Online ISSN: 2515-8260

Keywords : Amyloids


S. Vidyashri; Jayalakshmi Somasundaram; MP Brundha

European Journal of Molecular & Clinical Medicine, 2020, Volume 7, Issue 1, Pages 1520-1528

The objective of this article is to provide an overview on the association between Prion proteins and diabetes mellitus which is important so as to understand the aetiology of diabetes mellitus and provide better treatment plans. Prions are misfolded proteins Which have the ability to transmit their misfolded structure to normal variants of the same protein. Prions form abnormal aggregates of protein known as amyloids. Islet amyloid polypeptide, IAPP, is a precursor protein which causes islet amyloid polypeptide amyloidosis, AIAPP, and is said to lead to type two diabetes. Prion aggregates are generally stable and resist proteolysis. Diabetes mellitus is a group of metabolic disorders characterised by high blood sugar level over a long period of time. It is mainly caused by insulin deficiency or resistance. Prion mediated diseases are generally neurodegenerative disorders such as Kuru, Parkinson's disease, Alzheimer's disease etc. There are two isoforms of prions which are PrP and PrPSc. PrPSc is the infective form and is capable of converting PrPC into infective state. In this review, we discuss the association of prion protein with diabetes mellitus, the structure and propagation of Prion proteins and the link between diabetes mellitus and other prion mediated diseases via cross seeding. A review has been done in order to understand and analyse the association between prion protein and diabetes mellitus by retrieving a minimum of 20 articles from various data search engines including pubmed, Google scholar, MESH, core, bioRXiv, Semantic scholar and so on. This review gives a clear understanding of prion proteins, their structure, propagation and disease causing abilities. It is also analyzed that diabetes mellitus could not be just a disease which is caused by insulin deficiency or resistance but could also be the consequence of protein misfolding.