The newly-discovered relation of haemoglobin to the distribution of nitric oxide in the body could lead to treatments for blood pressure related disorders
HAEMOGLOBIN, the ubiquitous component of red blood cells (RBC), known to
be a transporter of gases - ferrying
oxygen from the lungs to tissues and
carbon dioxide (c02) on the return
journey - has been found to distribute
a third gas on its rounds through the
body. This gas is nitric oxide (NO),
according to a team of researchers from
Duke University Medical School, us, led
by Jonathan Stamler.
NO, though known as a noxious gas
in nature, is important in keeping cells
and tissues alive. The cells which line
blood vessels release NO in adjoining tissues. The gas has a relaxing effect on
muscle cells and thus can increase blood
flow. NO, hence, plays a role in altered
blood flow at specific sites and also in
related biological functions like
memory formation, blood pressure and
sexual erection.
Each haernoglobin sub-unit cradles
an atom of iron which has a strong
affinity for oxygen. The researchers isolated another component of haemoglobin, a segment of its protein chain called
the cysteine residue, that can hold and
release No at cellular sites. Haemoglobin
thus directly controls the ability to regulate local levels Of NO in the circulatory
system according to need. "People
thought that they knew everything there
was to know about haemoglobin. That it
has another basic function is a stunning
revelation," said Stamler.
A question Stamler's team members
asked themselves was how muscle cells
got their necessary fix of,nitric acid.
When No acquires an extra electron, the
Duke researchers observed, it takes on
an altogether different chemistry. The
more energetic NO molecules, dubbed
'super' No by the scientists, bind to the
tail of the amino acid called cysteine,
present in the beta units of a haemoglobin molecule. Stamler and his colleagues
Li Jia and Joseph Bonaventura found
that super NO is indeed present in the
blood cells as they leave the lungs, but
not in those returning to the lungs from
the tissues. This implies that super NO is
formed in the lungs and transported to
the tissues. The team is now trying hard
to find out the details of the mechanism.
This new discovery calls for a major
revision in all textbook pictures of the
respiratory cycle. When an RBc enters
the lungs, its haemoglobin molecules
release C02 and pick up oxygen and super NO. The RBC travel through the
arteries and the, tiny capillaries where
oxygen is released. Free of oxygen, the
iron atoms trap any local excess Of NO
making the blood vessels contract.
Wherever necessary, super NO is
released and the blood vessels expand.
The RBc returning to the lungs dump
the co2 and NO picked up from the tissues and get recharged with oxygen and
super No; the cycle continues in a like
manner.
Though the experiments at the
Duke Medical School were performed
on rats, Stamler believes that the same
results would be found in human tissues
because of the basic physiological similarities between rats and humans. The
new finding suggests solutions to several
medical mysteries. When the heart is
deprived of oxygen - the most common cause of a heart attack - it also
lacks in super NO. A @dose Of NO-rich
haernoglobin may help restore the natural balance and ward off initial attacks.
The most important fallout of the
new research, opines Nobel prize-winner Max Perutz of the molecular biology
department of Cambridge University,
UK (who discovered the crystal structure
of haemoglobin) would be new ways to
control blood pressure related diseases.
A time may come when haemoglobin
doped with the right amount Of NO can
work like the proverbial magic potion to
treat high blood pressure cases.
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