Methylglyoxal-tubulin interaction: studies on the aldehyde effects on hepatoma, liver and purified microtubular protein.
Methylglyoxal antiproliferative action is well known; this action may be exerted by a non-enzymic mechanism and may directly involve the microtubular system. Our purpose was to verify this hypothesis, by studying the aldehyde effect on normal and tumour microtubular protein. Methylglyoxal incubation of normal and tumour liver cell homogenates causes inhibition of colchicine binding activity above all at higher concentrations. The aldehyde administration to the purified microtubular protein induces alterations in some tubulin properties already at lower concentrations. These results show a possible tubulin-methylglyoxal interaction, also if the reaction mechanism is so far unclear.
D000447:Aldehydes / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites; D003078:Colchicine / Q000378:metabolism; D066298:In Vitro Techniques; D008099:Liver / Q000187:drug effects / Q000378:metabolism*; D008114:Liver Neoplasms, Experimental / Q000378:metabolism*; D008297:Male; D011765:Pyruvaldehyde / Q000378:metabolism / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D014404:Tubulin / Q000378:metabolism*
D000447:Aldehydes; D014404:Tubulin; D011765:Pyruvaldehyde; D003078:Colchicine