Multiple Aflatoxin B1Binding Proteins Exist in Rat Liver Cytosol

Taggart, Pamela; Devlin, Thomas M.; Ch'ih, John J.

doi:10.3181/00379727-182-42310

Cited by 4 publications

(2 citation statements)

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“…Dirr estimated in 1987 that a 45-kDa protein is the major AFB1-binding component [19]. Taggart et al found multiple proteins capable of binding AFB1 in rat liver cytosol, using gel permeation chromatography, ammonium sulfate fractionation, and DEAE-cellulose chromatography [20]. In the present study, AFB1-binding proteins were screened using immobilized affinity chromatography (IAC), developed for this study, and identified by liquid chromatography-tandem mass spectrometry.…”

Section: Introductionmentioning

confidence: 98%

Identification of AFB1-interacting proteins and interactions between RPSA and AFB1

Zhuang

Huang

et al. 2016

Journal of Hazardous Materials

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Section: Introductionmentioning

confidence: 98%

Identification of AFB1-interacting proteins and interactions between RPSA and AFB1

Zhuang

Huang

et al. 2016

Journal of Hazardous Materials

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“…Iwaki et al (19) found a cytosolic 25-kDa AFB1-binding protein and speculated that the 25-kDa protein is involved in the intracellular process of AFB1-mediated toxicity in 1983, and a 45-kDa protein was estimated by Dirr and Schabort (20) to be the major AFB1-binding component in 1987. Taggart et al found that multiple proteins are capable of binding to AFB1 (21). In this study, AFB1-binding proteins were screened with the method of immobilized affinity chromatography technology (IAC) developed by Zhuang et al in 2016 and identified by LC-MS/MS (22).…”

Section: Introductionmentioning

confidence: 99%

Estradiol 17 beta-dehydrogenase 5 is involved in aflatoxin B1 transportation

Yang¹,

Huang²,

Zeng³

et al. 2017

Turk J Vet Anim Sci

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Numerous studies have focused on the mechanism of aflatoxin B1 (AFB1) metabolism and its carcinogenic mechanism, but how AFB1 is transported into hepatocytes and how it is transferred inside hepatocytes remains unknown. In this study, the AFB1interacting protein, estradiol 17 beta-dehydrogenase 5 (Akr1c6), was identified with an immobilized affinity chromatography technique and LC-MS/MS. The interaction between Akr1c6 and AFB1 was confirmed with ELISA, and the results showed that Akr1c6 could efficiently bind AFB1. Anti-Akr1c6 polyclonal antibody from rabbit was prepared, and the IC 50 values of AFB1 to BRL (normal big rat liver cells) and NRK (normal rat kidney cells) were detected using the MTT assay. It was found that the Akr1c6 expression level in BRL was significantly affected under the IC 50 value of AFB1 (P < 0.05), but no obvious expression difference of Akr1c6 was observed in NRK. This suggested that Akr1c6 in liver cells participates in the transportation and/or metabolism of AFB1, and though Akr1c6 was expressed in the kidneys, it did not play a role in AFB1 transportation or metabolism. The conclusions of this study lay a foundation for further exploring the role of AFB1 binding proteins in the toxicology of AFB1 to hepatocytes and the pathway through which AFB1 enters hepatocytes and their nuclei.

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Aflatoxins: Detection, toxicity, and biosynthesis

Hanwan

Choi

2007

Biotechnol. Bioprocess Eng.

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Multiple Aflatoxin B1Binding Proteins Exist in Rat Liver Cytosol

Cited by 4 publications

References 0 publications

Identification of AFB1-interacting proteins and interactions between RPSA and AFB1

Identification of AFB1-interacting proteins and interactions between RPSA and AFB1

Estradiol 17 beta-dehydrogenase 5 is involved in aflatoxin B1 transportation

Aflatoxins: Detection, toxicity, and biosynthesis

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