PubMed HealthSearch

PubMed · 7503564

Decrease of red cell membrane fluidity and -SH groups due to hyperglycemic conditions is counteracted by alpha-lipoic acid.

Abstract

Human red cell membranes (ghosts) were treated by 5 min of incubation with fasting or hypo- and hyperglycemic concentrations of D-glucose. This simulation of nondiabetic or diabetic conditions revealed an influence on membrane fluidity and on protein -SH reactivity. Protein -SH groups, measured with Ellman's reagent, generally behave in the same way as membrane fluidity determined with diphenylhexatriene. Maximal values were obtained with 5 mM D-glucose, whereas decrease was observed above 10 mM D-glucose. Addition of alpha-lipoic acid (4 nmol/mg protein) resulted in a significant increase in membrane fluidity and titratable -SH groups at glucose concentrations of 10 mM and above. Dithiothreitol diminished titrable-SH groups and did not restore membrane fluidity. 2-Mercaptopropionylglycine was only effective in restoration of -SH groups. By contrast to D-glucose, other sugars such as L-glucose, D-fructose, or sucrose revealed no comparable changes on membrane fluidity and titratable membrane -SH groups between concentrations of 5 and 10 mM. The hyperglycemic effects of D-glucose were corroborated with isolated, reconstituted membrane proteins and erythrocyte glucose carrier, indicating that, in general, the observed divergent biochemical/biophysical changes of the red cell membrane are influenced by the glucose transport protein GluT1. The natural R-form and the S-form of alpha-lipoic acid were compared with racemic R-/S-forms for their efficiencies in alterations of red cell membrane fluidity. Decreased fluidities in presence of 10 mM glucose were found to be influenced in differentiated ways: the S-form was highly active in increasing fluidity at 4 nmol/mg and increasingly less active up to 20 nmol/mg protein. By contrast the R-form of lipoic acid was moderately efficient in increasing fluidity through a larger concentration range between 4 and 80 nmol/mg protein.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

M Hofmann, P Mainka, H Tritschler, J Fuchs, G Zimmer. 1995-12-01. Decrease of red cell membrane fluidity and -SH groups due to hyperglycemic conditions is counteracted by alpha-lipoic acid.. https://doi.org/10.1006/abbi.1995.9925

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Kinetic studies of the regeneration of recombinant hirudin variant 1 with oxidized and reduced dithiothreitol.

The regeneration of native recombinant hirudin variant 1 (rHV1) from the reduced unfolded form to the fully oxidized native state has been carried out with mixtures of oxidized and reduced dithiothreitol at pH 8.3 and 12 degrees C. The regeneration reaction was quenched at various times by the addition of 2-aminoethyl methanethiosulfonate to block unreacted sulfhydryl groups. The quenched protein-folding intermediates were fractionated by both capillary electrophoresis and a combination of anion exchange and reverse phase HPLC and characterized by mass spectrometry, amino acid analysis, and disulfide analysis. These intermediates (before quenching) were found to interconvert rapidly so as to achieve a steady-state distribution early in the regeneration process. The experimental data were fitted to a steady-state kinetic scheme. The analysis reveals that the rate-determining step in the regeneration of rHV1 with oxidized and reduced dithiothreitol involves the oxidation of one or more two-disulfide-containing species, most likely those already containing two native disulfide bonds. This regeneration mechanism is different from one that has been proposed by Chatrenet and Chang [(1993) J. Biol. Chem. 268, 20988]. The differences are discussed, and possible explanations for the differences are presented.

Dithiothreitol

Role of glycoprotein PE2 in formation and maturation of the Sindbis virus spike.

Sindbis virus envelope assembly is a multistep process resulting in the maturation of a rigid, highly ordered T=4 icosahedral protein lattice containing 80 spikes composed of trimers of E1-E2 heterodimers. Intramolecular disulfide bonds within E1 stabilize E1-E1 associations required for envelope formation and maintenance of the envelope's structural integrity. The structural integrity of the envelope protein lattice is resistant to reduction by dithiothreitol (DTT), indicating that E1 disulfides which stabilize structural domains become inaccessible to DTT at some point during virus maturation. The development of E1 resistance to DTT occurs prior to the completion of E1 folding and is temporally correlated with spike assembly in the endoplasmic reticulum. From these data we have predicted that in the final stages of spike assembly, E1 intramolecular disulfides, which stabilize the structural integrity of the envelope protein lattice, are buried within the spike and become inaccessible to the reductive activity of DTT. The spike is formed prior to the completion of E1 folding, and we have suggested that PE2 (the precursor to E2) may play a critical role in E1 folding after PE2-E1 oligomer formation has occurred. In this study we have investigated the role of PE2 in E1 folding, oligomer formation, and development of E1 resistance to both protease digestion and reduction by DTT by using a Sindbis virus replicon (SINrep/E1) which allows for the expression of E1 in the presence of truncated PE2. Through pulse-chase analysis of both Sindbis virus- and SINrep/E1-infected cells, we have determined that the folding of E1 into a trypsin-resistant conformation and into its most compact and stable form is not dependent upon association of E1 with PE2. However, E1 association with PE2 is required for oligomer formation, the export of E1 from the endoplasmic reticulum, and E1 acquisition of resistance to DTT.

Dithiothreitol

Immunoglobulin cleavage by hypochlorous acid treatment.

IgA, IgG and IgM were cleaved by hypochlorous acid treatment. The apparent calculated molecular masses of three polypeptides obtained from IgA were 81.1. 25.8 and 13.9 kDa. The amounts of released IgA fragments were proportional to the amount of HOCl employed. At a HOCl:IgA molar ratio above 320:1, a profound degradation of IgA polypeptide chains occurred, resulting in a yellow-coloured product. The HOCl treatment of IgG resulted in similar effects, the liberation of three fragments, one of them being of a size slightly larger than that of the light chain (30.4 kDa). The treatment of IgM with HOCl also produced three fragments: one corresponding to the monomeric IgM molecule, the second to the light chain (26.4 kDa) and the third of a size smaller than the heavy chain. The optimal protein/HOCl ratios for the degradation of IgG and IgM were 375:1 and 808:1, respectively.

Dithiothreitol