Functional Regulation of the Plasma Protein Histidine-Rich Glycoprotein by Zn in Settings of Tissue Injury

Overview

Journal Biomolecules

Publisher MDPI

Specialties Biochemistry
Molecular Biology

Date 2017 Mar 4

PMID 28257077

Citations 14

Authors

Kristin M Priebatsch

Marc Kvansakul

Ivan K H Poon

Mark D Hulett

Affiliations

Soon will be listed here.

Abstract

Divalent metal ions are essential nutrients for all living organisms and are commonly protein-bound where they perform important roles in protein structure and function. This regulatory control from metals is observed in the relatively abundant plasma protein histidine-rich glycoprotein (HRG), which displays preferential binding to the second most abundant transition element in human systems, Zinc (Zn). HRG has been proposed to interact with a large number of protein ligands and has been implicated in the regulation of various physiological and pathological processes including the formation of immune complexes, apoptotic/necrotic and pathogen clearance, cell adhesion, antimicrobial activity, angiogenesis, coagulation and fibrinolysis. Interestingly, these processes are often associated with sites of tissue injury or tumour growth, where the concentration and distribution of Zn is known to vary. Changes in Zn levels have been shown to modify HRG function by altering its affinity for certain ligands and/or providing protection against proteolytic disassembly by serine proteases. This review focuses on the molecular interplay between HRG and Zn, and how Zn binding modifies HRG-ligand interactions to regulate function in different settings of tissue injury.

Citing Articles

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