Carbonic anhydrase influences asymmetric sodium and acetate transport across omasum of sheep

• Main Authors: Imtiaz Rabbani, Habib Rehman, Holger Martens, Khalid Abdul Majeed, Muhammad Shahbaz Yousaf, Zia Ur Rehman
• Format: Article
• Language: English
• Published: Asian-Australasian Association of Animal Production Societies 2021-05-01
• Series: Animal Bioscience
• Subjects: flux measurements; ovine; short circuit current; ussing chamber
• Online Access: http://www.animbiosci.org/upload/pdf/ajas-20-0163.pdf

Objective Omasum is an important site for the absorption of short chain fatty acids. The major route for the transport of acetate is via sodium hydrogen exchanger (NHE). However, a discrepancy in the symmetry of sodium and acetate transport has been previously reported, the mechanism of which is unclear. In this study, we investigated the possible role of carbonic anhydrase (CA) for this asymmetry. Methods Omasal tissues were isolated from healthy sheep (N = 3) and divided into four groups; pH 7.4 and 6.4 alone and in combination with Ethoxzolamide. Electrophysiological measurements were made using Ussing chamber and the electrical measurements were made using computer controlled voltage clamp apparatus. Effect(s) of CA inhibitor on acetate and sodium transport flux rate of Na22 and 14C-acetate was measured in three different flux time periods. Data were presented as mean±standard deviation and level of significance was ascertained at p≤0.05. Results Mucosal to serosal flux of Na (JmsNa) was greater than mucosal to serosal flux of acetate (JmsAc) when the pH was decreased from 7.4 to 6.4. However, the addition of CA inhibitor almost completely abolished this discrepancy (JmsNa ≈ JmsAc). Conclusion The results of the present study suggest that the additional protons required to drive the NHE were provided by the CA enzyme in the isolated omasal epithelium. The findings of this study also suggest that the functions of CA may be exploited for better absorption in omasum.