Osmoregulatory plasticity during hypersaline acclimation in red drum, Sciaenops ocellatus

J Comp Physiol B. 2021 Jul;191(4):731-740. doi: 10.1007/s00360-021-01356-y. Epub 2021 Apr 12.

Abstract

Prolonged drought and freshwater diversion are making periods of hypersalinity more common in coastal ecosystems. This is especially true in the Laguna Madre system along the Texas coast where salinities can exceed 60 g/kg. As such, the ability to tolerate hypersalinity is critical to the success of endemic species, such as the commercially important red drum (Sciaenops ocellatus). This study evaluated acclimation of red drum to hypersalinity (60 g/kg) using a direct transfer protocol. Hypersalinity exposure resulted in significant impacts on plasma osmolality and muscle water in the first 24 h, but returned to control values coincident with a significant increase in intestinal water volume. Hypersalinity acclimation resulted in significant branchial and intestinal plasticity. The gill showed significant elevated nka α1a, nkcc1 and vha (B subunit) mRNA abundance, as well as NKA enzyme activity. The posterior intestine showed a stronger plasticity signal than the anterior intestine, which included a 12-fold increase in nkcc2 mRNA abundance and significant increases in NKA and VHA enzyme activity. These changes were corroborated by a significant threefold increase in bumetanide-sensitive absorptive short circuit current. These data suggest that the dynamic regulation of NKCC2-mediated intestinal water absorption is an important compliment to HCO3--mediated water absorption during hypersalinity exposure and acclimation.

Keywords: Hypersalinity; NKCC; Na+ K+ ATPase; Osmoregulation; Salinity transfer; V-type ATPase.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acclimatization
  • Animals
  • Ecosystem*
  • Gills / metabolism
  • Osmoregulation
  • Salinity
  • Seawater
  • Sodium-Potassium-Exchanging ATPase* / metabolism
  • Water-Electrolyte Balance

Substances

  • Sodium-Potassium-Exchanging ATPase