At present, there are also many different types of treatment for heart disease. The success of treatment often depends on early diagnosis. The symptoms of heart disease vary depending on the type of heart disease. Modern medicine has made tremendous advances in the recent years and the research is still going on.
Recently researchers at the Indiana University and Stanford University Schools of medicine have found a new class of drugs, that lessen the muscle damage caused by heart attacks. Thomas Hurley, Ph.D., together with his team found a compound, Alda-1, which assist in restoring the function of a key enzyme, ALDH2. ALDH2 also known as Aldehyde dehydrogenase 2, is a human gene found on chromosome 12. The enzyme encoded by this gene belongs to the aldehyde dehydrogenase family of enzymes which catalyze the chemical transformation from acetaldehyde to acetic acid. Aldehyde dehydrogenase is the second enzyme of the major oxidative pathway of alcohol metabolism. It plays a vital role in metabolizing alcohol and other toxins, including those created by a lack of oxygen in the wake of a heart attack. Furthermore, it is involved in the metabolism of nitroglycerin, which is used to prevent chest pain (angina) caused by restricted blood flow and oxygen to the heart.
According to some reports, though some people, including about 40 percent of people of East Asian descent, carry a mutated form of the ALDH2 enzyme that does not carry out its intended functions well. People with the mutated form of the enzyme are at increased risk of cardiovascular damage. Previously in 2008, the IU and Stanford team reported that Alda-1 bypassed the body’s usual signaling system and activated the ALDH2 enzyme directly, reducing damage to heart muscle tissue. That finding raised the possibility of new treatments for heart attacks, methods to protect hearts during open heart surgery, and other situations in which blood flow is interrupted.
The current study states that Alda-1 activates the ALDH2 enzyme in a process wherein Alda-1 attaches to the ALDH2 enzyme at a crucial spot and acts like a shim or wedge to prop it up. A mutation to normal gene would make it dysfunctional because a mutation in the gene causes the parts of the protein structure become loose or altered. Dr. Hurley, director of the Center for Structural Biology on the Indiana University-Purdue University Indianapolis campus, says that determining how the Alda-1 compound works will enable the researchers to begin working on alternative compounds that hold more promise as potential drugs. One primary improvement needed is the ability to give the drug orally, rather than by injection. The team forsee that the alternative compound could be available for testing by mid-2010.