New Blood Test Could Detect Heart Attacks More Quickly

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Newswise MAYWOOD, Ill. A new blood test can detect heart attacks hours faster than the current gold-standard blood test, according to a study led by Loyola University Chicago Stritch School of Medicine researchers.

The new test measures a protein that is released to the bloodstream by dying heart muscle. The protein is called cardiac myosin binding protein-C (cMyBP-C). The study found that cMyBP-C is released to the blood within just 15 minutes of cardiac damage, and rises to significant levels in three hours.

This is a potential ultra-early biomarker that could confirm whether a patient has had a heart attack, leading to faster and more effective treatment, said Sakthivel Sadayappan, PhD, senior author of the study, published in the American Journal of Physiology Heart and Circulatory Physiology.

Between 60 and 70 percent of all patients who complain of chest pain do not have heart attacks. Many of these patients are admitted to the hospital, at considerable time and expense, until a heart attack is definitively ruled out.

An electrocardiogram can diagnose major heart attacks, but not minor ones. There also are blood tests for various proteins associated with heart attacks. But most of these proteins are not specific to the heart. Elevated levels could indicate a problem other than a heart attack, such as a muscle injury.

The only protein now used in blood tests that is specific to the heart is called cardiac troponin-I. Its the gold standard for detecting heart attacks. But it takes at least four to six hours for this protein to show up in the blood following a heart attack. So the search is on for another heart attack protein that is specific to the heart.

Like troponin-I , cMyBP-C is a protein specific to the heart. But it is more readily detected because of its large molecular size and relatively high concentration in the blood. During a heart attack, a coronary artery is blocked, and heart muscle cells begin to die due to lack of blood flow and oxygen. As heart cells die, cMyBP-C breaks into fragments and is released into the blood.

Sadayappan and colleagues found that cMyBP-C levels in a group of 176 heart attack patients were more than 18 times higher than cMyBP-C levels in a control group of 153 patients who did not have heart attacks. In a separate analysis of 12 cardiac patients who underwent a procedure that mimicked a minor heart attack, researchers found that cMyBP-C levels peaked four hours after the procedure. Researchers found similar results in a porcine model of heart attack.

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New Blood Test Could Detect Heart Attacks More Quickly

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Zebrafish Discovery May Shed Light on Human Kidney Function

Released: 2/20/2014 1:00 PM EST Source Newsroom: Mayo Clinic Contact Information

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Newswise ROCHESTER, Minn. Feb. 20, 2014 Researchers say the discovery of how sodium ions pass through the gill of a zebrafish may be a clue to understanding a key function in the human kidney. The findings from a collaboration between Mayo Clinic and the Tokyo Institute of Technology appear in the online issue of the American Journal of Physiology-Regulatory, Integrative and Comparative Physiology.

The researchers discovered a protein responsible for gas exchanges in the fish gill structure. Specifically they studied and characterized the Na+/H+ (sodium/hydrogen) exchanger named NHE3, responsible for controlling sodium and hydrogen ions across the gill. The researchers also directly demonstrated that NHE3 can function as a Na+/NH4+ (sodium/ammonium) exchanger.

This is significant because the fish tends to mimic the process in humans, says Michael Romero, Ph.D., a Mayo Clinic physiologist who works in nephrology. This is the true beauty of comparative physiology- a lot of the organs function by very similar processes, down to ionic transfer.

In this case the protein allows the sodium ions to be absorbed from the forming urine while at the same time discarding waste from normally functioning cells, thus keeping the body in balance and serving as an energy saving system. The researchers say the same NHE3 protein performs a similar function in the intestine, pancreas, liver, lungs and reproductive system.

The gill is used in the fish as a transport system: sodium ions are nutrients and ammonium carries away waste. Its a key process allowing zebrafish to extract sodium ions from fresh water. In humans, NHE3 is involved in the acid-waste control system in the kidney, but there hasnt been a good analysis of that process in humans. Part of this acid-control process in the human kidney is ammoniagenesis which requires the initial part of the kidney tubule (proximal tubule) to export ammonia/ammonium. Physiologically, it has been assumed that NHE3 can perform a Na+/NH4+ exchange, but this has never been experimentally demonstrated.

Ammoniagenesis and increased renal sodium bicarbonate absorption are partly under the control of the renin-angiotensin-aldosterone system (RAAS), which means that this work enhances understanding of human hypertension. Researchers say their results in fish can be a clue or starting point for analyzing the process in people. Researchers say they hope to continue their work in other species and ultimately further describe the process in humans.

The research was funded by both institutions. Co-authors include Yusuke Ito, Akira Kato, Ph.D., and Shighisa Hirose, Ph.D., all of the Tokyo Institute of Technology; and Taku Hirata, Ph.D., of Mayo Clinic. Yusuke Ito was a visiting graduate student at Mayo Clinic. Dr. Akira Kato is a visiting research collaborator with Dr. Romero at Mayo Clinic. ### About Mayo Clinic Recognizing 150 years of serving humanity in 2014, Mayo Clinic is a nonprofit worldwide leader in medical care, research and education for people from all walks of life. For more information, visit 150years.mayoclinic.org, http://www.mayoclinic.org and newsnetwork.mayoclinic.org.

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