Assessment of Di- and Tri-butyltin interaction with skeletal muscle membranes

Cell membranes of muscles are prime target sites for interactions from environmental pollutant exposure. Binding of di- and tributyltin compounds, which cause hepatotoxicity and inhibit oxidative phosphorylation, to frog muscle basement membrane and sarcolemma is studied. About 81% of the dibutyltin...

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Bibliographic Details
Published in:Bulletin of environmental contamination and toxicology 1990-01, Vol.44 (1), p.29-38
Main Authors: Ali, A.A. (Industrial Toxicology Research Centre, Lucknow, India), Upreti, R.K, Kidwai, A.M
Format: Article
Language:English
Subjects:
Animals
Cell Membrane - drug effects
Cell Membrane - metabolism
COMPOSE ORGANOSTANNIQUE
COMPUESTO ORGANICO DEL ESTANO
FROGS
GRENOUILLE
In Vitro Techniques
Kinetics
MOLLUSCICIDE
MOLLUSCICIDES
MOLUSCOCIDAS
MUSCLE
MUSCLES
Muscles - drug effects
MUSCULOS
ORGANOTIN COMPOUNDS
Organotin Compounds - toxicity
RANA
Ranidae
Sarcolemma - drug effects
Sarcolemma - metabolism
THIOL
THIOLS
TIOLES
Trialkyltin Compounds - toxicity
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Summary:Cell membranes of muscles are prime target sites for interactions from environmental pollutant exposure. Binding of di- and tributyltin compounds, which cause hepatotoxicity and inhibit oxidative phosphorylation, to frog muscle basement membrane and sarcolemma is studied. About 81% of the dibutyltin dichloride administered was found in the sarcolemma plasma membrane and 19% in the basement membrane. Organotin binding with basement membranes may provide some protection for enzymatic activities of plasma membranes and cell function activities. Four thiol compounds were used to antagonize organotin binding with a resulting maximum decrease of 67% of total binding and 20% of sulfhydryl content. The thiol organotin interaction may produce inactive species of tin compounds, which cannot bind with sarcolemmal membrane proteins.
ISSN:0007-4861
1432-0800
DOI:10.1007/BF01702358