Effect of hypoxia on the composition and state of lipids and oxygen-transport properties of erythrocyte haemoglobin

Abstract

The aim of this study was to investigate the relationship between the composition and state of erythrocytic lipids and oxygen-binding properties of erythrocyte haemoglobin-derived haematoporphyrin under hypoxia. The results from this study showed that hypoxia causes a profound change in the composition of the lipids that form the bilayer of erythrocyte membranes, as well as in the functional characteristics of erythrocytes. The detected changes correlate with morphological reconstruction of erythrocytes and, consequently, affect the oxygen-transport properties of erythrocytes. The obtained results showed that the lipid phase plays an important role in the functioning of erythrocytes in health as well as in event of development of ischemic heart disease and other pathological processes that accompany hypoxia.

Raman spectroscopy as a novel method in placental research: Recognizing the pattern of placental hypoxia

“…The hypoxic treatment of placenta ex vivo in our study represents the models, mimicking pre‐eclampsia (PE) [10a] ; interestingly, these spectra are similar to the Raman shift, reported for human normal and pre‐eclamptic placentas and blood samples from women with PE . The Raman peak of 1,129 cm −1 was quite close to 1,127 cm −1 hemoglobin‐derived hemoporfirin shift reported in exposed to hypoxia erythrocytes and myocardium and the same as found in placentas from women suffering from PE . 1,128 cm −1 Raman shift was identified for myristic acid, which has also chain vibration expansion shift of 414 cm −1 —close to detected in our study 415 cm −1 .…”

Effects of Polyphenol Compounds and Nitrogen Oxide Donors on Lipid Oxidation, Membrane-Skeletal Proteins, and Erythrocyte Structure under Hypoxia

“…The morphology of erythrocytes is sensitive to the action of sodium nitroprusside and phenolic compounds of natural origin. Considering the abundant literature [55–57] and the results of our previous study of the lipid component of erythrocyte membranes [58, 59], we thought that the structure and condition of erythrocytes is interconnected not only with the lipid components of membranes, but also with proteins of the cytoskeleton. Therefore, in the second series of experiments, we quantified the condition of the erythrocyte membrane-skeletal proteins during hypoxia and treatment with nitroprusside sodium and quercetin.…”

Nitric oxide inhibits hypoxia‐induced impairment of human RBC deformability through reducing the cross‐linking of membrane protein band 3

“…In fact, it has been documented that the function of NO mediators maintaining RBCs deformability throughout regulate the normal structure of membrane proteins: this function is related to the reaction of NO with the protein free thiol of cysteine residue which is reversible, to prevent the target cysteine residue(s) from the further oxidative modification. Additionally, RBCs are among the cells that are most prone to oxidative damage induced by hypoxia with oxidatively damaged proteins and other lipid protein becoming nonfunctional, and then impair the structure and function of RBCs …”