Action of the mycotoxin of Fusarium sporotrichiella v. sporotrichioides on lysosomal membranes.
The effect of the mycotoxin of Fusarium sporotrichiella v. sporotrichioides (sporofusarin) was studied in vitro on the total and nonsedimenting activity of eight lysosomal enzymes: acid ribonuclease, aryl sulfatases A and B, beta-glucuronidase, alpha- and beta-galactosidases, beta-glucosidase, beta-acetylglucosaminidase, and alpha-mannosidase. Incubation of a suspension of rat liver lysosomes with an aqueous solution of sporofusarin led to inhibition of the total activity of the membrane-bound lysosomal enzyme beta-glucosidase. In a dose of only 1.6 x 10-5 M sporofusarin caused a significant increase in the nonsedimenting activity of nearly all the enzymes; in a concentration of 1.6 x 10-3 M most of the enzymes of the lysosomal matrix (beta-glucuronidase, beta-galactosidase, aryl sulfatases A and B) were liberated almost completely into the supernatant, and nearly all the beta-glucosidase also was liberated. It is postulated that damage to the subcellular membranes is an important component of the toxic action of sporofusarin.
D000818:Animals; D005670:Fusarium; D005959:Glucosidases / Q000378:metabolism; D005966:Glucuronidase / Q000378:metabolism; D006026:Glycoside Hydrolases / Q000378:metabolism; D006867:Hydrolases / Q000378:metabolism*; D008099:Liver / Q000648:ultrastructure; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology*; D008297:Male; D008358:Mannose; D008566:Membranes / Q000187:drug effects; D009183:Mycotoxins / Q000494:pharmacology*; D051381:Rats; D012260:Ribonucleases / Q000378:metabolism; D013429:Sulfatases / Q000378:metabolism
D009183:Mycotoxins; D006867:Hydrolases; D012260:Ribonucleases; D013429:Sulfatases; D005959:Glucosidases; D006026:Glycoside Hydrolases; D005966:Glucuronidase; D008358:Mannose