Glutathione S-transferase in human bile
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Cited by (14)
Human glutathione-S-transferase pi potentiates the cysteine-protease activity of the Der p 1 allergen from house dust mite through a cysteine redox mechanism
2019, Redox BiologyCitation Excerpt :Howie et al. [56] found high levels of GSTpi in (and purified from) bronchoalveolar lavage fluid of patients with neoplastic and non-neoplastic lung diseases. The presence of GSTpi in human bile has also been reported [57]. Moreover, our results suggest that GSTpi secreted by human bronchial epithelial cells might be involved in the upregulation of the cysteine-protease activity of Der p 1, since the upregulation effect of the apical medium was reduced by TLK199, a specific inhibitor of GSTpi.
Strong carcinogenic stress response induction of preneoplastic cells positive for GST-P in the rat liver: Physiological mechanism for initiation
2018, Life SciencesCitation Excerpt :Human GST pi, which belongs to the same pi class GST [22], is also detectable in various tissues and lesions [23,24]. In particular, GST pi was identified in bile fluid as the major GST form together with other alpha and mu class GSTs [25]. Thus, the present findings suggest that GST-P is also excreted from hepatocytes into canalicular tracts in response to the strong carcinogenic stress via some excretory pump/transporter in the phase III drug-metabolizing enzyme [26].
Spectrophotometric assay for serum glutathione transferase: A re-examination
2012, Clinical BiochemistryCitation Excerpt :In conclusion, all our findings suggest that the GST activity cannot be correctly determined spectrophotometrically both in a normal serum and in samples where the concentration of this enzyme is only a few times higher than the basal level. A different scenario may appear in some pathologic conditions that cause release of higher amounts (at least thirty times higher than the basal level) of intracellular GSTs in the serum [23–26]. However, the rapid inactivation of the Pi isoenzyme in the extra-cellular environment described in this paper (see Fig. 3A) indicates that particular caution must be given for a precise quantification of this enzyme when it is based on spectrophotometric activity determinations.
Rapid spectrophotometric method for serum glutathione S-transferases activity
2002, Clinica Chimica ActaGlutathione S-Transferases: Biomedical Applications
1993, Advances in Clinical Chemistry