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20-September-2008 10:21:21 - Catecholamine epinephrine epinephrine norepinephrine norepinephrine dopamine dopamine Catecholamines are chemical compounds derived from the amino acid tyrosine containing catechol and amine groups. Some of them are biogenic amines. Catecholamines are water-soluble and are 50% bound to plasma proteins, so they circulate in the bloodstream. The most abundant catecholamines are epinephrine adrenaline, norepinephrine noradrenaline and dopamine, all of which are produced from phenylalanine and tyrosine. Tyrosine is created from phenylalanine by hydroxylation by the enzyme phenylalanine hydroxylase. Tyrosine is also ingested directly from dietary protein. It is then sent to catecholamine-secreting neurons. Here, many kinds of reactions convert it to dopamine, to norepinephrine, and eventually to epinephrine.1 Catecholamines are hormones that are released by the adrenal glands in situations of stress such as psychological stress or low blood sugar levels.2 Contents 1 Production 1.1 Location 1.2 Synthesis 2 Function 2.1 Modality 2.2 Effects 2.3 Function in plants 3 Structure 4 Degradation 5 See also 6 References 7 External links Production Location Catecholamines are produced mainly by the chromaffin cells of the adrenal medulla and the postganglionic fibers of the sympathetic nervous system. Dopamine, which acts as a neurotransmitter in the central nervous system, is largely produced in neuronal cell bodies in two areas of the brainstem: the substantia nigra and the ventral tegmental area. Synthesis Dopamine is the first cathecholamine to be synthesised from steps shown. Norepinephrine and epinephrine, in turn, are derived from further modifications of dopamine. It is important to note that the enzyme dopamine hydroxylase requires copper as a cofactor not shown and DOPA decarboxylase requires PLP not shown. Catecholamine synthesis. Catecholamine synthesis. Catecholamine synthesis is inhibited by alpha-Methyltyrosine, by inhibiting tyrosine-3 monooxygenase.3 Function Modality Two catecholamines, norepinephrine and dopamine, act as neuromodulators in the central nervous system and as hormones in the blood circulation. The catecholamine norepinephrine is a neuromodulator of the peripheral sympathetic nervous system but is also present in the blood mostly through spillover from the synapses of the sympathetic system. High catecholamine levels in blood are associated with stress, which can be induced from psychological reactions or environmental stressors such as elevated sound levels, intense light, or low blood sugar levels. Extremely high levels of catecholamines also known as catecholamine toxicity can occur in central nervous system trauma due to stimulation and/or damage of nuclei in the brainstem, in particular those nuclei affecting the sympathetic nervous system. In emergency medicine, this occurrence is widely known as catecholamine dump. Extremely high levels of catecholamine can also be caused by neuroendocrine tumors in the adrenal medulla, a treatable condition known as pheochromocytoma. Effects Catecholamines cause general physiological changes that prepare the body for physical activity fight-or-flight response. Some typical effects are increases in heart rate, blood pressure, blood glucose levels, and a general reaction of the sympathetic nervous system. Some drugs, like tolcapone a central COMT-inhibitor, raise the levels of all the catecholamines. Function in plants They have been found in 44 plant families, but no essential metabolic function has been established for them. They are precursors of benzocphenanthridine alkaloids, which are the active principal ingredients of many medicinal plant extracts. CAs have been implicated to have a possible protective role against insect predators, injuries, and nitrogen detoxification. They have been shown to promote plant tissue growth, somatic embryogenesis from in vitro cultures, and flowering. CAs inhibit indole-3-acetic acid oxidation and enhance ethylene biosynthesis. They have also been shown to enhance synergistically various effects of gibberellins.4 Structure Catecholamines have the distinct structure of a benzene ring with two hydroxyl groups, an intermediate ethyl chain, and a terminal amine group. Degradation They have a half-life of approximately a few minutes when circulating in the blood. Monoamine oxidase MAO is the main enzyme responsible for degradation of catecholamines. Methamphetamine and MAOIs bind in order for MAOs to inhibit their action of breaking down catecholamines. This is primarily the reason why the effects of amphetamines have a longer lifespan than those of cocaine and other substances. Amphetamines not only cause a release of dopamine, epinephrine, and norepinephrine into the blood stream but also suppress re-absorption. See also Catechol-O-methyl transferase Hormone Julius Axelrod Phenethylamines Steroid hormone Peptide hormone Sympathomimetics Vanillyl mandelic acid References ^ Dopamine beta-hydroxylase: biochemistry and molecu...Ann N Y Acad Sci. 1987 - PubMed Result ^ Hypoglycemia by Ronald Hoffman, M.D., July 1999, The Holistic M.D. ^ wrongdiagnosis.com - Description of Alpha-Methyltyrosine ^ A. I. Kuklin and B. V. Conger, Catecholamines in plants, Journal of Plant Growth Regulation, Springer New York ISSN 0721-7595 Print, ISSN 1435-8107 Online, Issue Volume 14, Number 2 / June, 1995 DOI 10.1007/BF00203119, pp. 91-97. External links MeSH Catecholamines Retrieved from http://en..org/wiki/Catecholamine Categories: Benzenediols | Biogenic amines | Catecholamines | Neurotransmitters | Sympathomimetics Views Article Discussion this page History Personal tools Log in / create account Navigation Main page Contents Featured content Current events Random article Search Go Search Interaction Community portal Recent changes Contact Donate to Help Toolbox What links here Related changes Upload file Special pages Printable version Permanent link Cite this page Languages Deutsch Español Français Ã?slenska Italiano МакедонÑ?ки 日本語 Nederlands Polski Português РуÑ?Ñ?кий SlovenÅ¡Ä?ina Suomi Svenska УкраїнÑ?ька This page was last modified on 19 July 2008, at 17:53
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