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�� [ catecholamine ]

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Biosynthetic pathway for catecholamines. The term catecholamine comes from the catechol (ortho-dihydroxybenzene) structure and a side chain with an amino group�the catechol nucleus(shown on left). Tyrosine is converted to 3,4-dihydroxyphenylalanine (dopa) by tyrosine hydroxylase (TH); this rate-limiting step provides the clinician with the option to treat pheochromocytoma with a TH inhibitor, �-methyl-paratyrosine (metyrosine). Aromatic L-amino acid decarboxylase (AADC) converts dopa to dopamine. Dopamine is hydroxylated to norepinephrine by dopamine �-hydroxylase (DBH). Norepinephrine is converted to epinephrine by phenylethanolamine N-methyltransferase (PNMT). Cortisol serves as a cofactor for PNMT, which explains why epinephrine-secreting neoplasms are almost exclusively localized to the adrenal medulla. 2_120, 549 (546)

��. �� . �� = Translate into Russian ��: Melmed S., Polonsky K.S., Larsen P.R., Kronenberg H.M., Eds. Williams Textbook of Endocrinology, 12th ed., Saunders, 2011, 1816 p., ��.: �� : ��. ��.

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Catecholamine metabolism. Metabolism of catecholamines occurs through two enzymatic pathways. Catechol-O-methyltransferase (COMT) converts epinephrine to metanephrine and converts norepinephrine to normetanephrine through meta-O-methylation. Metanephrine and normetanephrine are oxidized by monoamine oxidase (MAO) to vanillylmandelic acid (VMA) by oxidative deamination. MAO also may oxidize epinephrine and norepinephrine to dihydroxymandelic acid, which is then converted by COMT to VMA. Dopamine is also metabolized by MAO and COMT to the final metabolite, homovanillic acid (HVA). 2_120, 549 (546)

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��. �� (�� ) = A noradrenergic junction of the peripheral sympathetic nervous system (not to scale). �� ��: Gardner D.G., Shoback D.M., Eds. Greenspan's Basic & Clinical Endocrinology. 9th ed., Lange, 2011, 960 p., ��.: �� : ��. ��.

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Schematic diagram of a noradrenergic junction of the peripheral sympathetic nervous system (not to scale). The neural axons form synaptic junctions with cells in target organs. The neurotransmitter is norepinephrine, which originates through de novo synthesis from tyrosine or from norepinephrine that has been secreted and reabsorbed by a norepinephrine transporter (NET). Tyrosine is transported into the noradrenergic endings or varicosities by a sodium-dependent carrier (A). In the cytoplasm, tyrosine hydroxylase converts tyrosine to DOPA that is converted by DOPA decarboxylase to dopamine. Dopamine, as well as norepinephrine (NE) is transported into the vesicles by vesicular monoamine transferase (VMAT). Dopamine is converted to NE in the vesicle by dopamine--hydroxylase. Exocytosis of the neurosecretory vesicle with release of transmitter occurs when an action potential opens voltage-sensitive calcium channels and increases intracellular calcium. Fusion of vesicles with the surface membrane results in expulsion of norepinephrine, cotransmitters, and dopamine--hydroxylase. After release, norepinephrine diffuses out of the cleft or is transported into the cytoplasm of the nerve itself (uptake 1) or transported into the postjunctional target cell (uptake 2). Regulatory receptors are present on the presynaptic terminal (SNAPs, synaptosome-associated proteins; VAMPs, vesicle-associated membrane protein). Not shown: In adrenal medullary and pheochromocytoma cells, norepinephrine constantly diffuses from the vesicle into the cytoplasm where it may be converted to epinephrine by phenylethanolamine-N-methyltransferase (PNMT). Alternatively, cytoplasmic membrane-bound catecholamine-O-methyltransferase (COMT) can metabolize epinephrine and norepinephrine directly into metanephrine and normetanephrine, respectively, which are then released.

��. �� = Range of Plasma Catecholamine Levels Observed in Healthy Subjects and Patients. �� ��: Gardner D.G., Shoback D.M., Eds. Greenspan's Basic & Clinical Endocrinology. 9th ed., Lange, 2011, 960 p., ��.: �� : ��. ��.
�	�� / ��	Norepinephrine	Epinephrine
��
1	Basal	150-400 pg/mL (0.9-2.4 nmol/L)	25-100 pg/mL (0.1-0.6 nmol/L)
2	Ambulatory	200-800 pg/mL (1.2-4.8 nmol/L)	30-100 pg/mL(0.1-1 nmol/L)
3	Exercise	800-4000 pg/mL (4.8-24 nmol/L)	100-1000 pg/mL (0.5-5 nmol/L)
4	Symptomatic hypoglycemia	200-1000 pg/mL (1.2-6 nmol/L)	1000-5000 pg/mL (5-25 nmol/L)
��
5	Hypertension	200-500 pg/mL (1.2-3 nmol/L)	20-100 pg/mL (0.1-0.6 nmol/L)
6	Surgery	500-2000 pg/mL (3-12 nmol/L)	199-500 pg/mL (0.5-3 nmol/L)
7	Myocardial infarction	1000-2000 pg/mL (6-12 nmol/L)	800-5000 pg/mL (4-25 nmol/L)
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Table 11�1 Range of Plasma Catecholamine Levels Observed in Healthy Subjects and Patients.

��. �� = Range of Plasma Catecholamine Levels Observed in Healthy Subjects and Patients. �� ��: Gardner D.G., Shoback D.M., Eds. Greenspan's Basic & Clinical Endocrinology. 9th ed., Lange, 2011, 960 p., ��.: �� : ��. ��.
�	�� / ��	Norepinephrine	Epinephrine
��
1	Basal	150-400 pg/mL (0.9-2.4 nmol/L)	25-100 pg/mL (0.1-0.6 nmol/L)
2	Ambulatory	200-800 pg/mL (1.2-4.8 nmol/L)	30-100 pg/mL(0.1-1 nmol/L)
3	Exercise	800-4000 pg/mL (4.8-24 nmol/L)	100-1000 pg/mL (0.5-5 nmol/L)
4	Symptomatic hypoglycemia	200-1000 pg/mL (1.2-6 nmol/L)	1000-5000 pg/mL (5-25 nmol/L)
��
5	Hypertension	200-500 pg/mL (1.2-3 nmol/L)	20-100 pg/mL (0.1-0.6 nmol/L)
6	Surgery	500-2000 pg/mL (3-12 nmol/L)	199-500 pg/mL (0.5-3 nmol/L)
7	Myocardial infarction	1000-2000 pg/mL (6-12 nmol/L)	800-5000 pg/mL (4-25 nmol/L)
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Table 11�1 Range of Plasma Catecholamine Levels Observed in Healthy Subjects and Patients.

��. �� = Catecholamine Receptor Types and Subtypes. �� ��: Gardner D.G., Shoback D.M., Eds. Greenspan's Basic & Clinical Endocrinology. 9th ed., Lange, 2011, 960 p., ��.: �� : ��. ��.
�	Receptor	Relative Agonist	Potency Effects
��-��
1	Alpha1 Type	Norepinephrine > epinephrine
2	Alpha1A	-	↑ IP3, DAG common to all
3	Alpha1B	-	↑ IP3, DAG common to all
4	Alpha1D	-	↑ IP3, DAG common to all
5	Alpha2 Type	Norepinephrine > epinephrine; clonidine	↓ cAMP; K+ channels; Ca2+ channels
6	Alpha2A	-	-
7	Alpha2B	Norepinephrine > epinephrine	↓ cAMP; Ca2+ channels
8	Alpha2C	-	↓ cAMP
��-��
9	Beta1	Epinephrine = norepinephrine	↑ cAMP
10	Beta2	Epinephrine >>> norepinephrine	↑ cAMP
11	Beta3	Norepinephrine > epinephrine	↑ cAMP
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Table 11�2 Catecholamine Receptor Types and Subtypes. (Tables 11�2 and 11�3; Figures 11�5 and 11�6)↑ - ��,↓ - ��,> - ��,< - ��.

��. �� : �� = Catecholamine Receptors: Location and Actions. �� ��: Gardner D.G., Shoback D.M., Eds. Greenspan's Basic & Clinical Endocrinology. 9th ed., Lange, 2011, 960 p., ��.: �� : ��. ��.
�	Catecholamine Receptor	Tissue Location Action	Following Receptor Activation
��-��
1	Alpha1	Vascular smooth muscle	Increases vasoconstriction (increases blood pressure)
2	Alpha1	Liver	Increases glycogenolysis and gluconeogenesis
3	Alpha1	Eye	Increases ciliary muscle contraction (pupil dilation)
4	Alpha1	Skin	Increases pilomotor smooth muscle contraction (erects hairs)
5	Alpha1	Prostate	Increases contraction and ejaculation
6	Alpha1	Uterus	Increases gravid uterus contraction
7	Alpha1	Intestines	Increases sphincter tone and relaxes smooth muscle
8	Alpha1	Spleen capsule	Contracts spleen volume, expelling blood
9	Alpha2	Preganglionic nerves	Decreases release of neurotransmitter
10	Alpha2	Vascular smooth muscle	Increases vasoconstriction (increases blood pressure)
11	Alpha2	Pancreatic islet cells	Decreases release of insulin and glucagon
12	Alpha2	Blood platelets	Increases platelet aggregation
13	Alpha2	Adipose cells	Decreases lipolysis
14	Alpha2	Brain	Decreases norepinephrine release
��-��
15	Beta1	Myocardium	Increases force and rate of contraction
16	Beta1	Kidney (juxtaglomerular apparatus)	Increases secretion of renin
17	Beta1	Adipose cells	Increases lipolysis
18	Beta1	Most tissues	Increases calorigenesis
19	Beta2	Nerves	Increases conduction velocity
20	Beta2	Vascular smooth muscle	Decreases vasoconstriction (increases blood flow)
21	Beta2	Bronchiolar smooth muscle	Decreases contraction (bronchial dilation)
22	Beta2	Liver	Increases glycogenolysis and gluconeogenesis
23	Beta2	Intestinal smooth muscle	Decreases intestinal motility; increases sphincter tone
24	Beta2	Pancreatic islet cells	Increases release of insulin and glucagon
25	Beta2	Adipose tissue	Increases lipolysis
26	Beta2	Muscles	Increases muscle contraction speed and glycogenolysis
27	Beta2	Liver and kidney	Increases peripheral conversion of T4 to T3
28	Beta2	Uterus smooth muscle	Decreases nongravid uterine contraction (uterine relaxation)
29	Beta3	Adipose cells	Increases lipolysis
30	Beta3	Intestinal smooth muscle	Increases intestinal motility
��
31	Dopamine1	Vascular smooth muscle	Decreases vasoconstriction (vasodilation);
32	Dopamine1	Renal tubule	Enhances natriuresis
33	Dopamine2	Sympathetic nerves	Inhibits synaptic release of norepinephrine
34	Dopamine2	Pituitary lactotrophes	Inhibits prolactin release
35	Dopamine2	Gastrointestinal tract	Paracrine functions

στίξω

��. �� . �� α1-�� = Catecholamine Receptors. Activation of α1-adrenergic responses. �� ��: Gardner D.G., Shoback D.M., Eds. Greenspan's Basic & Clinical Endocrinology. 9th ed., Lange, 2011, 960 p., ��.: �� : ��. ��.

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Activation of α1-adrenergic responses. Stimulation of α1 receptors by catecholamines leads to the activation of a Gq-coupling protein. The activated αq subunit of this G protein activates phospholipase C, which catalyzes the conversion of PtdIns 4,5-P2 (phosphatidylinositol 4,5-bisphosphate) to IP3 (inositol 1,4,5-trisphosphate) and DAG (diacylglycerol). IP3 stimulates the release of sequestered stores of calcium, leading to an increased concentration of cytoplasmic Ca2+ that may then activate Ca2+-dependent protein kinases that phosphorylate their substrates. DAG activates protein kinase C (PKC) (GDP, guanosine diphosphate; GTP, guanosine triphosphate). See Table Catecholamine Receptors: Location and Actions and text for physiologic effects of α1 receptor activation.

στίξω

��. �� . �� β- � α2-�� = Catecholamine Receptors. Activation of β- and α2-adrenergic responses. �� ��: Gardner D.G., Shoback D.M., Eds. Greenspan's Basic & Clinical Endocrinology. 9th ed., Lange, 2011, 960 p., ��.: �� : ��. ��.

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Activation of β- and α2-adrenergic responses: activation vs inhibition of adenyl cyclase. Beta receptor ligands activate the stimulatory G protein, Gs, which leads to the dissociation of its Gs subunit, charged with GTP. The activated Gs subunit directly activates adenyl cyclase, resulting in increased cAMP that binds to the regulatory subunit (R) of the cAMP-dependent protein kinase, leading to the liberation of active catalytic subunits (C) that phosphorylate specific enzyme substrates and modify their activity. These catalytic units also phosphorylate the cAMP response element�binding protein (CREB), which modifies gene expression. Alpha2 adrenoreceptor ligands inhibit adenyl cyclase by causing dissociation of the inhibitory G protein (Gi) into its subunits; that is, the αi subunit charged with GTP and a βγ unit. The mechanism by which these subunits inhibit adenyl cyclase is uncertain. See Table Catecholamine Receptors: Location and Actions.

Carmichael S.W., Department of Anatomy Mayo Clinic. The Chromaffin Cell Home Page. �� .
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Carmichael S.W., Department of Anatomy Mayo Clinic. A History of the Adrenal Medulla. �� .
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URL: http://webpages.ull.es/users/isccb12/ChromaffinCell/History.html quotation

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