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New ways for heart treatment | A new American study has suggested new ways to improve heart treatment. The study, led by University
of Iowa scientists, demonstrated in theory, that it might be possible to use drugs
that maintain the positive effects on heart function of a known enzyme called
calmodulin kinase II (CaM kinase) while reducing its negative effects. Mark E.
Anderson, professor and head of internal medicine at the University of Iowa Roy
J. and Lucille A. Carver College of Medicine, said: "CaM kinase helps regulate
calcium, which is essential to heart function, but CaM kinase's calcium connection
also can play a role in electrical problems that lead to irregular heart beats
and cell death. This new finding suggests a specific way to keep the wanted CaM
kinase effects but at the same time eliminate the bad effects. "Most patients
with heart failure are at risk of sudden death. Figuring out how and why heart
failure happens is a major goal for academic medicine." CaM kinase adds phosphate
groups to other proteins, a process known as phosphorylation. This process can
activate proteins and set in motion or sustain cell activity. Anderson, who also
is a member of the University of Iowa Heart and Vascular Center , said: "The study
showed, surprisingly, the importance of CaM kinase's effect on two particular
amino acid targets among the thousands of amino acids that make up protein targets
for phosphorylation by CaM kinase. Controlling these targets might prevent the
'ripple effect' of other molecular events that result in arrhythmia and cell death."
For the study, researchers used rabbit heart cells, which behave much like human
heart cells, and demonstrated that if CaM kinase is prevented from interacting
with a protein that regulates calcium channels, negative effects, including cell
death, do not occur. In particular, they showed it was possible to either block
the specific site on the protein where CaM kinase binds or block the ability of
CaM kinase to perform phosphorylation on the protein. In both cases, blocking
the action of CaM kinase prevented too much calcium activity, which can be harmful.
Anderson said: " CaM kinase is needed to maintain calcium channel function, which
allows the heart to contract. But too much CaM kinase, and consequently too much
calcium entry into heart cells, causes electrical instability and other downstream
molecular problems that can lead to cell overload and cell death, which causes
heart failure." Researchers from Vanderbilt University also took part in the study,
which has appeared in the Early Online Edition of the Proceedings of the National
Academy of Sciences. |
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