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Diabetes vaccine / iron
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Martin McGowan
medicine forum beginner


Joined: 18 Jun 2006
Posts: 2

PostPosted: Thu Jun 22, 2006 7:53 am    Post subject: Re: Diabetes vaccine / iron Reply with quote

Gordon Burditt wrote:
Quote:
Nope, not even close. Even though a common protein was mentioned in both
abstracts, the biology they describe are very very different. They do
support my theory because oxygen was involved in both processes then
oxygen is the cause of all disease. Iron was involved in only one
abstract as an effect only. You cann't connect dots with a spray gun.

Is this another example of the evils of dihydrogen monoxide?

Gordon L. Burditt
Oh no, you haven't been taking dihydrogen monoxide, did your parents

not warn you of the dangers from poisoning, suffocation, oh yes and
rust too if linked with the ferrous molecule.
if you have been taking dihydrogen monoxide please stop, it's
involved with every danger up to and including death.
Martin McGowan
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Gordon Burditt
medicine forum beginner


Joined: 04 May 2005
Posts: 5

PostPosted: Wed Jun 21, 2006 6:35 pm    Post subject: Re: Diabetes vaccine / iron Reply with quote

Quote:
Nope, not even close. Even though a common protein was mentioned in both
abstracts, the biology they describe are very very different. They do
support my theory because oxygen was involved in both processes then
oxygen is the cause of all disease. Iron was involved in only one
abstract as an effect only. You cann't connect dots with a spray gun.

Is this another example of the evils of dihydrogen monoxide?

Gordon L. Burditt
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BJ in Texas
medicine forum beginner


Joined: 19 Jul 2005
Posts: 15

PostPosted: Wed Jun 21, 2006 12:42 pm    Post subject: Re: Diabetes vaccine / iron Reply with quote

babawali@world.com wrote:
|| Nope, not even close. Even though a common protein was
|| mentioned in both abstracts, the biology they describe are
|| very very different. They do support my theory because
|| oxygen was involved in both processes then oxygen is the
|| cause of all disease. Iron was involved in only one abstract
|| as an effect only. You cann't connect dots with a spray gun.

Gawd, just think if they removed oxygen from the atmosphere
it would go away with most all diseases.

--
--
"If you pick up a starving dog and make him prosperous, he will
not bite you; that is the principal difference between a dog and
a man." -- Mark Twain

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babawali@world.com
medicine forum addict


Joined: 29 Apr 2006
Posts: 81

PostPosted: Wed Jun 21, 2006 12:33 am    Post subject: Re: Diabetes vaccine / iron Reply with quote

Nope, not even close. Even though a common protein was mentioned in both
abstracts, the biology they describe are very very different. They do
support my theory because oxygen was involved in both processes then
oxygen is the cause of all disease. Iron was involved in only one
abstract as an effect only. You cann't connect dots with a spray gun.
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ironjustice@aol.com
medicine forum Guru


Joined: 28 Apr 2005
Posts: 1522

PostPosted: Wed Jun 21, 2006 12:33 am    Post subject: Diabetes vaccine / iron Reply with quote

<<snip>>
HSP60, is able to shut down the autoimmune response causing this
disorder
<<snip>>
<<snip>>
Hsp60 prevents the release of iron ions
<<snip>>

Public release date: 19-Jun-2006


Contact: Jennifer Manning
jennifer@acwis.org
212-895-7952
American Committee for the Weizmann Institute of Science

The molecular mechanism of a diabetes vaccine revealed
A team of researchers led by Prof. Irun Cohen of the Weizmann Institute
of Science Immunology Department has revealed the molecular mechanism
of a vaccine for Type 1 diabetes. The new findings should help amplify
the effectiveness of the vaccine, which is currently in advanced stages
of clinical trials. Type 1 diabetes is an autoimmune disorder in which
the immune system mistakenly attacks the body's own insulin-producing
pancreatic cells, reducing and ultimately eliminating the production of
insulin - a hormone needed to convert sugar, starches, and other
foods into energy.
Several years ago, Prof. Cohen and colleagues developed a vaccine that
arrests the progression of Type 1 diabetes in laboratory animals. They
had discovered that a particular protein called HSP60, or even only a
small particular fragment of it - the peptide designated p277 - is
able to shut down the autoimmune response causing this disorder. The
vaccine is currently being tested in clinical trials in Europe and the
United States, but its precise mechanism has until now been unknown.

"When translating these findings into a practical vaccine, we knew
enough about the mechanism to understand that this protein is able to
cause a decrease in the immune response, but how it actually works
eluded us," says Cohen. In a paper published in the Journal of Clinical
Investigation, the scientists have managed to identify the exact immune
cells that p277 acts upon and its mechanism of action.

Autoimmune diseases occur when certain T cells in the immune system
attack the body's own cells and tissues. The scientists discovered that
p277 directs the activity of the immune system in two ways. First, the
p277 peptide steps up the activities of a different type of T cell that
regulates the amount of potentially harmful T cells available. In
addition, T cells treated with p277 cause the delinquent T cells to
secrete anti-inflammatory substances instead of the
inflammation-causing ones that they usually make which lead to
autoimmune disease. This double action of the peptide weakens the
damaging activities of the immune response further. The scientists also
showed that in order to activate this response, p277 must be bound to
the receptor TLR-2, which is found on the cell walls of the regulatory
T cells.

"These findings are important, as it means that by identifying the
molecular activity of p277 with such precision, we can copy nature's
own system in regulating the immune system and therefore, help to boost
the immune system in preventing the destruction of insulin-producing
pancreatic cells," says Cohen.

Postdoctoral fellow Dr. Alexandra Zanin-Zhorov spearheaded the project;
the other scientists participating in this study were: the late Prof.
Ofer Lider, Dr. Liora Cahalon, postdoctoral fellow Guy Tal, and Raanan
Margalit.


###
Prof. Irun Cohen's research is supported by the Minna James Heineman
Stiftung; and the Robert Koch Minerva Center for Research in Autoimmune
Disease.

Prof. Cohen is the incumbent of the Helen and Morris Mauerberger
Professorial Chair in Immunology.


--------------------------------------------------------------------------------


J Biol Chem. 2002 Nov 15;277(46):44531-8. Epub 2002 Aug 27. Related
Articles, Links


Mitochondrial Hsp60, resistance to oxidative stress, and the labile
iron pool are closely connected in Saccharomyces cerevisiae.

Cabiscol E, Belli G, Tamarit J, Echave P, Herrero E, Ros J.

Departament de Ciencies Mediques Basiques, Facultat de Medicina,
Universitat de Lleida, Spain.

In the present study, we have analyzed the role of the molecular
chaperone Hsp60 in protection of Saccharomyces cerevisiae against
oxidative damage. We constructed mutant strains in which the levels of
Hsp60 protein, compared with wild-type cells, were four times greater,
and the addition of doxycycline gradually reduces them to 20% of
wild-type. Under oxidative-stress conditions, the progressive decrease
in Hsp60 levels in these mutants resulted in reduced cell viability and
an increase in both cell peroxide species and protein carbonyl content.
Protection of Fe/S-containing enzymes from oxidative inactivation was
found to be dose-dependent with respect to Hsp60 levels. As these
enzymes release their iron ions under oxidative-stress conditions, the
intracellular labile iron pool, monitored with calcein, was higher in
cells with reduced Hsp60 levels. Consistently, the iron chelator
deferoxamine protected low Hsp60-expressing cells from both
oxidant-induced death and protein oxidation. These results indicate
that the role of Hsp60 in oxidative-stress defense is explained by
protection of several Fe/S proteins, which prevent the release of iron
ions and thereby avert further damage.

PMID: 12200437 [PubMed - indexed for MEDLINE]

--------------------------------------------------------------------------------


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