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We began analyzing https://link.springer.com/article/10.1007/BF02110442, but it redirected us to https://link.springer.com/article/10.1007/BF02110442. The analysis below is for the second page.

Title[redir]:
The irreversibility of inner mitochondrial membrane permeabilization by Ca2+ plus prooxidants is determined by the extent of membrane protein thiol cross-linking | Journal of Bioenergetics and Biomembranes
Description:
We have previously shown that mitochondrial membrane potential (δψ) drop promoted by prooxidants and Ca2+ can be reversed but not sustained by ethylene glycol-bis(β-aminoethylether)-N,N,N′,N′-tetraacetic acid (EGTA) unless dithiothreitol (DTT), a disulfide reductant, is also added [Valle, V. G. R., Fagian, M. M., Parentoni, L. S., Meinicke, A. R., and Vercesi, A. E. (1993).Arch. Biochem. Biophys. 307, 1–7]. In this study we show that catalase or ADP are also able to potentiate this EGTA effect. When EGTA is added long after (12 min) the completion of swelling or δψ elimination, no membrane resealing occurs unless the EGTA addition was preceded by the inclusion of DTT, ADP, or catalase soon after δψ was collapsed. Total δψ recovery by EGTA is obtained only in the presence of ADP. The sensitivity of the ADP effect to carboxyatractyloside strongly supports the involvement of the ADP/ATP carrier in this mechanism. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of solubilized membrane proteins shows that protein aggregation due to thiol cross-linkage formed during δψ drop continues even after δψ is already eliminated. Titration with 5,5′-dithio-bis(2-nitrobenzoic acid) supports the data indicating that the formation of protein aggregates is paralleled by a decrease in the content of membrane protein thiols. Since the presence of ADP and EGTA prevents the progress of protein aggregation, we conclude that this process is responsible for both increased permeability to larger molecules and the irreversibility of δΩ drop. The protective effect of catalase suggests that the continuous production of protein thiol cross-linking is mediated by mitochondrial generated reactive oxygen species.

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Keywords {🔍}

google, scholar, pubmed, vercesi, membrane, article, biophys, castilho, biochem, protein, kowaltowski, biol, content, mitochondrial, egta, arch, privacy, cookies, journal, meinicke, adp, access, chem, gunter, data, publish, research, search, thiol, crompton, biochim, acta, pfeiffer, information, log, irreversibility, prooxidants, crosslinking, drop, acid, valle, fagian, catalase, effect, aggregation, permeability, discover, biochemistry, bioenerg, biomembr,

Topics {✒️}

protein thiol cross-linking thiol cross-linkage formed month download article/chapter membrane protein thiols privacy choices/manage cookies mitochondrial membrane permeabilization mitochondrial membrane potential full article pdf protein aggregation due related subjects membrane resealing occurs instituto de biologia european economic area tyrosine hydroxylase binding phospholipid membranes prompts pereira-da-silva conditions privacy policy ethylene glycol-bis check access instant access mitochondrial membrane accepting optional cookies december 1996 volume 28 carboxyatractyloside strongly supports total δψ recovery journal finder publish adp/atp carrier free radical biol δψ drop continues protein aggregation increased permeability proton permeability latest articles article journal protein aggregates article log biomembranes article mitochondria vercesi rights privacy policy article castilho �-tetraacetic acid 2-nitrobenzoic acid article cite personal data books a optional cookies manage preferences brasil roger journal publish

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      headline:The irreversibility of inner mitochondrial membrane permeabilization by Ca2+ plus prooxidants is determined by the extent of membrane protein thiol cross-linking
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         Animal Biochemistry
         Organic Chemistry
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