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5. Progressive defect in biliary GSH secretion in streptozotocin-induced diabetic rats

Author

Lu, Shelly C., Kuhlenkamp, John, Wu, HuiYuan, Sun, Wei-Min, Stone, Lee, and Kaplowitz, Neil

Subjects
Rats as laboratory animals -- Physiological aspects, Diabetes -- Physiological aspects, Glutathione -- Physiological aspects, Bile acids -- Physiological aspects, Biological sciences
Abstract

Biliary glutathione (GSH) efflux was measured in rats with streptozotocin (STZ)-induced diabetes to determine changes in hepatic GSH transport due to diabetes. Rats with STZ-induced diabetes exhibited significant alterations in hepatobiliary metabolism such as progressive and significant reductions in bile GSH output due to heightened protein kinase C levels. However, canalicular GSH transport was not affected STZ-induced diabetes in rats.

Published
1997

11. Progressive defect in biliary GSH secretion in streptozotocin-diabetic induced rats.

Author

Lu, Shelly C. and Kuhlenkamp, John

Subjects
*DIABETES, *GLUTATHIONE
Abstract

Examines the effect of streptozotocin-induced diabetes on biliary reduced glutathione efflux. Induction of diabetes; In vivo measurements of bile flow and biliary GSH efflux; Isolation of sinusoidal and canalicular membrane vesicles.

Published
1997

17. Identification and purification of a 36 kDa bile acid binder in human hepatic cytosol

Author

Stolz, Andrew, Sugiyama, Yuichi, Kuhlenkamp, John, and Kaplowitz, Neil

Abstract

We recently purified two closely related 33 kDa proteins from rat hepatic cytosol, designated bile acid binder I and II, which selectively bind bile acids with comparable affinity as glutathione S‐transferase B. This work has now been extended to human liver in which we have identified a similar cytosolic binding activity in the 30–40 kDa fraction from gel filtration. Subsequent chromatofocusing and hydroxyapatite chromatography resulted in the isolation of a homogenous monomeric protein of 36 kDa. The binding affinity of this protein for lithocholate using the displacement of 1‐anilino‐8‐naphthalenesulfonate (ANS) was 0.1 μM, whereas human hepatic glutathione S‐transferases purified from glutathione affinity chromatography demonstrated no competitive displacement of ANS.

Published
1984
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