.9-kb cloned fragment containing the first exon of the MAOA gene, which consists of a GT microsatellite directly adjacent to an imperfectly duplicated novel 23-bp VNTR motif.
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