Investigation of the potential molecular recognition sites of two human vitamin C transporters.

Abstract

Vitamin C (L-ascorbic acid), a cofactor for numerous mammalian enzymes and a well- known antioxidant, is renowned for its range of health advantages and protective capabilities against degenerative disorders. The mechanisms regulating the cellular movement of ascorbic acid signify a primary aspect for recognising the roles played by vitamin C in human biology. The ability for this nutrient to be absorbed and occupied in cells is accomplished via the two sodium-coupled proteins, hSVCT1 and hSVCT2. The two transporters have varying roles in relation to ascorbate, nevertheless they are both rely on certain membrane targeting to achieve their essential functions. If the correct localisation for the two proteins is not found they are unable to complete their functions, leading to reduced transport capabilities. Deficiency of vitamin C in humans is fatal and has been linked with an increased chance of cancer and other degenerative diseases, therefore the two protein carriers are crucial for human health. Despite numerous studies evaluating vitamin C’s benefits for humans, detailed knowledge on the membrane targeting of the two transporters is still limited. It is unclear how these proteins react to the interaction and presence of new substances entering the human body and how this will affect their functionality. Consequently, the aim of this research is to modify the potential molecular recognition sites on the hSVCT1 and hSVCT2 genes through site directed mutagenesis. This study could therefore indicate regions on the amino acid sequences which could be fundamental for functionality for the two carriers. This knowledge would assist the growth of therapeutic strategies in fighting certain conditions and even in the production of new drugs.