Role of sulfhydryl groups in erythrocyte membrane structure

Carter, Jr. James R.

doi:10.1021/bi00725a028

Cited by 72 publications

(21 citation statements)

References 24 publications

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“…conclusion, the present study is in agreement with the reports by Gordin and Schrier (1972), Smith and Verpoorte (1970) and Carter Jr. (1973) in respect of the dissociation of red cell membrane proteins by sulfhydryl inhibitors . Reduced extraction of these membrane proteins in PNH, HS and hereditary elliptocytosis suggests the possibility that the erythrocyte actomyosin system proposed by Guidotti (1972) may be qualitatively abnormal.…”

Section: Morphology Of Ghostssupporting

confidence: 94%

“…Recent observations have indicated an intimate association betweenn spectrin and the intramembranous particles (Elgsaeter and Branton 1974;Tilney and Detmers 1975;Elgsaeter et al 1976). As have been confirmed in this study, the ghosts lose their original shape and eventually vesiculate into small membrane fragments during spectrin removal (Carter Jr. 1973;Steck et al 1970). At the same time, a second component, band 5, is invariably released with spectrin.…”

Section: Morphology Of Ghostssupporting

confidence: 83%

“…4. Electrophoretic patterns of erythrocyte membrane proteins in normal subject and AIHA patient (AIHA, Case 1 in Table 1 (Gordin and Schrier 1972;Carter Jr. 1973). In our experiments, p-hydroxymercuribenzoate and NEM were employed and the results were in agreement with their observations in most respects.…”

Section: Morphology Of Ghostsmentioning

confidence: 99%

“…Extraction of proteins from normal human red cell membranes has been described by several investigators (Smith and Verpoorte 1970;Gordin and Schrier 1972;Steck and Yu 1973;Carter Jr. 1973), who agreed that approximately 20 to 30% of membrane proteins were liberated following the treatment of ghosts with sulfhydryl inhibitors resulting in morphological changes of the membrane. These findings, however, are all concerned with the effect of sulfhydryl inhibitors on normal ghosts, and information as to their effect on the abnormal red cell membrane seems to be quite lacking.…”

mentioning

confidence: 99%

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Extraction of erythrocyte membrane proteins by sulfhydryl inhibitors.

Matsumoto

Shiomura

Ishihara

et al. 1976

Tohoku J. Exp. Med.

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Section: Morphology Of Ghostssupporting

confidence: 94%

Section: Morphology Of Ghostssupporting

confidence: 83%

Section: Morphology Of Ghostsmentioning

confidence: 99%

mentioning

confidence: 99%

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Extraction of erythrocyte membrane proteins by sulfhydryl inhibitors.

Matsumoto

Shiomura

Ishihara

et al. 1976

Tohoku J. Exp. Med.

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“…These two cysteine residues may have been either in the same protein molecule or in the neighboring two molecules. Futhermore, SH groups were assumed to stabilize the membrane structure (5,12,28,29), hydrophobically interacting with the double bonds of lipid molecules. The formation of mercaptides possibly altered the state of interaction between a protein molecule and surrounding lipid molecules, thus changing the manner of those molecules when shearing force was exerted on the membrane.…”

Section: Methodsmentioning

confidence: 99%

Cytochemical Studies on the Intramembranous Particles of Erythrocyte Membranes

Fujimoto

Ogawa

1980

Acta Histochem. Cytochem

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The chemical composition and the function of intramembranous particles (IMP) of erythrocyte membranes were examined. Firstly, the sulfhydryl (SH) groups detected by the Fast Blue BBN method on ultrathin sections of rabbit erythrocyte ghosts were found to show a correlative distribution with IMP. Secondly, after treating human erythrocyte ghosts with mercuric chloride, IMP appeared to have become larger than the controls. The mean diameter of IMP was approximately 165 A on the P face and 160 A on the E face for the ghosts treated with mercuric chloride, whereas it was 94 A on the P face and 100 A on the E face for fresh ghosts.This result indicates that protein molecules which have SH groups are included in IMP of erythrocyte membrane. Thirdly, acetylcholinesterase (AchEase) activity was detected cytochemically in human erythrocyte ghosts from which IMPfree vesicles were blebbing.AchEase activity was found to be localized only on the external surface of IMP-aggregated ghosts and not on the IMP-free vesicles, suggesting a close relationship of AchEase and IMP. A cytochemical method for detecting AchEase activity on freeze-etched replicas was also described.The present results indicate that IMP in erythrocyte membranes are proteinaceous in nature and that some of them are enzyme molecules.The intramembranous particles (IMP) observed on freeze-cleaved plasma membranes are generally believed to represent protein molecules (19,40). One of the most conclusive results that support this hypothesis is given in the experiments with reconstituted membranes, that is, IMP appear on artificial lipid membranes only after definite proteins are introduced, such as rhodopsin (13), cytochrome oxidase (20) and so on. The results obtained hitherto, including the reconstitution experiments, have shown that protein molecules could contribute to IMP. But no answer has been given to the following questions: 1) Do all IMP consist of protein molecules? Isn't there any heterogeneity among IMP? 2) What kind of roles are those IMP playing physiologically? Concerning the first problem, some investigators claim that IMP which have a complementary depression on the opposite fracture face are made up of lipid and/or lipopolysaccharide molecules (37). More over, they have shown particles in liposomal membranes which are devoid of protein (36). The composition of IMP may be different among membranes of various species. But it is very difficult to examine whether heterogeneous IMP could exist

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Altered Permeability of Cell Membranes

Kinter

Pritchard

1977

Comprehensive Physiology

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The sections in this article are: Membrane Theory of Toxicity Heavy Metals — Mercury and its Compounds Passive Ion and Water Permeability of Cells Carrier‐Mediated Ion Transport Inhibition of Other Transport Systems Environmental Role Organochlorines — DDT and its Metabolites Passive Na + and K + Permeability of Axolemma Active Na + Transport in Epithelia and Cells Inhibition of Other Active Transport Systems Conclusions and Speculations

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Role of sulfhydryl groups in erythrocyte membrane structure

Cited by 72 publications

References 24 publications

Extraction of erythrocyte membrane proteins by sulfhydryl inhibitors.

Extraction of erythrocyte membrane proteins by sulfhydryl inhibitors.

Cytochemical Studies on the Intramembranous Particles of Erythrocyte Membranes

Altered Permeability of Cell Membranes

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