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Acute and chronic temperature dependence of Na+/H+ exchange activity of Pimephales promelas gills.
Ye, William; Patel, Jill; Thede, Katrina; Aravindabose, Varsha; Wentworth, Simon; Monroe, Ian; Garvin, Matthew L; Garvin, Jeffrey L; Packer, Randall K.
Affiliation
  • Ye W; Department of Physiology and Biophysics, Case Western Reserve University, 10900 Euclid Ave, Cleveland, OH 44106, United States of America.
  • Patel J; Department of Physiology and Biophysics, Case Western Reserve University, 10900 Euclid Ave, Cleveland, OH 44106, United States of America; Department of Biology, Case Western Reserve University, 2080 Adelbert Road, Cleveland, OH 44106, United States of America.
  • Thede K; Department of Biology, Case Western Reserve University, 2080 Adelbert Road, Cleveland, OH 44106, United States of America.
  • Aravindabose V; Department of Biology, Case Western Reserve University, 2080 Adelbert Road, Cleveland, OH 44106, United States of America.
  • Wentworth S; Department of Biological Sciences, George Washington University, 2029 G St N.W., Washington, D.C. 20052, United States of America.
  • Monroe I; Department of Biological Sciences, George Washington University, 2029 G St N.W., Washington, D.C. 20052, United States of America.
  • Garvin ML; Department of Biology, Case Western Reserve University, 2080 Adelbert Road, Cleveland, OH 44106, United States of America.
  • Garvin JL; Department of Physiology and Biophysics, Case Western Reserve University, 10900 Euclid Ave, Cleveland, OH 44106, United States of America. Electronic address: jlg5@case.edu.
  • Packer RK; Department of Biological Sciences, George Washington University, 2029 G St N.W., Washington, D.C. 20052, United States of America.
Article in En | MEDLINE | ID: mdl-33974967
ABSTRACT
Na+/H+ exchangers (NHE) mediate at least part of Na+ entry into gill epithelia via Na+/NH4+ exchange. For homeostasis, Na+ entry into and exit via Na+/K+ ATPase from gill epithelia must balance. Na+/K+ ATPase activity is reduced in cold- compared to warm-acclimated freshwater temperate fish. We hypothesized gill NHE activity is greater in warm- than cold-acclimated fish when measured at acclimation temperatures, and NHE activity displays a temperature dependence similar to Na+/K+ ATPase. Since NHE mRNA expression does not differ, we measured the Na+-dependence of pH-induced Na+ fluxes in gill vesicles from warm- and cold-acclimated fathead minnows at 20o and 7 °C, and calculated maximum transport rates (Vmax) and Na+ K1/2s. We also measured NH4+-induced Na+ fluxes and Na+-induced H+ fluxes. In vesicles from warm-acclimated fish, NHE Vmaxs were 278 ± 33 and 149 ± 23 arbitrary unit/s (au/s) and Na+ K1/2s were 12 ± 4 and 6 ± 4 mmol/l when assayed at 20o and 7 °C (p < 0.004), respectively. In vesicles from cold-acclimated fish, Vmaxs were 288 ± 35 and 141 ± 13 au/s and Na+ K1/2s 17 ± 5 and 7 ± 2 mmol/l when assayed at 20o and 7 °C (p < 0.002), respectively. Na+-induced H+ fluxes were 98 ± 8 and 104 ± 26 au/s in warm- and cold-acclimated fish assayed at 20 °C, respectively. Na+/NH4+ exchange was 120 ± 11 and 158 ± 13 au/s in warm- and cold-acclimated fish, respectively.

Conclusions:

Gill NHE activity was greater in warm- than cold-acclimated fish assayed at acclimation temperatures. The temperature dependence of NHE activity was similar in both groups, but differed from that reported for Na+/K+ ATPase suggesting complex mechanisms to maintain Na+ homeostasis.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cyprinidae / Sodium-Potassium-Exchanging ATPase / Gills / Acclimatization Limits: Animals Language: En Journal: Comp Biochem Physiol A Mol Integr Physiol Journal subject: BIOLOGIA MOLECULAR / FISIOLOGIA Year: 2021 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cyprinidae / Sodium-Potassium-Exchanging ATPase / Gills / Acclimatization Limits: Animals Language: En Journal: Comp Biochem Physiol A Mol Integr Physiol Journal subject: BIOLOGIA MOLECULAR / FISIOLOGIA Year: 2021 Document type: Article Affiliation country:
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