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04-19-2012, 08:27 AM | #11 | ||
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In Remembrance
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[quote=pegleg;871528]paula -
I'm off right now, feeling crappy, and know I should not push the submit button. But your comment singling out one person's opinion is out of order, in my humble opinion. Lindy said ". . ., I read it a second time and found that the sentence near to the end "I'm excited........." did not fit my feelings. I am putting this one on a back burner in my mind, I really do not want to think about it" All of us prioritize our items of opinion onto burners in our minds. The author has just put something out there to think about - you commented, gave us your thoughts and others their opinions. Why cause anyone to not feel free to also add his/her thoughts? Respectfully, Peggy[/quote I'm sorry Peg, I thanked everyone who refuted and agreed with lindy that it's best not to think about it. I didn't mean the thread should end, altho i can see how it looks like it. As for the specifics about what you wrote, i've always said it worries me to be dealing with alpha synuclein without knowing it's function. Hopefully it will stop the disease but still no cause.
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paula "Time is not neutral for those who have pd or for those who will get it." |
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"Thanks for this!" says: | pegleg (04-19-2012) |
04-19-2012, 08:50 AM | #12 | ||
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In Remembrance
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Quote:
Hey wait a minute! i didn't even see your post before i typed mine!/ hope that helps...i was just starting mine when you posted.
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paula "Time is not neutral for those who have pd or for those who will get it." Last edited by paula_w; 04-19-2012 at 08:51 AM. Reason: realized this while taking a shower |
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"Thanks for this!" says: | lindylanka (04-19-2012), pegleg (04-19-2012) |
04-19-2012, 08:54 AM | #13 | ||
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Senior Member
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Frankly, I have to put it on the back burner, because I have things to do and cannot afford right now to go off on a protracted research binge on prions and prion-like things. So I am grateful for Giriijas post that helps me understand a little more. But putting something on the back burner does not mean rejecting it, rather letting it stay in a place where I can process it without it stopping me in my tracks.
As far as I can see a prion like cause does not rule out many of the other things often discussed here over the years, like autoimmune response, inflammation etc. They could be effects of the cause........ Peggy, Paula, I love you both dearly, and know where you are coming from. Just can't get too off-topic....... it's just that the author has a tendency to cover all bases just in case....... As far as I can see there is still no real explanation about how the prion like thing gets there, into our brains, I mean. |
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"Thanks for this!" says: | pegleg (04-19-2012) |
04-19-2012, 02:46 PM | #14 | |||
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In Remembrance
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Wellll, It may be better news than you think. Consider the following-
1. Neurosci Res. 2012 Mar 23. [Epub ahead of print] Autophagy induced by resveratrol prevents human prion protein-mediated neurotoxicity. Jeong JK, Moon MH, Bae BC, Lee YJ, Seol JW, Kang HS, Kim JS, Kang SJ, Park SY. Korea Zoonoses Research Institute, Bio-Safety Research Institute, Center for Healthcare Technology Development, College of Veterinary Medicine, Chonbuk National University, Jeonju 561-756, South Korea. Our previous study revealed that resveratrol blocks prion protein peptide PrP(106-126)-induced neurotoxicity. However, the mechanism of resveratrol-mediated neuroprotection in prion diseases is not clear. Resverstrol initiates neuroprotective effects via the activation of autophagy, which protects organelles, cells, and organisms against misfolded protein-disorders, including Alzheimer's disease and Parkinson's disease via regulation of mitochondrial homeostasis. Thus, we focused on elucidating the mechanisms responsible for resveratrol-mediated neuroprotection related to mitochondrial homeostasis as a result of autophagy activation. Resveratrol prevented PrP(106-126)-induced neuronal cell death by activating autophagy. Moreover, resveratrol-induced autophagy prevented the PrP(106-126)-induced reduction in mitochondrial potential and translocation of Bax to the mitochondria and cytochrome c release. Our results indicate that treatment with resveratrol appears to protect against neurotoxicity caused by prion protein peptides and the neuroprotection is induced by resveratrol-mediated autophagy signals. Copyright © 2012 Elsevier Ireland Ltd and the Japan Neuroscience Society. All rights reserved. PMID: 22465415 [PubMed - as supplied by publisher] and 1. J Pineal Res. 2012 Jan 30. doi: 10.1111/j.1600-079X.2012.00980.x. [Epub ahead of print] Melatonin-induced autophagy protects against human prion protein-mediated neurotoxicity. Jeong JK, Moon MH, Lee YJ, Seol JW, Park SY. Korea Zoonoses Research Institute, Bio-Safety Research Institute, Center for Healthcare Technology Development, College of Veterinary Medicine, Chonbuk National University, Jeonju, Korea. * Melatonin has neuroprotective effects in the models of neurodegenerative disease including Alzheimer's and Parkinson's disease. Several studies have shown that melatonin prevents neurodegeneration by regulation of mitochondrial function. However, the protective action of melatonin has not been reported in prion disease. We investigated the influence of melatonin on prion-mediated neurotoxicity. Melatonin rescued neuronal cells from PrP(106-126)-induced neurotoxicity by prevention of mitochondrial dysfunction. Moreover, the protective effect of melatonin against mitochondrial dysfunction was related with autophagy activation. Melatonin-treated cells were dose-dependently increased in LC3-II, an autophagy marker. Melatonin-induced autophagy prevented a PrP(106-126)-induced reduction in mitochondrial potential and translocation of Bax to the mitochondria and cytochrome c release. On the other hand, downregulation of autophagy protein 5 with Atg5 siRNA or the autophagy blocker 3-methyladenine prevented the melatonin-mediated neuroprotective effects. This is the first report demonstrating that treatment with melatonin appears to protect against prion-mediated neurotoxicity and that the neuroprotection is induced by melatonin-mediated autophagy signals. The results of this study suggest that regulation of melatonin is a therapeutic strategy for prion peptide-induced apoptosis. © 2012 John Wiley & Sons A/S. PMID: 22335252 [PubMed - as supplied by publisher] and 1. Front Psychiatry. 2012;3:9. Epub 2012 Feb 17. A Medicinal Herb Scutellaria lateriflora Inhibits PrP Replication in vitro and Delays the Onset of Prion Disease in Mice. Eiden M, Leidel F, Strohmeier B, Fast C, Groschup MH. Institute for Novel and Emerging Infectious Diseases, Friedrich-Loeffler-Institut, Federal Research Institute for Animal Health Greifswald, Germany. Transmissible spongiform encephalopathies (TSE) are characterized by the misfolding of the host encoded prion protein (PrP(C)) into a pathogenic isoform (PrP(Sc)) which leads to the accumulation of β-sheet-rich fibrils and subsequent loss of neurons and synaptic functions. Although many compounds have been identified which inhibit accumulation or dissolve fibrils and aggregates in vitro there is no therapeutic treatment to stop these progressive neurodegenerative diseases. Here we describe the effects of the traditional medicinal herb Scutellaria lateriflora (S. lateriflora) and its natural compounds, the flavonoids baicalein and baicalin, on the development of prion disease using in vitro and in vivo models. S. lateriflora extract as well as both constituents reduced the PrP(res) accumulation in scrapie-infected cell cultures and cell-free conversion assays and lead to the destabilization of pre-existing PrP(Sc) fibrils. Moreover, tea prepared from S. lateriflora, prolonged significantly the incubation time of scrapie-infected mice upon oral treatment. Therefore S. lateriflora extracts as well as the individual compounds can be considered as promising candidates for the development of new therapeutic drugs against TSEs and other neurodegenerative diseases like Alzheimer's and Parkinson's disease. PMCID: PMC3281244 PMID: 22363300 [PubMed - in process] and 1. Biochemistry. 2010 Sep 21;49(37):8127-33. The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Meng F, Abedini A, Plesner A, Verchere CB, Raleigh DP. Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, USA. Islet amyloid polypeptide (IAPP, amylin) is the major protein component of the islet amyloid deposits associated with type 2 diabetes. The polypeptide lacks a well-defined structure in its monomeric state but readily assembles to form amyloid. Amyloid fibrils formed from IAPP, intermediates generated in the assembly of IAPP amyloid, or both are toxic to β-cells, suggesting that islet amyloid formation may contribute to the pathology of type 2 diabetes. There are relatively few reported inhibitors of amyloid formation by IAPP. Here we show that the tea-derived flavanol, (-)-epigallocatechin 3-gallate [(2R,3R)-5,7-dihydroxy-2-(3,4,5-trihydroxyphenyl)-3,4-dihydro-2H-1-benzopyran-3-y l 3,4,5-trihydroxybenzoate] (EGCG), is an effective inhibitor of in vitro IAPP amyloid formation and disaggregates preformed amyloid fibrils derived from IAPP. The compound is thus one of a very small set of molecules which have been shown to disaggregate IAPP amyloid fibrils. Fluorescence-detected thioflavin-T binding assays and transmission electron microscopy confirm that the compound inhibits unseeded amyloid fibril formation as well as disaggregates IAPP amyloid. Seeding studies show that the complex formed by IAPP and EGCG does not seed amyloid formation by IAPP. In this regard, the behavior of IAPP is similar to the reported interactions of Aβ and α-synuclein with EGCG. Alamar blue assays and light microscopy indicate that the compound protects cultured rat INS-1 cells against IAPP-induced toxicity. Thus, EGCG offers an interesting lead structure for further development of inhibitors of IAPP amyloid formation and compounds that disaggregate IAPP amyloid. PMCID: PMC3199968 PMID: 20707388 [PubMed - indexed for MEDLINE] ------------ I do wish they would figure out whether dissolving those tangles is a good thing or not.
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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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