Publication Database

Carbonic anhydrase influences asymmetric sodium and acetate transport across omasum of sheep (2021)

Art

Zeitschriftenartikel / wissenschaftlicher Beitrag

Autoren

Rabbani, Imtiaz

Rehman, Habib

Martens, Holger (WE 2)

Majeed, Khalid Abdul

Yousaf, Muhammad Shahbaz

Rehman, Zia Ur

Quelle

Animal bioscience : (AB)

Bandzählung: 34

Heftzählung: 5

Seiten: 880 – 885

ISSN: 2765-0235

Sprache

Englisch

Verweise

URL (Volltext): https://www.animbiosci.org/journal/view.php?doi=10.5713/ajas.20.0163

DOI: 10.5713/ajas.20.0163

Pubmed: 32810932

Kontakt

Institut für Veterinär-Physiologie

Oertzenweg 19 b
14163 Berlin
+49 30 838 62600
physiologie@vetmed.fu-berlin.de

Abstract / Zusammenfassung

Objective:
Omasum is an important site 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 carbonic anhydrase 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.