A Novel Oxygen Delivery Therapeutic Recovered the Function of Low Oxygen Heart Tissue in an Animal Model of Global Hypoxia in New Studies at UC San Francisco. The study was published in the Journal of PLOS Biology. For body tissues, lack of oxygen is a great danger, especially to the heart. Such hypoxic conditions can lead to long-lasting tissue damage or even heart attacks.
The new drug, called OMX-CV, unlike its experimental predecessors, does not seem to cause any systemic side effects or be toxic to cause excessive blood oxygenation. Instead, the new drug delivered its precious oxygen charge only to the tissues that need it most.
Emin Maltepe, co-senior author of the newspaper, said that any tissue with impaired blood flow, whether due to trauma, stroke or cardiovascular disease such as coronary heart disease, can starve and starve the heart of oxygen Adult heart failure or heart attacks trigger, but also hypoxia in the heart is a problem in children. According to the Centers for Disease Control and Prevention (CDC), every year around 1
Under normal conditions, the heart consumes more oxygen than any other organ, and when the oxygen content is low; his demand increases even higher. The hypoxic heart pumps harder to deliver oxygen to the rest of the body and, paradoxically, requires more and more oxygen itself to maintain function. An oxygen-providing drug such as OMX-CV could alleviate the physical stress of hypoxia and improve recovery from heart attacks or open heart surgery in adults and children.
Hemoglobin-based drugs have also proven to be too good at work: they tend to flood the blood with excess oxygen, which can itself cause serious tissue damage. In addition, when outside the confines of a red blood cell, hemoglobin can take up nitric oxide, a natural muscle relaxant found in blood vessels. Vessels that have been deprived of nitric oxide contract, causing blood pressure to rise, increasing the risk of heart attack and reducing blood flow to key organs such as the kidneys.
OMX-CV avoids these problems by using a manipulated bacterial protein called H-NOX as its basis, rather than hemoglobin. H-NOX proteins contain a "co-factor", a heme group – the same co-factor that gives hemoglobin its name – that allows the protein to bind not only oxygen but also nitric oxide. By changing the chemical structure of H-NOX proteins, Omniox scientists have reshaped them to adhere closely to oxygen but leave nitric oxide alone. The researchers also showed that the modified proteins bind oxygen so tightly that they only give up when they hit a highly hypoxic tissue.
Published: October 20, 2018 8:05 pm