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Beth Leslie, Off hand I would say that they are not related, but I am= just getting started to work on the Nicotine and nicotinamide, but I have = some info on the NADH that may be of interest. I have never formally introduced myself to this list, so here goes, = I am the mother of an autistic child, I have been relentlessly studing thi= s=20 disorder for 4 years, during the past year I learned that my father h= as Parkinsons Disease, so I have been grabbing at information on this al= so. Although there are many treatments out there, I strive to find the = safest way to help my son and father. I truely think this Thioctic Acid is g= oing to be beneficial to my father. Linda Forrests Mom TI: Efficient reduction of lipoamide and lipoic acid by mammalian thi= oredoxin r AU: Arner-ES; Nordberg-J; Holmgren-A SO: Biochem-Biophys-Res-Commun. 1996 Aug 5; 225(1): 268-74 PY: 1996 AB: Reduction of the antioxidant lipoic acid has been proposed to be = catalyzed in vivo by lipoamide dehydrogenase (LipDH) or glutathione reductase (= GR). We have found that thioredoxin reductase (TR) from calf thymus, calf liv= er, human placenta, and rat liver efficiently reduced both lipoic acid and lipo= amide with Michaelis-Menten type kinetics in NADPH-dependent reactions. In contr= ast to LipDH, lipoic acid was reduced almost as efficiently as lipoamide. Un= der equivalent conditions at 20 degrees C, pH 8.0, mammalian TR reduced l= ipoic acid by NADPH 15 times more efficiently than the corresponding NADH depend= ent reduction catalyzed by LipDH (297 min-1 for TR vs. 20.3 min-1 for Lip= DH). Moreover, TR was 2.5 times faster in reducing lipoic acid with NADPH = than in catalyzing the reverse reaction (oxidation of dihydrolipoic acid with= NADP+). In contrast, LipDH was only 0.048 times as efficient in the forward r= eaction as compared to the reverse reaction (using NADH and NAD+). We conclude t= hat all or part of the previously described NADPH-dependent lipoamide dehydrogen= ase (diaphorase) activities in mammalian systems should be attributed to = TR. Our results suggest that in mammalian cells a significant part of the therapeutically important reduction of lipoic acid is catalyzed by th= ioredoxin reductase. P, Marsden CD. Biochem Pharmacol 1996;51:983-986.=20 Nigral cell death in Parkinson's disease is associated with decreased reduced glutathione (GSH) levels, impaired complex I activity and inh= ibition of alpha-ketoglutarate dehydrogenase (alpha-KGDH) in substantia nigra= . Thioctic acid exerts antioxidant activity through a thiol-disulphide = redox couple and is an essential cofactor for alpha-KGDH. However, it is no= t known whether or not thioctic acid enters basal ganglia or exerts beneficia= l effects in Parkinson's disease. As a global measure of altered cerebr= al function, the effect of R- and S-thioctic acid on 14C-2-deoxyglucose (14C-2DG) incorporation was investigated in rats. Rats were treated w= ith either R- or S-thioctic acid (50 mg/kg IP) or 0.9% saline acutely or = for 5 days and 14C-2DG incorporation in basal ganglia was assessed. Followi= ng acute administration, R- but not S-thioctic acid caused an overall in= crease in 14C-2DG incorporation that was significant in both substantia nigr= a zona compacta and zona reticulata. R-thioctic acid also increased the incorporation of 14C-2DG in the medial forebrain bundle, thalamus, an= d red nucleus. S-thioctic acid decreased 14C-2DG incorporation in the subth= alamic nucleus, but increased it in the red nucleus. Following repeated administration, R-thioctic acid no longer increased 14C-2DG incorpora= tion in either zona compacta or zona reticulata of substantia nigra. However,= both R- and S-thioctic acid now decreased 14C-2DG incorporation in the subthalamic nucleus. The data suggest that thioctic acid does enter t= he brain and can alter neuronal activity in areas of the basal ganglia intimately associated with the motor deficits exhibited in Parkinson= =D5s disease.=20 In-reply-to: Your message dated "Fri, 24 Jan 1997 02:26:20 -0500" <[log in to unmask]> >Thank you for all the info on NADH. I have one quick qusetion (it m= ay >seem simplistic, but it's puzzling me): How/Are nicotine, nicotinam= ide, and >NADH related? >Beth Leslie >On Thu, 23 Jan 1997, Forrests Mom wrote: >> NADH FAQ's >> >> >> Q. What is NADH? >> >> A. NADH is the abbreviation for the reduced form of >> nicotinamide-adenine-dinucleotide. This reduced form contains high= energy >> hydrogen (the H in NADH) that provides energy to the cell. NADH oc= curs in >> all living cells and plays a central role in the energy production= of the >> cells(1). The more energy a cell needs, the more NADH it needs. Fo= r example, >> muscle cells and brain cells contain about 50 micrograms NADH per = gram >> tissue, heart cells 90 micrograms, red blood cells 4 micrograms(2)= . In other >> words, if you supply NADH to the body, it acts as an energy supple= ment, >> which provides the organism with additional energy. >> >> NADH occurs naturally in the muscle tissue of many animals, such a= s fish, >> poultry and cattle that are part of our diet (3). >> >> Q. What does NADH do in the body? >> >> A. NADH is the first and most energetic component in the central e= nergy >> producing mechanism in our cells(4). Thus it plays a crucial role = in >> supplying our cells with energy. >> >> In addition NADH supplies the energy for the production of importa= nt >> compounds in our cells. NADH increases the production of adrenalin= e and >> dopamine, particularly in the brain(5, 6) It improves aspects of b= rain and >> central nervous system function which are related to the activity = of >> dopamine and adrenaline. >> >> Q. How was NADH discovered? >> >> A. NADH was discovered in 1934 by Kaplan, an American scientist wh= o found >> that it plays an essential role in the energy production of cells(= 7). >> >> Q. Who should take NADH? >> >> A. Anyone that that wants to support the function of the central n= ervous >> system and the energy production in all cells. >> >> Q. Who is Georg Birkmayer? >> >> A. Professor Georg Birkmayer, MD, Ph.D., is the director of a clin= ical >> laboratory in Vienna, Austria as well as a world renowned biochemi= cal >> researcher. He is associated with the University of Vienna and is = a visiting >> professor at the University of Beijing, China. He is the general s= ecretary >> of the International Academy of Tumor Marker Oncology. In addition= to being >> a practicing physician, he is the author of more than 100 scientif= ic articles. >> >> References: >> >> 1. Lehninger, A.L. (1970): Biochemistry, Worth Publisher Inc. 1970= . >> >> 2. Klingenberg M. (1960): Zur Bedeutung der freien Nucleotide. 11.= Moosbacher >> Kolloquium Springer Verlag p. 82-114 >> >> 3. Sauberlich H.E. (1987): Nutritional Aspects of Pyridine Nucleot= ides, in >> Dolphin D, Poulson R., Avramovic O. (editors): Pyridine Nucleotide= Coenzymes >> (Part B), John Wiley & Sons, Inc. 1987, p. 599-626 >> >> 4. Alberts B, et al (1983): Molecular Biology of the Cell, Garland >> Publishing, 1983, p. 491-495. >> >> 5. Vrecko K., Birkmayer JGD and Krainz J. (1993): Stimulation of d= opamine >> biosynthesis in cultured PC12 phaeochromocytoma cells by the coenz= yme >> nicotinamide adenine dinucleotide (NADH), J. Neur. Trans. 5:147-15= 6 >> >> 6. Gardier M. (1994) Study Report to Labor Birkmayer, Department >> Pharmacology, University Paris Sud. >> >> 7. Kaplan N.O. (1960) in Boyer PD, Lardy H. and Myrbaeck K.: The E= nzymes >> Vol. 3, Ac Press New York p. 156-172 >> >> Colloidal NaDH, Order Form >> >> Home Page >> ------------------------------------------------------------------= ------ >> >> >> Copyright =A91996 by Chronic Wellness International=99 >> >> Last Updated 11/03/96 >>