Glycine is a protein amino acid found in the protein of all life forms. It is the simplest amino acid in the body and the only protein amino acid that does not have chirality. Although most glycine is found in proteins, free glycine is found in body fluids as well as in plants. The normal diet contributes approximately 2 grams of glycine daily.
Glycine is not considered an essential amino acid, i. e., the cells in the body can synthesize sufficient amounts of glycine to meet physiological requirements. However, glycine is of major importance in the synthesis of proteins, peptides, purines, adenosine triphosphate (ATP), nucleic acids, porphyrins, hemoglobin, glutathione, creatine, bile salts, one-carbon fragments, glucose, glycogen, and L-serine and other amino acids. Glycine is also a neurotransmitter in the central nervous system (CNS). Glycine and gamma-aminobutyric acid (GABA) are the major inhibitory neurotransmitters in the CNS. Recently, a glycine-gated chloride channel has been identified in neurophils that can attenuate increases in intracellular calcium ions and diminish oxidant damage mediated by these white blood cells. Thus, glycine may be a novel antioxidant.
Posts: 294 | From nevada | Registered: Sep 2005
| IP: Logged |
posted
Glycine also chelates aluminum if I remember correctly.
Hubby has taken large doses for at least a couple of months in the past (sometime during his 6 year battle with Lyme and tickborne infections). Have thought of restarting glycine after I read about it being used for stiff-man syndrome recently.
Think this might help with detox and/or act as an antioxidant to fight free radicals. However, do not think this will work as a cure -- will not kill any bugs in my opinion.
As with any amino acids, suggestion is to take it on an empty stomach. However, be aware that large doses may cause nausea or other G.I. symptoms.
Bea Seibert
Posts: 7306 | From Martinsville,VA,USA | Registered: Oct 2004
| IP: Logged |
The amino acid glycine can help prevent degenerative diseases such as osteoporosis and arthrosis, according to a new Spanish study. In addition, the study found that glycine supplementation may be required by most people because of the body's limited ability to synthesize it.
Glycine, which occurs naturally in fish, meat, and dairy products, is used by the body to make collagen and cartilage. The breakdown of cartilage, which leaves bones in joints exposed, is the hallmark of degenerative diseases. There is no cure for such diseases, and the only current treatments are painkillers, which do nothing to repair damaged cartilage.
The new study, conducted by the University of Granada and the Cellular Metabolism Institute in Tenerife, analyzed the effect of glycine supplementation on a group of 600 volunteers, average age 45, suffering from degenerative joint pain brought on by osteoporosis, arthrosis, or physical injuries. The study showed some improvement in all cases. Study leader Dr. Patricia de Paz Lugo said, ``We concluded that many degenerative diseases such as arthrosis can be treated as deficiency diseases due to the lack of glycine, since supplementing a diet with this amino acid leads to a notable improvement in symptomology without the need to take painkillers.''
The researchers believe glycine should be considered an essential amino acid, and that many degenerative diseases are in fact deficiency diseases brought on by the lack of glycine. They concluded that a daily 10 gram dose of glycine divided into two doses of five grams in morning and evening will lead to improvement in pain over a period of time ranging from two weeks to four months.
Posts: 294 | From nevada | Registered: Sep 2005
| IP: Logged |
treepatrol
Honored Contributor (10K+ posts)
Member # 4117
posted
From Jungle to Space in Pursuit of New Drugs The above article about Chagas' disease and space missions by Dinah Eng appeared on page 13 of the International Herald Tribune of 30 November 2000.
Some more background information on the technical aspects of the experiments in this article is given here by Fred Opperdoes
3-D structure of Trypanosome glyceraldehydephosphate dehydrogenase (GAPDH, 1GGA.PDB). Created with PDB to Animated Gif
Trypanosoma cruzi enzyme crystallized in space Trypanosomatidae are all without exception parasitic and some cause important disease, such as Chagas' disease in humans in the rural areas of Central and South America, which kills about 45,000 people a year, sleeping sickness in Tropical Africa, responsible for an estimated 300.000 fatal cases per year and leishmaniasis in most tropical and subtropical parts of the world, responsible for some 12 million infected people and an estimated hundred thousand deaths per year.
Few drugs are available for the treatment of these diseases and many are not without side effects. Also an increasing drug resistance of the parasites causes great concern for the future.
Several laboratories have now engaged in the development of new and better drugs for these diseases of the poor. The glycolytic pathway MARNIE!!! of the trypanosomatid parasites causing these diseases is considered an excellent drug target.
Biochemists in Brussels (Belgium) and protein crystallographers in Seattle (USA) and in Sao Carlos in Brazil, have since 1985 studied the glycolytic enzymes of these parasites in great detail with the aim of developing specific drugs that interfere with the their functioning and so may lead to a rapid cure for trypanosomiasis and leishmaniasis.
Studies on the glyceraldehydephosphate dehydrogenase (GAPDH) of Trypanosoma brucei and the related parasites Leishmania mexicana all these are similar to lyme they break up into coccoid or into cyst forms when threatend and Trypanosoma cruzi have revealed that especially this enzyme would be a very good drug target indeed. However, drug development depends of a detailed knowledge of the differences in three-dimensional structure of the target enzyme and the corresponding enzyme of the human host.
Therefore, the crystal structures of all three parasite enzymes and of the human enzyme had to be solved. The Leishmania and T. brucei enzymes were crystallized using conventional techniques in the laboratory. However, the T. cruzi enzyme was taken on board of the space shuttle in 1996 for crystallization experiments.
For this experiment the enzyme GAPDH was first brought to overexpression in the bacterium Escherichia coli by V�ronique Hannaert and Paul Michels in the group of Fred Opperdoes in Brussels. Then the purified enzyme was produced in large quantities in the laboratory of Glaucius Oliva at the University of Sao Paulo in Sao Carlos, Brazil.
This protein was then crystallized in space under conditions of micro gravity. In the first experiment in 1996, they tried to get better diffracting crystals of the protein made by the parasite, but the flight proved too short.
Experiments were continued on later flights. In NASA Space Shuttle mission STS-91 in May 1998 crystallization of T. cruzi GAPDH with flavone inhibitors isolated from the Brazilian plant Neoraputia magnifica was attempted, but only a structure of the enzyme in complex with a coumarine inhibitor was obtained. The strategy is to find a substance that will bind with a protein made by the parasite and keep it from multiplying. Finally a high resolution structure of this protein was obtained by the Brazilian crystallographers.
The other protein crystallographers of the Howard Hughes institute in Seattle (USA) in collaboration with chemists at the University of Washington and working with the same enzyme but from the related parasites T. brucei and Leishmania mexicana, succeeded to synthesize a highly specific drug that inhibited the parasite enzyme but not the corresponding enzyme of the host. This drug was then tested on live parasites and turned out to kill both T. cruzi, T. brucei and L. mexicana, without affecting the human host cells. This story demonstrates how scientists when they join all possible efforts may succeed in developing new drugs that can be of benefit to the poorest people.
-------------------------------------------------------------------------------- Created by Fred R. Opperdoes on 5 Dec, 2000
-------------------- Do unto others as you would have them do unto you. Remember Iam not a Doctor Just someone struggling like you with Tick Borne Diseases.
posted
My NY LLMD suggested Glycine as part of a liver detox combination which also includes ALA, NAC and Vit C.
I can't find Glycine in any health stores here though (Ireland). Does anyone know if it is available in most health stores in the States, or know of a good online source for it?
Thanks Elaine
Posts: 261 | From Herx-ville!! | Registered: Aug 2006
| IP: Logged |
Marnie
Frequent Contributor (5K+ posts)
Member # 773
posted
Peptidoglycan (PG), an essential cell wall polymer of most bacteria, has been isolated from many species of spirochetes.
Our interest in the host response to Borrelia burgdorferi led us to isolate and characterize its PG .
Extracted cells were solubilized with warm 1% SDS followed by digestion with proteases.
Amino acid analysis of the isolated PG demonstrated the presence of alanine, glycine, glutamic acid, and ornithine as occurs in other spirochetes and bacteria .
Intense erythematous reactions were observed after id injection of 10 micrograms of PG into normal human skin. PG was not mitogenic for human peripheral blood mononuclear cells. Murine splenocytes of certain strains responded to the PG, but only at concentrations of 25 micrograms/ml or more.
PG stimulated macrophages to produce interleukin 1.
Sixteen micrograms of PG injected iv into rabbits produced biphasic fevers .
These observations on the in vitro and in vivo activities associated with the cellular components of the B. burgdorferi spirochete give further insight to how a small number of invading organisms can cause a multisystemic disease such as Lyme disease.
PMID: 2310405
Back to Rh...HUGE difference between rabbit blood and the blood of rhesus monkeys which is more like ours!
"The Rh, or rhesus, factor was discovered in 1940 by K. Landsteiner and A. S. Wiener, when they observed that an injection of blood
from a rhesus monkey into rabbits caused an antigenic reaction in the serum component of rabbit blood (see immunity).
When blood from humans was tested with the rabbit serum, the red blood cells of 85% of the humans tested agglutinated (clumped together).
The red blood cells of the 85% (later found to be 85% of the white population and a larger percentage of blacks and Asians) contained the same factor present in rhesus monkey blood; such blood was typed
Rh positive.
The term Rhesus blood group system refers to the five main Rhesus antigens (C, c, D, E and e) as well as the many other less frequent Rhesus antigens. The terms Rhesus factor and Rh factor are equivalent and refer to the Rh D antigen only."
"The proteins which carry the Rhesus antigens are transmembrane proteins, whose structure suggest that they are ion channels."
"red cell antigens cause the production of antibodies
Each red cell has > 1 million antigens. Some antigens are evenly distributed over the red cell surface, and some are distributed in clusters
In general, antigens are composed of carbohydrates, lipids, and proteins, usually a combination of any two. For example, ABH antigens are glycosphingolipids (sugars attached to a lipid backbone) and glycoproteins (sugars attached to a protein backbone)
Rh antigens are lipoproteins.
The biological role of blood group antigens is unknown, but one is presumed to exist. In a general sense, antigens obviously provide a way to distinguish between self and non-self, and thus play a role in immunity.
But this does not explain why so many blood group antigens exist.
Some antigens are associated with susceptibility or protection against diseases, but these associations are statistical and the causes are not well understood.
For example, group A people have a higher incidence of cancer of the stomach, and group O people have a higher incidence of gastric/duodenal ulcers.
On a trivial level, studies have shown that mosquitoes prefer group O blood, and group O people have a higher IQ than group A people, at least in the north of England.
One association of importance is that the Duffy phenotype Fy(a-b-), prevalent among West Africans and American blacks (68%), acts to protect against infection by certain malarial parasites."
The answer IS out there...it is just "buried" in all the current knowledge!
What a puzzle!
Posts: 9424 | From Sunshine State | Registered: Mar 2001
| IP: Logged |
Marnie
Frequent Contributor (5K+ posts)
Member # 773
posted
Treepatrol, you quoted:
"Experiments were continued on later flights. In NASA Space Shuttle mission STS-91 in May 1998 crystallization of T. cruzi GAPDH with flavone inhibitors isolated from the Brazilian plant Neoraputia magnifica was attempted, but only a structure of the enzyme in complex with a coumarine inhibitor was obtained."
Re: experiments conducted in space...
I think we need to be careful about space research versus grounded-on-earth research.
We could jump to the wrong conclusions.
Into a search engine, type in the following words (very interesting!):
space travel oxidative stress gravity
Posts: 9424 | From Sunshine State | Registered: Mar 2001
| IP: Logged |
canefan17
Frequent Contributor (5K+ posts)
Member # 22149
posted
Bump- Dr S, in his book, talks about using 2000-3000mg of glycine before bed. Says it helps with Deep REM sleep.
Anybody?
Posts: 5394 | From Houston, Tx | Registered: Aug 2009
| IP: Logged |
The Lyme Disease Network is a non-profit organization funded by individual donations. If you would like to support the Network and the LymeNet system of Web services, please send your donations to:
The
Lyme Disease Network of New Jersey 907 Pebble Creek Court,
Pennington,
NJ08534USA http://www.lymenet.org/