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Anion Exchanger in Hypertension
Published in Antonio Coca, Ricardo P. Garay, Ionic Transport in Hypertension: New Perspectives, 2019
On the other hand, we have described recently that the activity of the Na+-independent Cl-/ AE is increased in RBC of patients with essential hypertension as compared to normotensive controls.135 Interestingly, the activity of this transport system was inversely correlated with pHi and directly correlated with blood pressure.135 Thus, it appears that this AE mechanism could serve as a marker for alterations in pHrdependent control of vascular tone in hypertension. Again, a potential consideration arises when considering antihypertensive treatment of patients with this abnormality. In fact, the antihypertensive drug cicletanine has been shown to inhibit the Na+-independent Cl−/ AE both in erythrocytes and in vascular smooth muscle cells.136
Species differences in plasma protein binding of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) main protease inhibitor nirmatrelvir
Published in Xenobiotica, 2023
Siennah R. Greenfield, Heather Eng, Qingyi Yang, Chunyang Guo, Laura Byrnes, Alyssa Dantonio, Graham West, Li Di, Amit S. Kalgutkar
At a low concentration (1 µM), nirmatrelvir is highly bound to both dog SA/AAG and rabbit AAG resulting in low fraction unbound values. In contrast, binding of nirmatrelvir to rabbit SA was moderate and occurred in a concentration-independent fashion. The increase in fraction unbound for dog SA/AAG and rabbit AAG at higher nirmatrelvir concentrations (10 and 100 µM) suggests that dog SA and dog/rabbit AAG are subject to saturable binding at their respective binding sites. While saturable binding can be considered to be unusual for SA given that the protein is typically regarded as a low-affinity, high-capacity protein (Smith and Waters 2019), there are some reports of saturable human SA binding sites for marketed drugs such as cicletanine, cefazolin, and diclofenac (Chamouard et al. 1985; Zini et al. 1988; Vella-Brincat et al. 2007). AAG is a high-affinity, low-capacity protein present at lower concentrations in plasma compared to SA (Smith and Waters 2019). This feature most likely explains saturation of dog and rabbit AAG binding with increases in nirmatrelvir concentrations. Concentration-independent binding to human AAG and concentration-dependent binding to rabbit AAG reflect what was observed for human and rabbit PPB, while dog AAG and dog SA binding reflect what was observed for dog PPB. The different glycosylation distribution as well as the different N-glycosylation site in dog and rabbit AAG (Figures 8 and 9) may result in a protein conformational (and property) change that favours a higher affinity interaction with nirmatrelvir, relative to human AAG.