Nuclear translocation of aflatoxin B1 - protein complex.
The in vitro binding of [3H]-AFB1 to various proteins was studied by equilibrium dialysis. At 23 +/- 1 degree C, [3H]-AFB1 binding activity (mmol/mol) decreased as follows: pyruvate kinase > albumin-NLS > albumin > carbonic anhydrase > RNase > histones. The nuclear translocation and activation of AFB1 and AFB-protein complexes was investigated using isolated rat liver nuclei in the presence of ATP and a NADPH regenerating system. Proteins containing NLS such as histones and albumin-NLS facilitated AFB1 translocation into the nucleus where activation and adduct formation took place.
Ch'ih
J J
JJ
Department of Biological Chemistry, Hahnemann University, School of Medicine, Philadelphia, PA 19102-1192.
Ewaskiewicz
J I
JI
Taggart
P
P
Devlin
T M
TM
D016604:Aflatoxin B1 / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002256:Carbonic Anhydrases / Q000378:metabolism; D002417:Cattle; D002467:Cell Nucleus / Q000378:metabolism*; D003600:Cytosol / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D011485:Protein Binding; D011506:Proteins / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D012709:Serum Albumin / Q000378:metabolism; D014316:Tritium
D006657:Histones; D011506:Proteins; D012709:Serum Albumin; D014316:Tritium; D016604:Aflatoxin B1; D011770:Pyruvate Kinase; D012259:Ribonuclease, Pancreatic; D002256:Carbonic Anhydrases