Year: 2013
Type: article
Abstract: Human serum albumin (HSA) has been used for a long time as a resuscitation fluid in critically ill patients. It is known to exert several important physiological and pharmacological functions. Among them, the antioxidant properties seem to be of paramount importance as they may be implied in the potential beneficial effects that have been observed in the critical care and hepatological settings. The specific antioxidant functions of the protein are closely related to its structure. Indeed, they are due to its multiple ligand-binding capacities and free radical-trapping properties. The HSA molecule can undergo various structural changes modifying its conformation and hence its binding properties and redox state. Such chemical modifications can occur during bioprocesses and storage conditions of the commercial HSA solutions, resulting in heterogeneous solutions for infusion. In this review, we explore the mechanisms that are responsible for the specific antioxidant properties of HSA in its native form, chemically modified forms, and commercial formulations. To conclude, we discuss the implication of this recent literature for future clinical trials using albumin as a drug and for elucidating the effects of HSA infusion in critically ill patients.
Source: Annals of Intensive Care
Institutions: Université Paris-Sud, Centre National de la Recherche Scientifique, Université Paris-Saclay, Institut Galien Paris-Saclay, Inserm, Sorbonne Paris Cité, Hôpital Cochin, Assistance Publique – Hôpitaux de Paris, Groupe Hospitalier Cochin - Port-Royal, Hôtel-Dieu, Broca - La Collégiale, Institut Cochin, Université Paris Descartes, Hôpital Saint-Antoine, Université Pierre-et-Marie-Curie
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,490
OpenAlex ID: W2165988110