Sandbox Reserved 163

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	{{Sandbox_Reserved_Irma_Santoro_7}}		{{Sandbox_Reserved_Irma_Santoro_7}}
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-	<Structure load='C:\Users\Jenn\Desktop\Animated 3dax.gif' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />	+	<Structure load='get_data.cgi.gif' size='400' frame='true' align='right' caption='Aromatase Cytochrome P450, 3dax' scene='Insert optional scene name here' />
		+
		+	== Background ==
		+	Aromatase cytochrome P450, Cholesterol 7-alpha-monooxygenase, is protein that plays a vital part in the regulation the ovarian sex cycle and other reproductive functions through the production of estrogen from androgens. <ref name="Simpson">Simpson ER et al, "Aromatase cytochrome P450, the enzyme responsible for estrogen biosynthesis." Endocrine Review, 1994, 342</ref>. As a member of the Cytochrome P450 family, this protein is classified as monooxygenases. Members of this family act throughout the body to both catalyze and synthesize a multitude of reactions.
		+
		+	==Structure==
		+	Aromatase is located on chromosome 15q21.1 in humans and has two ligands. The first is Protopophyrin IX containing iron and the second is an unknown atom or molecule. [[Image:3dax pic| 200 px|left]]
		+
		+
		+	==
		+
		+	This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases that catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, and other lipids. This protein localizes to the endoplasmic reticulum and catalyzes the last steps of estrogen biosynthesis from androgens. These steps include three successive hydroxylations of the 19-methyl group of androgens followed by simultaneous elimination of the methyl group as formate and aromatization of the A-ring. Mutations in this gene can result in either increased or decreased aromatase activity; the associated phenotypes suggest that estrogen functions both as a sex steroid hormone and in growth or differentiation.
		+
		+	This synthesis occurs in various tissues through tissue-specific regulatory factors. The regulation of aromatase is tissue-specific and acts through suppression and inductive processes. In the majority of tissues, aromatase is activated by cAMP or factors that use cAMP as a secondary messenger. In adipose tissues aromatase is induced by dexamethasone and phorbol ester which is suppressed by TGFß.
		+
		+	aromatase through tissue-specific regulatory factorsIL-6 is produced by various types of lymphoid and non-lymphoid cells, such as T cells, B cells, monocytes, fibroblasts, kerationcytes, endothelial cells, mesangium cells, and several tumor cells <ref>Kishimoto, T. "The Biology of Interleukin 6." Am J Hematol, Jul, 1989, 74(1), 1-10.</ref>.

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Current revision

This Sandbox is Reserved from March 9, 2011, through May 30, 2011 for use by the course Biochemistry at Reinhardt University, Waleska, USA, taught by Irma Santoro. This reservation includes Sandbox Reserved 162 through Sandbox Reserved 168.

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spinqualitylabelsall models Aromatase Cytochrome P450, 3dax Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Background

Aromatase cytochrome P450, Cholesterol 7-alpha-monooxygenase, is protein that plays a vital part in the regulation the ovarian sex cycle and other reproductive functions through the production of estrogen from androgens. ^[1]. As a member of the Cytochrome P450 family, this protein is classified as monooxygenases. Members of this family act throughout the body to both catalyze and synthesize a multitude of reactions.

Structure

Aromatase is located on chromosome 15q21.1 in humans and has two ligands. The first is Protopophyrin IX containing iron and the second is an unknown atom or molecule.

==

This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases that catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, and other lipids. This protein localizes to the endoplasmic reticulum and catalyzes the last steps of estrogen biosynthesis from androgens. These steps include three successive hydroxylations of the 19-methyl group of androgens followed by simultaneous elimination of the methyl group as formate and aromatization of the A-ring. Mutations in this gene can result in either increased or decreased aromatase activity; the associated phenotypes suggest that estrogen functions both as a sex steroid hormone and in growth or differentiation.

This synthesis occurs in various tissues through tissue-specific regulatory factors. The regulation of aromatase is tissue-specific and acts through suppression and inductive processes. In the majority of tissues, aromatase is activated by cAMP or factors that use cAMP as a secondary messenger. In adipose tissues aromatase is induced by dexamethasone and phorbol ester which is suppressed by TGFß.

aromatase through tissue-specific regulatory factorsIL-6 is produced by various types of lymphoid and non-lymphoid cells, such as T cells, B cells, monocytes, fibroblasts, kerationcytes, endothelial cells, mesangium cells, and several tumor cells ^[2].