Pathophysiology, The Biochemical And Clinical Significance Of Lactate Dehydrogenase
Mohammed Hasan Barrak, F. Dawood, Safa Nihad Abed Shubar, Ali A. Al-fahham
Abstract
Lactate dehydrogenase (LDH) is a family of enzymes that catalyzes oxidation-reduction enzymes, the interconversion between pyruvic acid and lactic acid. It is an enzyme that terminates the final catabolic reaction in which glucose id hydrolyzes anaerobically (glycolysis) resulting in lactate from pyruvate. These varied biochemical characteristics significantly influence its specificity to cells, tissues, and organs. Although LDH is mainly found in the cytoplasm, it is also located in multiple organelles. The presence of blood LDH implies an enzyme marker, and it may be a sign of death for many conditions such as ARDS, severe COVID-19, and some cancers. When LDH levels in the blood are increased they can reflect liver disease or anemia plus heart attack in addition to bone fracture — and muscle trauma. This also includes cancerous formations; infections like encephalitis or meningitis — along with HIV.