The binding of the radioprotective agent cysteamine with the phospholipidic membrane headgroup-interface region

Berleur, François; Roman, V. K.; Jaskierowicz, Donald; Fatome, M.; Leterrier, F; Ter-Mlnassian-Saraga, Lisbeth; Madelmont, Georgette

doi:10.1016/0006-2952(85)90149-2

Cited by 8 publications

(2 citation statements)

References 25 publications

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“…Thiol:disulfide interconversions triggered by CySH could involve membrane proteins, intragranular storage hormone thiols and disulfides, and/or quantitatively minor intragranular nonhormonal proteins. CySH can also bind to phospholi pids [16], and it is possible that some of the binding to membranes we have studied is lipid-directed. It does not seem likely, however, that a CySH-phospholipid interac tion would be involved in mediating the specific effects of CySH on PRL.…”

Section: Discussionmentioning

confidence: 99%

Preferential Interaction of [<sup>35</sup>S]Cysteamine with Pituitary Secretory Granule Storage Forms of Prolactin

Lorenson

Jacobs²

1988

Neuroendocrinology

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Cysteamine (CySH) inhibits the immunodetectability and bioactivity of prolactin (PRL), and we have proposed that it may act by impeding the conversion from secretory granule hormone storage forms to releasable and assayable hormone. This process appears to be dependent upon thiol:disulfide interchange reactions, which can be inhibited by the aminothiol. The present studies utilized [³⁵S]CySH to determine whether preferential interactions could be demonstrated between CySH and bovine pituitary storage hormone forms as opposed to monomeric PRL. [³⁵S]CySH was incubated with purified intact secretory granules, with granule ‘core’ preparations enriched in oligomeric forms by prior hypotonic exposure, with chromatographically isolated oligomers, and with monomeric PRL. Binding to granules was saturable and pH-dependent with greatest binding observed at pH 7.5–8.0. Binding to monomer was much less than binding to all other fractions, being 20% or less than that to any other form. HPLC studies of granules treated with [³⁵S]CySH indicated that exposure to CySH was associated with a predominance of very high molecular weight oligomers. These forms were entrapped on the gel permeation columns, resulting in decreased protein and PRL recovery; as little as 6.6% of the PRL was eluted after 60 min of CySH exposure. CySH not only bound to storage forms of PRL but also to secretory granule membranes; whether the bioeffect is mediated through membrane modifications is unknown. Despite its relative ineffectiveness at altering growth hormone immunoactivity or secretion, CySH nonetheless also bound to growth hormone. Thus, further studies are required to establish with certainty the site(s) of CySH binding and to establish the molecular mechanism which accounts for inhibitory aminothiol effects on PRL storage forms and PRL secretion.

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Section: Discussionmentioning

confidence: 99%

Preferential Interaction of [<sup>35</sup>S]Cysteamine with Pituitary Secretory Granule Storage Forms of Prolactin

Lorenson

Jacobs²

1988

Neuroendocrinology

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“…At a low concentration (10 -4 M), Cyst behaved like a divalent cation (amine and SH groups), creating electrostatic bridges with the negatively charged phosphate groups of the polar heads of lipids leading to an increase in membrane stability. These bridges are disrupted when Cyst is present at high concentration (10 -2 and 10 -1 M) inducing a decrease in the lipid membrane rigidity; Cyst acted like a monovalent cation and displacement of the slightly charged SH extremity by the amine of Cyst is occurred (Berleur et al, 1985).…”

Section: Berleur Et Al Studied the Interaction Of Cyst With Dipalmito...mentioning

confidence: 99%

Development of cysteamine loaded liposomes in liquid and dried forms for improvement of cysteamine stability

Atallah

Greige‐Gerges

Charcosset

2020

International Journal of Pharmaceutics

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Inhibitory effects of thiols on a mutagenic contaminant from the synthesis of N-nitrosothiazolidine

Miller

Fiddler

1987

Mutation Research/Fundamental and Molecular Mechanisms of Mutag

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The binding of the radioprotective agent cysteamine with the phospholipidic membrane headgroup-interface region

Cited by 8 publications

References 25 publications

Preferential Interaction of [<sup>35</sup>S]Cysteamine with Pituitary Secretory Granule Storage Forms of Prolactin

Preferential Interaction of [<sup>35</sup>S]Cysteamine with Pituitary Secretory Granule Storage Forms of Prolactin

Development of cysteamine loaded liposomes in liquid and dried forms for improvement of cysteamine stability

Inhibitory effects of thiols on a mutagenic contaminant from the synthesis of N-nitrosothiazolidine

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