Association between the glycation of erythrocyte membrane proteins and membrane fluidity

Bryszewska, Maria; Szosland, Konrad

doi:10.1016/s0009-9120(88)80111-5

Cited by 30 publications

(18 citation statements)

References 13 publications

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“…45) Non-enzymatic glycation of erythrocyte-membrane protein decreases erythrocyte membrane fluidity, 46,47) and glycated erythrocytes can easily be recognized by macrophages through the modified membrane protein, 48,49) suggesting that erythrocytes functionally deteriorated by AGE-modification of membrane proteins were removed from circulation by macrophages. However, we have not clarified that how macrophages recognize the AGE-modified erythrocytes.…”

Section: Discussionmentioning

confidence: 99%

Macrophage Recognition of Toxic Advanced Glycosylation End Products through the Macrophage Surface-Receptor Nucleolin

Miki

Dambara

Tachibana

et al. 2014

Biological & Pharmaceutical Bulletin

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Advanced glycosylation end-products (AGEs) are non-enzymatically glycosylated proteins that play an important role in several diseases and aging processes, including angiopathy, renal failure, diabetic complications, and some neurodegenerative diseases. In particular, glyceraldehyde (GCA)-and glycolaldehyde (GOA)-derived AGEs are deemed toxic AGEs, due to their cytotoxicity. Recently, the shuttling-protein nucleolin has been shown to possess scavenger receptor-activity. Here, we investigated whether or not macrophages recognize toxic AGEs through nucleolin receptors expressed on their surface. Free amino acid groups and arginine residues found in bovine serum albumin (BSA) were time-dependently modified by incubation with GCA and GOA. In addition, average molecular size was increased by incubation with GCA and GOA. While GCA-treated BSA (GCA-BSA) and GOA-treated BSA (GOA-BSA) were recognized by thioglycollate-elicited mouse peritoneal macrophages in proportion to their respective aldehyde-modification ratios, aldehyde-untreated control-BSA was not. Surface plasmon-resonance analysis revealed that nucleolin strongly associated with GCA-BSA and GOA-BSA, but not with control-BSA. Further, pretreating macrophages with anti-nucleolin antibody, but not control-Immunoglobulin G, inhibited recognition of GCA-BSA and GOA-BSA by macrophages. Additionally, AGRO, a nucleolin-specific oligonucleotide aptamer, inhibited recognition of GCA-BSA and GOA-BSA. Moreover, nucleolin-transfected HEK293 cells recognized more GCA-BSA and GOA-BSA than control HEK cells did. Binding of nucleolin and GCA-BSA/GOA-BSA was also blocked by anti-nucleolin antibody at molecular level. These results indicate that nucleolin is a receptor that allows macrophages to recognize toxic AGEs.Key words advanced glycosylation end-product (AGE); glyceraldehyde; glycolaldehyde; macrophage; nucleolin; toxic AGE The modification, aggregation, and deposition of proteins are prominent events in many pathological processes and can play a direct role in tissue damage. Advanced glycation end-products (AGEs) are one type of post-translational modification product that form from non-enzymatic reactions between proteins and reducing sugars, dicarbonyl compounds, or reactive aldehydes such as α-hydroxyaldehyde, which are followed by several chemical modifications including crosslinking, rearrangement, and condensation.

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Section: Discussionmentioning

confidence: 99%

Macrophage Recognition of Toxic Advanced Glycosylation End Products through the Macrophage Surface-Receptor Nucleolin

Miki

Dambara

Tachibana

et al. 2014

Biological & Pharmaceutical Bulletin

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“…на возможное из-менение свойств мембраны в условиях карбо-нильного стресса указывает и тот факт, что hb лучше связывается с мембранами эритроцитов больных сахарным диабетом, чем с мембрана-ми контрольных эритроцитов [Bryszewska, Szosland, 1988]. Примечательно, что сродство гли-кированного hb к мембранам было ниже, чем у немодифицированного.…”

Section: результаты и обсуждениеunclassified

Effect of Nitric Oxide Metabolites on the Formation of Membranebound Hemoglobin Under Carbonyl Stress

Nasybullina¹,

Космачевская²,

Topunov³

et al. 2018

Proceedings of KarRC of RAS

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в интактных эритроцитах гемоглобин (hb) может существовать в растворимой и мембраносвязанной формах. Переход гемоглобина в мембраносвязанное со-стояние (MBhb) может иметь физиологическое значение и являться адаптивной реакцией, направленной на изменение состояния мембраны и метаболизма эрит-роцита. Известно, что оксид азота (NO) и активные карбонильные соединения мо-гут влиять на связывание hb с мембранами. в работе показано, что добавление NaNO 2 , сysNO и GSNO в различных концентрациях к суспензии эритроцитов вызы-вает изменения содержания MBhb. наибольшие изменения уровня MBhb наблю-дались при действии на эритроциты NaNO 2 , что может быть связано с образовани-ем свободнорадикальных метаболитов в системе (oxyhb−NaNO 2 ). Метилглиоксаль (MG) вызывал дозозависимое увеличение уровня MBhb, не оказывая влияния на окислительно-восстановительное состояние hb. наблюдалась отрицательная корреляция между долей MBhb и количеством восстановленных Sh-групп мем-бранных белков. добавление метаболитов NO к суспензии эритроцитов на фоне действия MG приводило к разным последствиям: NaNO 2 снижал концентрацию MBhb на 50 %, сysNO на 20 %, а GSNO, напротив, приводил к незначительному уве-личению уровня MBhb. действие нитрозотиолов можно объяснить образованием свободнорадикальных продуктов в системе (MG−Nh 3 -hb−RSNO), которые, инду-цируя окислительные процессы у липидов и белков, способствуют связыванию hb с компонентами мембраны. Показано, что даже незначительные флуктуации уров-ня MBhb влияли на степень гемолиза эритроцитов.

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“…Hemoglobin is glycated at two sites: on the valine residue of the N-terminalchains at the ε-amino group of the and -chains, and at the N-termini of the -chains (McDonald et al, 1978). Other intracellular and membrane proteins of red blood cells (RBC) are also glycated, for example Spectrin, a major RBC membrane protein, band 3 transmembrane protein, and band 4-1 (Retnaikes et al, 1987;Bryszewska & Szosland 1988). Hence glycation results in RBC deformability and an increased adherence to endothelium.…”

Section: Pathophysiological Mechanism Of Ages Formation In Diabetic Rmentioning

confidence: 99%

Gluco-Oxidation of Proteins in Etiology of Diabetic Retinopathy

Khan¹,

Banga²,

Khan³

2012

Diabetic Retinopathy

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Association between the glycation of erythrocyte membrane proteins and membrane fluidity

Cited by 30 publications

References 13 publications

Macrophage Recognition of Toxic Advanced Glycosylation End Products through the Macrophage Surface-Receptor Nucleolin

Macrophage Recognition of Toxic Advanced Glycosylation End Products through the Macrophage Surface-Receptor Nucleolin

Effect of Nitric Oxide Metabolites on the Formation of Membranebound Hemoglobin Under Carbonyl Stress

Gluco-Oxidation of Proteins in Etiology of Diabetic Retinopathy

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