Structurally, OTA is composed of a chlorinated dihydroisocoumarin bound to a phenylalanine
moiety (Table 2a). As a result, OTA has been shown to compete with phenylalanine and inhibit
enzymes for which phenylalanine is a substrate [50]. This is further supported by the fact that
supplementation with phenylalanine has been shown to prevent OTA toxicity in an in vivo model [51].
Glomerular filtration of ochratoxin A is negligible as the majority is bound to plasma proteins [52],
and as such, the major route of cellular entry is via the organic anion transport system, highlighting the
renal specificity associated with OTA induced toxicity. In vivo and in vitro studies have shown that
inhibition of organic anion transport with probenecid prevents OTA renal clearance [53,54], indicating
that excretion of OTA occurs via this transcellular organic anion transport system.
Structurally, OTA is composed of a chlorinated dihydroisocoumarin bound to a phenylalanine
moiety (Table 2a). As a result, OTA has been shown to compete with phenylalanine and inhibit
enzymes for which phenylalanine is a substrate [50]. This is further supported by the fact that
supplementation with phenylalanine has been shown to prevent OTA toxicity in an in vivo model [51].
Glomerular filtration of ochratoxin A is negligible as the majority is bound to plasma proteins [52],
and as such, the major route of cellular entry is via the organic anion transport system, highlighting the
renal specificity associated with OTA induced toxicity. In vivo and in vitro studies have shown that
inhibition of organic anion transport with probenecid prevents OTA renal clearance [53,54], indicating
that excretion of OTA occurs via this transcellular organic anion transport system.
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