I asked myself..

AnnT2 · 10-31-2007, 08:00 PM

When I went to school and when I first started to teach, classes were arranged according to level of achievement. That is no longer politically correct. However, I can tell you folks above would have been in the top group. When I read some of these scientific tomes, I get glassy eyed and dazed. I do not have the background to understand the content of your posts. Somebody should speak for those of who are not as clued in to the science of what you are saying. You have heard of legal-eze language. I need deciphering of the scientific-eze language, or in other words, "Say what?"

reverett123 · 10-31-2007, 08:42 PM

I, too, was once mortal....

But seriously, there are only two reasons to tackle the learning curve here. One is the sincere and not totally baseless hope of finding something that has been overlooked. The second is the feeling that one has some control over one's life. A writer once said ( I think it was Rhetta Ghrimley Johnson ) "I come from a family that believed that with enough library time any problem could be solved." Were that it was always true, but I gotta try.

The single greatest aid to understanding this language that I have found is a simple little program free for the download at www.answers.com called 1-Click Answers. Install it and anytime you run across a word you don't know just Alt-click it. A little popup screen appears with a short definition and then goes away. It is one of the most elegant little pieces of software I have ever seen.

michael7733 · 11-01-2007, 01:25 AM

Those molecules that readily give up an electron from a hydrogen ion and are small enough or nimble enough to invade complex 1 or complex 4 are the substances we need to watch. The resulting yields in the equation lack the production of water as a by-poduct and result in dehydration and eventual acidosis and apoptosis or necrosis. Once the molecule is utilized by the mitochondria, it is tagged as being "human" and is no longer considered an aliien by the immune system and is, essentially, granted a pass to move on to another cell.

That's the way I see it, anyway. See electron donors and electron acceptors---hydrogen donors and hydrogen acceptors and cross reference what you find with known Parkinson's initiators.

michael b.

paula_w · 11-01-2007, 01:46 AM

Welcome Michael, I was hoping this conversation would get your attention.

I'm fascinated that i can follow it even some. We are fortunate to have such. as Rick might label them, 'superpower minds' [which we all know from watching Spiderman, are not mortal] on the forum.

paula

michael7733 · 11-01-2007, 01:49 AM

Quote:

I FOUND IT, I FOUND IT, I FOUND IT!!!!!!!! ONE REASON WHY THE NEURONS DIE!!!!!!!!!!!! SOME OF THE POSSIBLE CULPRITS AND HOW THEY DO IT!!!!!!!!!!!!!!!!!!!! A METHOD OF IDENTIFYING OTHERS!!!!!!!!!! TAKE A LOOK----IT IS DOCUMENTED, SCIENTIFIC DATA AND NOT SPECULATION ON MY PART!!!!!!!!! START POLISHING YOUR DANCING SHOES!!!!!!! quote: "58.What is a cytochrome? (Notes, 36) The cytochromes are electron acceptors which as a class are heme-containing proteins which mediate Fe+++/Fe++ one-electron transfers. There are five cytochromes with increasing electron accepting potentials. The heme in cytochromes b, c1, and c are Fe-protoporphyrin IX which is also the prosthetic group in myoglobin and hemoglobin. It is covalently attached to the protein in these cytochromes. 59.Which cytochrome is responsible for the reduction of molecular oxygen? (Notes, 36) Cytochrome oxidase. Contains cytochromes a and a3 as a complex, they are the terminal electron transport carriers. Each have a different prosthetic group, heme A, but the same basic Fe-tetrapyrrole structure. It also contains two copper atoms which alternate between Cu++ and Cu+. Electron transfer through cytochrome oxidase is inhibited by cyanide or CO which appear to bind very tightly to the cytochrome a3 moiety. 60.What type of structure is protoporphyrin IX? Where does it occur? (Notes, 36) The heme in cytochromes b, c1, and c are Fe-protoporphyrin IX which is also the prosthetic group in myoglobin and hemoglobin. It is covalently attached to the protein in these cytochromes. 61.What are several agents which inhibit electron transfer in the process of oxidative phosphorylation? (Notes, 33) It is of scientific and medical interest to note a number of chemicals which inhibit electron transport at different sites. The lethality of cyanide and carbon monoxide depends upon the selective blockage of cytochrome oxidase. Cyanide binds to the ferric form of iron of the (a) cytochromes and carbon monoxide binds to the ferrous form. The antibiotic antimycin A blocks electron flow at site two (cytochrome reductase), wheras rotenone and amytal block electron transfer within the NADH-Q reductase complex (below). Blockage at any site interrupts the generation of a proton gradient (below), and ATP synthesis is inhibited. Blockage sites: 62.Define the "uncoupling" of oxidative phosphorylation. What are several agents which uncouple oxidative phosphorylation? (Notes, 38) The chemiosmotic theory is supported by observations that compounds capable of disrupting a proton gradient across the inner mitochondrial membrane effectively UNCOUPLE oxidative phosphorylation. "Uncoupling" means that electron flow and oxygen reduction proceeds without simultaneous formation of ATP. 2,4-dinitrophenol (DNP) and other phenolic compounds are effective uncouplers. These lipophilic compounds transfer protons across the inner mitochondrial membrane, breaking down the proton gradient. 63.How does cyanide inhibit oxidative phosphorylation? How does carbon monoxide inhibit oxidative phosphorylation? (Notes, 33) The lethality of cyanide and carbon monoxide depends upon the selective blockageof cytochrome oxidase. Cyanide binds to the ferric form of iron of the (a) cytochromes and carbon monoxide binds to the ferrous form. 64.Brifly describe the "Chemosmotic Hypotheses" of oxidative phosphorylation. (Notes, 37) The coupling of OXIDATION and PHOSPHORYLATION is indirect. Briefly stated: 1.protons are pumped from the inner to the outer side of the inner mitochondrial membrane during electron transport. 2.the inner membrane is not freely permeable to protons so an electromotive potential is established across this membrane. 3.a transmembrane multisubunit enzyme ATP synthetase (intrinsic to themitochondrial membrane) converts ADP to ATP as outermembrane protons re-enter themitochondria through a channel coupled to ATP synthase. Supported by evidence of the pH gradient which exists across the inner mitochondrial membrane.... "I didn’t say it was easy to understand. Are you excited, michael?? You betcha!!! michael oops. I forgot to give the source: So, what has caused me to come to this conclusion? First, what is that conclusion? I have concluded that a class of substances that can potentially cause Parkinson’s disease, has been identified and profiled. By using that profile, we should be able to identify other substances with the same profile and test them to see if they do indeed cause Parkinson’s or Parkinson’s like symptoms. It’s like reducing a haystack down to a handfull of hay. What brought me to this conclusion? Well, tonight I started thinking about some of the products that I have used (alternatives) that have given me significant improvement. I realized that most of them had Hydrogen in their formulas. I then looked at what goes on in the mitochondria, and I realized that Hydrogen is a key element in the production of ATP, the energy of the cell. I then saw that NADH gave up its Hydrogen in the process, so in my mind, it is a hydrogen donor. That is what I called it, anyway. I did a Google search on ‘Hydrogen donors,’ and there they were, along with ‘Hydrogen Acceptors.’ "Hmmmmmmmm" I said. Then, I asked myself, "What are some Hydrogen Acceptors?" Guess what I found in the list. I found, among others, Iron, Manganese, copper, and Rotenone. Every one of these are suspected as possible causes of PD., but I have never seen anything that said they were in any way related. Next, I wondered if there were a way to identify other such substances. Low and behold, there is a database into which one can submit a specific profile Query, and it will spit out the names of substances that match that profile. By this time I was really getting excited. Next, I learned that many of these substances can be neutralized. WOWZERS!!! Do you know what that means?? That’s how I see it, anyway. I think that we can reverse this disease in many if not most cases. NOW I AM REALLY EXCITED, BUT NOBODY IS AWAKE!!!!!!!!!

What do you think Chuck? Will this hold water? Pun intended.

michael7733 · 11-01-2007, 01:53 AM

Oops, I didn't know anybody was watching. How are you?

AnnT2 · 11-01-2007, 07:59 AM

Thanks for making it so clear!

Ann

michael7733 · 11-01-2007, 09:43 AM

http://www.brooklyn.cuny.edu/bc/ahp/...ochondria.html

Here are the contents of that website.

Quote:

Mitochondria

The energy stored in food comes in large denominations. Lipids, carbohydrates and even proteins ingested or taken up by cells provides them with the energy they need for growth and metabolic activities. Before cells can access this energy, however, it must be broken down into "bite size" pieces. This is the role of the mitochondria.
In eukaryotic cells mitochondria

are involved in the final stages of energy release from food molecules such as sugars. After being broken down to two-carbon fragments in the cytoplasm, the terminal products of catabolic processes such as glycolysis move inside the mitochondria organelles. In a further series of chemical breakdown reactions carbon dioxide is produced and energy trapped in high energy electrons. Finally the energy in these electrons is released in a stepwise chain reaction that transfers manageable packets of energy to molecules of ATP and the final waste product, water, is created.
Such complex activities are possible because of the structural organization of the mitochondrion. Each organelle has a double membrane; an outer membrane which is smooth and defines the shape of the organelle, and an inner membrane which is heavily folded into finger-like cristae producing a large surface area.
Within the central compartment of the inner mitochondrial membrane are the Krebs cycle enzymes that, in a cyclical series of chemical reactions, break down the two-carbon fragments to carbon dioxide. As part of these breakdown reactions high energy electrons are produced. Carried by modified nucleotide molecules, these electrons are transferred to a highly organized series of proteins, enzymes and electron carriers that are embedded in the inner mitochondrial membrane. In a stepwise, cascading fashion the electrons are serially transferred down an energy chain, loosing some of their energy at each step. This released energy is not lost, but used to pump hydrogen ions from one side of the membrane to the other.
When the electrons are at their lowest levels they are combined with oxygen and hydrogen ions to produce water. But, back in the mitochondrial membranes, the unbalanced gradient of hydrogen ions on either side of the mitochondrial membrane is producing an energy potential across the barrier. As the electrons flow back to the inner compartment, they pass through an enzyme/protein complex embedded within the mitochondrial inner membrane. Energy is once again moved, this time into a chemical reaction that forms ATP. This ATP molecule is the short term energy currency of cells and organisms.
All eukaryotic cells have mitochondria. Heart cells or other similar cells with high metabolic activity, have a lot of mitochondria to keep the cell provided with the ATP it needs for its specialized role. Other cells, such as lipid storage cells, still have mitochondria, but, because of their much lower levels of metabolic activity, they have fewer such organelles and produce less ATP.
Unlike other organelles within the cell, the mitochondria have their own DNA molecules and this genetic material is responsible for coding for some of the proteins and components used in the metabolic activities. Mitochondria also have their own distinct types of ribosomes and undergo what looks like a division process. At the time of sexual reproduction in animals, the fertilized zygote receives all its mitochondria from its mother. This 'maternal' inheritance of mitochondria and the DNA they carry makes it possible to trace backwards the genesis of our species to the 'original' woman on who's mitochondria we still all depend.

I hope that makes things a bit clearer.

michael b.

Curious · 11-01-2007, 11:24 AM

Quote:

Originally Posted by AnnT2

When I went to school and when I first started to teach, classes were arranged according to level of achievement. That is no longer politically correct. However, I can tell you folks above would have been in the top group. When I read some of these scientific tomes, I get glassy eyed and dazed. I do not have the background to understand the content of your posts. Somebody should speak for those of who are not as clued in to the science of what you are saying. You have heard of legal-eze language. I need deciphering of the scientific-eze language, or in other words, "Say what?"

ann,

at the top of the NeuroTalk page there is also direct links to PubMed, Drugs and a Medical Dictionary. makes it easy to look up something without leaving the post you were reading.

i hope this helps. also the link rick gave is great.

ZucchiniFlower · 11-01-2007, 10:02 PM

I'm in a rush to go home, but want to leave you with this link:

Inhibition of brain mitochondrial respiration by dopamine and its metabolites: implications for Parkinson's disease and catecholamine-associated diseases

"In summary, mitochondrial respiration can be inhibited by DA and its metabolites by four distinct MAO-dependent and independent mechanisms."

Journal of Neurochemistry

Volume 91 Issue 4 Page 788-795, November 2004

Martin R. Gluck, Gail D. Zeevalk (2004)

http://www.blackwell-synergy.com/doi....x?cookieSet=1

Let me know if you don't have access to the article. I can email it if necessary.

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