London, Nov 26: Better treatments could soon be available for diseases associated with disrupted circadian rhythm - the roughly 24-hour body clock a person has - thanks to research by a biochemistry student at Valparaiso University.

Keith Stayrook has made an important discovery in a class of proteins, said to play a critical role in designing better treatments for diseases associated with disrupted circadian rhythm.

The research was conducted along with Amanda Nosie, a senior from Plainfield, Indiana.

As a part of their research, Stayrook and Nosie explored the function of two receptors – REV-ERBa and REV-ERBß – belonging to a class of proteins known as nuclear hormone receptors (NHRs) that are bound and activated by hormones such as estrogen and vitamin D, thus allowing them to work.

While most NHRs are well-defined and often the targets for pharmaceutical drugs, REV-ERBa and REV-ERBß have been considered “orphans” as no known hormones – often referred to as ligands – had been identified as binding to them since their discovery two decades ago.

Now, the two researchers have found that the two receptors are indeed ligand-regulated and the discovery that the porphyrin heme behaves as a reversible activator for the receptors could help scientists design new drugs treating diseases associated with disturbed circadian rhythm, including psychiatric and metabolic disorders, as well as cancer.

During her research internship, Nosie completed a critical final experiment that confirmed heme-binding to the two receptors activated their biological functions.

Stayrook and Nosie’s paper, “Identification of Heme as the Ligand for the Orphan Nuclear Receptors REV-ERBa and REV-ERBß”, appears in the journal Nature Structural and Molecular Biology. (ANI)