Monensin and bile protein secretion. A tool to investigate hepatocyte intracellular vesicular polarity.
Bile derived from monensin treated bile-fistula rats was analysed by SDS-polyacrylamide gels. Differences in proteins were observed for bands presumptively corresponding to transferrin, secretory-IgA and free secretory components after treatment with the ionophore. The results show that the secretion of proteins in bile is differentiated and asyncronous, confirming a polarity of the hepatocyte subcellular compartments.
Casu
A
A
Istituto di Patologia Generale, Università, Genova.
Averame
M M
MM
Piemontese
R
R
D000818:Animals; D001646:Bile / Q000187:drug effects* / Q000378:metabolism; D005260:Female; D006863:Hydrogen-Ion Concentration; D007071:Immunoglobulin A, Secretory / Q000378:metabolism; D008099:Liver / Q000187:drug effects* / Q000378:metabolism; D008985:Monensin / Q000494:pharmacology*; D011506:Proteins / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D012635:Secretory Component / Q000302:isolation & purification; D014168:Transferrin / Q000378:metabolism
D007071:Immunoglobulin A, Secretory; D011506:Proteins; D012635:Secretory Component; D014168:Transferrin; D008985:Monensin