Effect of Mercury on Membrane Proteins, Anionic Transport and Cell Morphology in Human Erythrocytes.
Anion Exchange Protein 1, Erythrocyte
/ metabolism
Ankyrins
/ metabolism
Annexin A5
/ metabolism
Cysteine
/ metabolism
Environmental Pollutants
Erythrocytes
/ metabolism
Humans
Membrane Proteins
/ metabolism
Mercury
/ metabolism
Phosphatidylserines
/ metabolism
Phospholipids
/ metabolism
Sulfates
/ metabolism
Ankyrin; Anionic transport; Erythrocytes; Flotillin-2; Mercury
Journal
Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology
ISSN: 1421-9778
Titre abrégé: Cell Physiol Biochem
Pays: Germany
ID NLM: 9113221
Informations de publication
Date de publication:
21 Sep 2022
21 Sep 2022
Historique:
accepted:
03
09
2022
entrez:
20
9
2022
pubmed:
21
9
2022
medline:
24
9
2022
Statut:
ppublish
Résumé
Mercury (Hg) is a heavy metal widespread in all environmental compartments as one of the most hazardous pollutants. Human exposure to this natural element is detrimental for several cellular types including erythrocytes (RBC) that accumulate Hg mainly bound to the SH groups of different cellular components, including protein cysteine residues. The cellular membrane represents a major target of Hg-induced damage in RBC with loss of physiological phospholipid asymmetry, due to phosphatidylserine (PS) exposure to the external membrane leaflet. To investigate Hg-induced cytotoxicity at the molecular level, the possible interaction of this heavy metal with RBC membrane proteins was investigated. Furthermore, Hg-induced alterations in band 3 protein (B3p) transport function, PS-exposing macrovesicle (MVs) formation and morphological changes were assessed. For this aim, human RBC were treated in vitro with different HgCl Findings presented in this paper indicate that RBC exposure to HgCl Altogether, the findings reported in this paper confirm that RBC are particularly vulnerable to Hg toxic effect and provide new insight in the Hg-induced protein modification in human RBC affecting the complex biological system of cellular membrane. In particular, Hg could induce dismantle of vertical cohesion between the plasma membrane and cytoskeleton as well as destabilization of lateral linkages of functional domains. Consequently, decreased membrane deformability could impair RBC capacity to deal with the shear forces in the circulation increasing membrane fragmentations. Furthermore, findings described in this paper have also significant implication in RBC physiology, particularly related to gas exchanges.
Sections du résumé
BACKGROUND/AIMS
OBJECTIVE
Mercury (Hg) is a heavy metal widespread in all environmental compartments as one of the most hazardous pollutants. Human exposure to this natural element is detrimental for several cellular types including erythrocytes (RBC) that accumulate Hg mainly bound to the SH groups of different cellular components, including protein cysteine residues. The cellular membrane represents a major target of Hg-induced damage in RBC with loss of physiological phospholipid asymmetry, due to phosphatidylserine (PS) exposure to the external membrane leaflet. To investigate Hg-induced cytotoxicity at the molecular level, the possible interaction of this heavy metal with RBC membrane proteins was investigated. Furthermore, Hg-induced alterations in band 3 protein (B3p) transport function, PS-exposing macrovesicle (MVs) formation and morphological changes were assessed.
METHODS
METHODS
For this aim, human RBC were treated in vitro with different HgCl
RESULTS
RESULTS
Findings presented in this paper indicate that RBC exposure to HgCl
CONCLUSION
CONCLUSIONS
Altogether, the findings reported in this paper confirm that RBC are particularly vulnerable to Hg toxic effect and provide new insight in the Hg-induced protein modification in human RBC affecting the complex biological system of cellular membrane. In particular, Hg could induce dismantle of vertical cohesion between the plasma membrane and cytoskeleton as well as destabilization of lateral linkages of functional domains. Consequently, decreased membrane deformability could impair RBC capacity to deal with the shear forces in the circulation increasing membrane fragmentations. Furthermore, findings described in this paper have also significant implication in RBC physiology, particularly related to gas exchanges.
Substances chimiques
Anion Exchange Protein 1, Erythrocyte
0
Ankyrins
0
Annexin A5
0
Environmental Pollutants
0
Membrane Proteins
0
Phosphatidylserines
0
Phospholipids
0
Sulfates
0
Mercury
FXS1BY2PGL
Cysteine
K848JZ4886
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
500-513Subventions
Organisme : Fondation SRTS-VD (Service Régional de Transfusion Sanguine - Vaud)
Pays : Switzerland
Commentaires et corrections
Type : ErratumIn
Informations de copyright
© Copyright by the Author(s). Published by Cell Physiol Biochem Press.
Déclaration de conflit d'intérêts
The authors have no conflicts of interest to declare.