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
>> ------------------------------------------------------------------=
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>>
>>
>> Copyright =A91996 by Chronic Wellness International=99
>>
>> Last Updated 11/03/96
>>