Distinct glutathione-dependent enzyme activities and a verapamil-sensitive binding of xenobiotics in a fresh-water mussel Anodonta cygnea.
A fresh-water mussel Anodonta cygnea, an aquatic invertebrate resistant to pollution, possesses an inherent high potential to bind 2-acetylaminofluorene onto membrane vesicles. This binding is saturable and trypsin- and verapamil-sensitive. Simultaneously, this mussel reveals a relatively high inherent activity of glutathione-dependent enzyme activities with a distinct spectrum of substrate affinities. Both these activities are similar to the elements of the molecular mechanism involved in the acquired multi-drug resistance phenomenon described in tumor cell-lines. The recognition that in organisms exposed to polluted waters a multi-xenobiotic resistance mechanism may be involved is essential for understanding both the biological impact of pollution and the development of methods for rational risk assessment in regulatory policy.
Kurelec
B
B
Ruder Bosković Institute, Center for Marine Research Zagreb, Croatia, Yugoslavia.
Pivcević
B
B
D015073:2-Acetylaminofluorene / Q000378:metabolism*; D000818:Animals; D049872:Bivalvia / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004064:Digestive System / Q000201:enzymology / Q000378:metabolism; D005978:Glutathione / Q000494:pharmacology*; D007700:Kinetics; D011955:Receptors, Drug / Q000187:drug effects / Q000378:metabolism*; D014700:Verapamil / Q000494:pharmacology*
D011955:Receptors, Drug; D015073:2-Acetylaminofluorene; D014700:Verapamil; D005978:Glutathione