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06-07-2009, 01:58 AM | #1 | |||
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In Remembrance
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The synthesis of dopamine in the body goes
protein----> phenylalanine ----> levodopa ----> dopamine Since dopamine can't pass the BBB, we take levodopa. But long term side effects mean dyskinesia etc. Therefore why not take phenylalanine?? Well, being a white rat, I tried it a year ago but it did not switch me on. Maybe I had too low a dose, I don't know. So I dropped the idea. However, the report below suggests that it works. Any ideas? Girija, what do you think? Ron Brain Food: Nuts! (Part 1) | Nutrition Wonderland By Christie Wilcox Almonds contain phenylalanine, which unlike other compounds crosses the blood-brain barrier easily, and has been shown to alleviate Parkinson's Disease and boost the neurotransmitters dopamine and adrenaline. ... Nutrition Wonderland - http://nutritionwonderland.com/
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"Thanks for this!" says: | rose of his heart (06-07-2009) |
06-07-2009, 04:51 AM | #2 | ||
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If phenylalanine converts to levodopa > dopamine , why do you expect that it is different from taking levodopa in terms of benifits and side effects? |
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06-07-2009, 11:37 AM | #3 | |||
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Hi Imark3000,
I have no evidence to say it will be any improvement on levodopa. I just thought it was worth trying, to see if there were fewer side effects, taking the precurser of levodopa, instead of levodopa itself. Phenylalanine like levodopa passes the BBB, and the report in my first post claims it "has been shown to alleviate Parkinson's Disease and boost the neurotransmitters dopamine and adrenaline". I wondered whether it was a more controlled and natural process if the brain manufactured the levodopa, rather than being fed it from a chemical factory material. A healthy person starts the eynthesis with protein. Starting the in brain process with phenylalanine is only one step away from that. Using levodopa is 2 steps away. Ron
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"Thanks for this!" says: | imark3000 (06-08-2009) |
06-07-2009, 10:41 PM | #4 | |||
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In Remembrance
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1: J Nutr. 2007 Jun;137(6 Suppl 1):1539S-1547S; discussion 1548S.
Tyrosine, phenylalanine, and catecholamine synthesis and function in the brain. Fernstrom JD, Fernstrom MH. Department of Psychiatry, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA. fernstromjd@upmc.edu Aromatic amino acids in the brain function as precursors for the monoamine neurotransmitters serotonin (substrate tryptophan) and the catecholamines [dopamine, norepinephrine, epinephrine; substrate tyrosine (Tyr)]. Unlike almost all other neurotransmitter biosynthetic pathways, the rates of synthesis of serotonin and catecholamines in the brain are sensitive to local substrate concentrations, particularly in the ranges normally found in vivo. As a consequence, physiologic factors that influence brain pools of these amino acids, notably diet, influence their rates of conversion to neurotransmitter products, with functional consequences. This review focuses on Tyr and phenylalanine (Phe). Elevating brain Tyr concentrations stimulates catecholamine production, an effect exclusive to actively firing neurons. Increasing the amount of protein ingested, acutely (single meal) or chronically (intake over several days), raises brain Tyr concentrations and stimulates catecholamine synthesis. Phe, like Tyr, is a substrate for Tyr hydroxylase, the enzyme catalyzing the rate-limiting step in catecholamine synthesis. Tyr is the preferred substrate; consequently, unless Tyr concentrations are abnormally low, variations in Phe concentration do not affect catecholamine synthesis. Unlike Tyr, Phe does not demonstrate substrate inhibition. Hence, high concentrations of Phe do not inhibit catecholamine synthesis and probably are not responsible for the low production of catecholamines in subjects with phenylketonuria. Whereas neuronal catecholamine release varies directly with Tyr-induced changes in catecholamine synthesis, and brain functions linked pharmacologically to catecholamine neurons are predictably altered, the physiologic functions that utilize the link between Tyr supply and catecholamine synthesis/release are presently unknown. An attractive candidate is the passive monitoring of protein intake to influence protein-seeking behavior. PMID: 17513421 [PubMed - indexed for MEDLINE]
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Born in 1953, 1st symptoms and misdiagnosed as essential tremor in 1992. Dx with PD in 2000. Currently (2011) taking 200/50 Sinemet CR 8 times a day + 10/100 Sinemet 3 times a day. Functional 90% of waking day but fragile. Failure at exercise but still trying. Constantly experimenting. Beta blocker and ACE inhibitor at present. Currently (01/2013) taking ldopa/carbadopa 200/50 CR six times a day + 10/100 form 3 times daily. Functional 90% of day. Update 04/2013: L/C 200/50 8x; Beta Blocker; ACE Inhib; Ginger; Turmeric; Creatine; Magnesium; Potassium. Doing well. |
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06-08-2009, 01:40 AM | #5 | |||
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Thanks Rick for the article, it reminded me I forgot to put tyrosine in the sequence. I did my first post from memory at 6-00am!!
The full sequence is. protein---->phenylalanine---->tyrosine---->levodopa---->dopamine Phenylalanine, tyrosine and levodopa are all amino acids, but differ by the number of hydroxyl groups on the aromatic ring. I originally tried phenylalanine since it is readily available in UK health shops. I did not find tyrosine. Surely someone somewhere has tried this before, with either phenylalanine or tyrosine, even on animal testing. Ron
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06-08-2009, 01:59 AM | #6 | ||
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Ron,
This is my guess. I think phenylalanine when accumulated or in excess in the blood is toxic to body as seen in PKU patients. I suspect drug developers didnt want to take a chance with Phe and the next step in biosynthesis seemed good enough. Quote:
http://www.nature.com/jcbfm/journal/v18/n11/index.html © 2009 International Society for Cerebral Blood Flow & Metabolism Last edited by Chemar; 06-08-2009 at 07:14 AM. Reason: sorry that Journal has clear copyright disclaimer! |
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06-08-2009, 08:42 AM | #7 | ||
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06-08-2009, 11:56 AM | #8 | ||
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Good Morning lurkingforacure,
There are tests available to see if you cannot metabolize Phenylalanine. Please check with your doctor. THe classical disorder is called PKU and it is a genetic disorder. see the links below (wikipedia links). I have not checked to see if there are any publications about this and PWPs I will check. Links: # Phenylalanine (abbreviated as Phe or F) is an α-amino acid with the formula HO2CCH(NH2)CH2C6H5, which is found naturally in the breast milk of mammals and ... en.wikipedia.org/wiki/Phenylalanine - Cached - Similar pages # Phenylalanine hydroxylase - Wikipedia, the free encyclopedia Phenylalanine hydroxylase is the rate-limiting enzyme of the metabolic pathway which degrades excess phenylalanine. The other substrates in the reaction are ... en.wikipedia.org/wiki/Phenylalanine_hydroxylase - Cached - Similar pages Girija |
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"Thanks for this!" says: | lurkingforacure (06-08-2009) |
06-08-2009, 12:04 PM | #9 | ||
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This is interesting information. Check it out!
Parkinson's Disease, Michael Fox, MS And The Aspartame Story Dr. Roberts goes in depth about aspartame and Parkinson's Disease. ... The enzyme phenylalanine hydroxylase converts phenylalanine to tyrosine. ... www.rense.com/general21/parkinsonFox.htm - Cached - Similar pages # Parkinson's disease and |
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06-08-2009, 07:14 PM | #10 | ||
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I've been taking tyrosine for the past 9 months, and enjoy a daily handful or two of almonds. Don't know whether these two, in combination, are helping slow the progression, but so far, 3 years after dx and 4 years after first symptoms, I've not had to take any medications (sinemet, etc).
I do wish that almonds had a lower fat content -- urp. Jon |
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