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Related Concept Videos

Adrenergic Neurons: Neurotransmission01:27

Adrenergic Neurons: Neurotransmission

Postganglionic sympathetic fibers (except those supplying the sweat glands) releasing noradrenaline or norepinephrine are called noradrenergic or adrenergic neurons. Noradrenaline, dopamine, adrenaline, or epinephrine are collectively called "catecholamines" as they contain a catechol moiety and an amine side chain. The five stages of neurotransmitter release involve their synthesis, storage, release, reuptake and metabolism.
Synthesis: Catecholamine synthesis requires tyrosine, which is taken...
Drugs Affecting Neurotransmitter Synthesis01:29

Drugs Affecting Neurotransmitter Synthesis

Drugs affecting neurotransmitter synthesis can impact the adrenergic neuron and the synthesis of neurotransmitters. For example, α-methyltyrosine and carbidopa target specific enzymes involved in catecholamine synthesis. α-methyltyrosine inhibits the enzyme tyrosine hydroxylase, which converts tyrosine into dopamine. By blocking this enzyme, α-methyltyrosine reduces dopamine production and other catecholamines. Carbidopa, on the other hand, inhibits the enzyme dopa decarboxylase, which converts...
Adrenergic Agonists: Indirect-Acting Agents01:25

Adrenergic Agonists: Indirect-Acting Agents

Indirect-acting adrenergic agonists potentiate the effects of endogenous catecholamines through different mechanisms without directly binding to adrenoceptors.
One mechanism involves depleting stored catecholamines by displacing them from synaptic vesicles. These agents, known as "displacers," are transported into vesicles at the expense of noradrenaline. Examples include amphetamine and tyramine, which lack a catechol moiety, resulting in prolonged action, improved oral bioavailability, and...
Drugs Affecting Neurotransmitter Release or Uptake01:21

Drugs Affecting Neurotransmitter Release or Uptake

Certain drugs can affect how neurotransmitters called catecholamines, are released or taken back up in the adrenergic neuron. They can have different effects on the body's sympathetic transmission. Reserpine, a natural compound found in the Rauwolfia shrub, blocks a transporter called vesicular monoamine transporter (VMAT), which leads to a buildup of catecholamines in the cell and reduces sympathetic transmission. Another drug called guanethidine works in multiple ways, including blocking...
Adrenergic Agonists: Chemistry and Structure-Activity Relationship01:16

Adrenergic Agonists: Chemistry and Structure-Activity Relationship

Adrenergic agonists' structure-activity relationship (SAR) determines their selectivity and efficacy. These agonists comprise a phenylethylamine moiety with an aromatic ring and an ethylamine side chain.
Aromatic ring substitutions: Substituting the aromatic ring with –OH groups at positions 3 and 4 yields catecholamines (e.g., epinephrine), which have a high affinity for adrenoceptors. Hydrogen bonding between –OH groups and receptors enhances adrenergic activity.
Separation of the aromatic...
Adrenergic Receptors: ɑ Subtype01:31

Adrenergic Receptors: ɑ Subtype

Adrenoceptors are classified into α and ꞵ classes based on their potencies to catecholamine agonists. α-adrenoceptors show the following order of catecholamine potency:
Adrenaline ≥ Noradrenaline >> Isoprenaline
α-adrenoceptors are further divided into α1 and α2-adrenoceptors.
α1-Adrenoceptors: These receptors are located postsynaptically on the effector organs and cause constriction of smooth muscle mediated by activation of phospholipase C—inositol-1,4,5-trisphosphate...

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Related Experiment Video

Updated: Jun 12, 2026

A Convenient Method for Extraction and Analysis with High-Pressure Liquid Chromatography of Catecholamine Neurotransmitters and Their Metabolites
13:35

A Convenient Method for Extraction and Analysis with High-Pressure Liquid Chromatography of Catecholamine Neurotransmitters and Their Metabolites

Published on: March 1, 2018

Studies on catecholamine-synthesizing enzymes.

M Goldstein1

  • 1New York University Medical Center, Neurochemistry Research Laboratories, 560 First Avenue, Rm H-544, New York, NY 10016, U.S.A.

Neurochemistry International
|May 28, 2010
PubMed
Summary
This summary is machine-generated.

Researchers purified and characterized key enzymes in catecholamine biosynthesis, including tyrosine hydroxylase (TH), dopamine beta-hydroxylase (DBH), and phenylethanolamine N-methyl-transferase (PNMT). Antibodies were developed to study enzyme activity regulation and map dopamine neurons in the CNS.

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A Convenient Method for Extraction and Analysis with High-Pressure Liquid Chromatography of Catecholamine Neurotransmitters and Their Metabolites
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Assessment of Dopaminergic Homeostasis in Mice by Use of High-performance Liquid Chromatography Analysis and Synaptosomal Dopamine Uptake

Published on: September 21, 2017

Area of Science:

  • Neuroscience
  • Biochemistry
  • Enzymology

Background:

  • Catecholamines are critical neurotransmitters involved in various physiological processes.
  • Understanding the enzymes responsible for catecholamine biosynthesis is essential for neurological research.
  • Tyrosine hydroxylase (TH), dopamine beta-hydroxylase (DBH), and phenylethanolamine N-methyl-transferase (PNMT) are key enzymes in this pathway.

Purpose of the Study:

  • To review the purification and characterization of three key catecholamine biosynthesis enzymes.
  • To investigate the role of antibodies in studying enzyme activity and localization.
  • To explore the regulation of tyrosine hydroxylase activity through phosphorylation.

Main Methods:

  • Purification of TH, DBH, and PNMT from various tissue sources.
  • Generation of polyclonal and monoclonal antibodies against these enzymes.
  • Enzyme activity assays and inhibition studies using antibodies.
  • Immunohistochemical localization of dopamine neurons and PNMT-containing neurons in the CNS.

Main Results:

  • Polyclonal antibodies against native TH inhibited its activity, while antibodies against a TH segment stimulated it.
  • Monoclonal antibodies against TH showed no significant effect on enzyme activity.
  • Phosphorylation by protein kinases was identified as crucial for short-term TH regulation.
  • DBH antibodies exhibited poor interspecies cross-reactivity.
  • PNMT antibodies enabled the immunohistochemical mapping of PNMT-containing neurons in C1 and C2 clusters.

Conclusions:

  • Antibodies are valuable tools for characterizing catecholamine biosynthesis enzymes and their functions.
  • Enzyme phosphorylation is a key mechanism for regulating TH activity.
  • Immunohistochemistry using specific antibodies is effective for mapping neurotransmitter systems in the CNS.
  • Distinct neuronal populations containing PNMT were identified and their projections characterized.