Glycosylation as a factor in the iron transport mechanism of human serum transferrin


The proposed fundamental research of transferrin, the principal iron-transporting protein in the human body, and the impact of its glycosylation pattern on the equilibrium and kinetics of iron binding has the following scientific objectives: 1. determination of the iron-binding equilibrium constants for transferrin glycoforms, 2. determination of the reduction potential of iron bound to transferrin glycoforms, and 3. determination of the kinetics and mechanism of iron binding and release from transferrin glycoforms.

Most transferrins are soluble glycoproteins consisting of a single chain of 700 amino acid residues and heterogeneous glycan structures. Physiological or pathophysiological changes in the organism lead to post-translational changes in the glycosylation of transferrin, resulting in the significantly increased levels of desialylated transferrin. Changes in relatively large glycan structures of transferrin may have a significant effect on the iron-binding constant and may also affect binding to the target cell receptors. The iron binding and release mechanism is associated with its reduction potential that depends on various factors (e.g. pH, synergic anion, etc.). Any alteration of the transferrin glycosylation pattern can result in changes in the reduction potential as well as the kinetics of iron binding or release.

This project will facilitate scientific excellence and development of independent research careers of young scientists by increasing employment and improving their working conditions in terms of equipment and other resources or by removing obstacles to their mobility. Implementation of the project will also strengthen the capacity of young scientists to withdraw financial resources from EU funds and other sources and thus ensure the sustainability and expansion of the established research group’s scientific activity.

HRZZ UIP-2017-05-9537

Home        Team        Research        Collaborations        Activities        Publications

Leader: doc. dr. sc. Tin Weitner

HRZZ project UIP-2017-05-9537

February 1, 2018 – January 31, 2023