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Polyadenosine Diphosphate–Ribose Polymerase Inhibition Modulates Skeletal Muscle Injury Following Ischemia Reperfusion—Invited Critique

Polyadenosine Diphosphate–Ribose Polymerase Inhibition Modulates Skeletal Muscle Injury Following... Invited Critique f you are one of those surgeons who believes that Darwin was correct, then you must also trust the constructive forti- I tude of an enzyme that has survived millennia of evolutionary hurdles. It must be doing something good. And the thera- peutic arrogance of selectively inhibiting this enzymatic hall-of-famer should be dangerous—like challenging the pope on scripture. But, in this issue of the ARCHIVES, this is exactly what Hua et al have done. Polyadenosine diphosphate–ribose polymerase is a DNA repair enzyme that is concentrated in cellular royalty (like heart, brain, and skeletal muscle), while PARP is essentially absent in cellular foot soldiers (like white cells). The body is not a democracy. Polyadenosine diphosphate–ribose polymerase requires energy to accomplish its repair work; so, it makes sense that we invest in the nuclear repair of terminally differentiated cells rather than squandering remorse on a bunch of granu- locytes that will die soon anyway. So, how did Hua et al contrive a circumstance in which fueling repair machinery proved counterproductive? In an el- egant series of studies these investigators depleted PARP both pharmacologically and by genetic deletion. No one believes that even the most “selective inhibitor” has no adverse http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png JAMA Surgery American Medical Association

Polyadenosine Diphosphate–Ribose Polymerase Inhibition Modulates Skeletal Muscle Injury Following Ischemia Reperfusion—Invited Critique

JAMA Surgery , Volume 140 (4) – Apr 1, 2005

Polyadenosine Diphosphate–Ribose Polymerase Inhibition Modulates Skeletal Muscle Injury Following Ischemia Reperfusion—Invited Critique

Abstract

Invited Critique f you are one of those surgeons who believes that Darwin was correct, then you must also trust the constructive forti- I tude of an enzyme that has survived millennia of evolutionary hurdles. It must be doing something good. And the thera- peutic arrogance of selectively inhibiting this enzymatic hall-of-famer should be dangerous—like challenging the pope on scripture. But, in this issue of the ARCHIVES, this is exactly what Hua et al have done. Polyadenosine...
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Publisher
American Medical Association
Copyright
Copyright 2005 American Medical Association. All Rights Reserved. Applicable FARS/DFARS Restrictions Apply to Government Use.
ISSN
2168-6254
eISSN
2168-6262
DOI
10.1001/archsurg.140.4.352
Publisher site
See Article on Publisher Site

Abstract

Invited Critique f you are one of those surgeons who believes that Darwin was correct, then you must also trust the constructive forti- I tude of an enzyme that has survived millennia of evolutionary hurdles. It must be doing something good. And the thera- peutic arrogance of selectively inhibiting this enzymatic hall-of-famer should be dangerous—like challenging the pope on scripture. But, in this issue of the ARCHIVES, this is exactly what Hua et al have done. Polyadenosine diphosphate–ribose polymerase is a DNA repair enzyme that is concentrated in cellular royalty (like heart, brain, and skeletal muscle), while PARP is essentially absent in cellular foot soldiers (like white cells). The body is not a democracy. Polyadenosine diphosphate–ribose polymerase requires energy to accomplish its repair work; so, it makes sense that we invest in the nuclear repair of terminally differentiated cells rather than squandering remorse on a bunch of granu- locytes that will die soon anyway. So, how did Hua et al contrive a circumstance in which fueling repair machinery proved counterproductive? In an el- egant series of studies these investigators depleted PARP both pharmacologically and by genetic deletion. No one believes that even the most “selective inhibitor” has no adverse

Journal

JAMA SurgeryAmerican Medical Association

Published: Apr 1, 2005

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