Environmentally mediated carbonic anhydrase induction in the gills of euryhaline crustaceans

2001 ◽  
Vol 204 (5) ◽  
pp. 991-1002 ◽  
Author(s):  
R.P. Henry
Keyword(s):  
Carbonic Anhydrase ◽  
Sea Water ◽  
Carbonic Anhydrase Activity ◽  
Transport Processes ◽  
Cell Swelling ◽  
Low Salinity ◽  
The Individual ◽  
Physiological And Biochemical ◽  
Carbonic Anhydrase Gene

The enzyme carbonic anhydrase appears to be a central molecular component in the suite of physiological and biochemical adaptations to low salinity found in euryhaline crustaceans. It is present in high activities in the organs responsible for osmotic and ionic regulation, the gills, and more specifically, the individual gills that are specialized for active ion uptake from dilute sea water. Within those gills carbonic anhydrase is distributed among different subcellular pools, the cytoplasm, mitochondria and microsomes. The cytoplasmic pool represents the largest subcellular fraction of carbonic anhydrase activity, and it is this fraction that undergoes a tenfold induction during acclimation to low salinity. Carbonic anhydrase activity is present in excess of that needed to support the general ion-transport processes, and so it is doubtful that carbonic anhydrase activity itself is a point of short-term regulation in response to salinity changes. Rather, upregulation of carbonic anhydrase appears to be a result of selective gene expression, representing a permanent response to long-term adaptation to low salinity. The exact signal that initiates the induction of carbonic anhydrase, and the pathway through which that signal is transduced to the activation of the carbonic anhydrase gene, are unknown, but two promising avenues of research exist. First, induction of carbonic anhydrase is immediately preceded by hemodilution and subsequent cell swelling, a potential initiating event in the process. Second, recent work indicates that expression of carbonic anhydrase is under the control of a repressor substance, located in the eyestalk, whose effect is removed upon exposure to low salinity.

scholarly journals Enzymatic Suppression of the Membrane Conductance Associated with the Glutamine Transporter SNAT3 Expressed in Xenopus Oocytes by Carbonic Anhydrase II

2007 ◽  
Vol 130 (2) ◽  
pp. 203-215 ◽  
Author(s):  
Alexandra Weise ◽  
Holger M. Becker ◽  
Joachim W. Deitmer
Keyword(s):  
Carbonic Anhydrase ◽  
Membrane Conductance ◽  
Carbonic Anhydrase Activity ◽  
Transport Processes ◽  
Transport Activity ◽  
Ion Conductance ◽  
Neutral Amino Acid Transporter ◽  
Cation Conductance ◽  
Glutamine Transporter ◽  
New Type

The transport activity of the glutamine/neutral amino acid transporter SNAT3 (former SN1, SLC38A3), expressed in oocytes of the frog Xenopus laevis is associated with a non-stoichiometrical membrane conductance selective for Na+ and/or H+ (Schneider, H.P., S. Bröer, A. Bröer, and J.W. Deitmer. 2007. J. Biol. Chem. 282:3788–3798). When we expressed SNAT3 in frog oocytes, the glutamine-induced membrane conductance was suppressed, when carbonic anhydrase isoform II (CAII) had been injected into the oocytes. Transport of substrate, however, was not affected by CAII. The reduction of the membrane conductance by CAII was dependent on the presence of CO2/HCO3−, and could be reversed by blocking the catalytic activity of CAII by ethoxyzolamide (10 μM). Coexpression of wild-type CAII or a N-terminal CAII mutant with SNAT3 also reduced the SNAT3- associated membrane conductance. The catalytically inactive CAII mutant V143Y coexpressed in oocytes did not affect SNAT3-associated membrane conductance. Our results reveal a new type of interaction between CAII and a transporter-associated cation conductance, and support the hypothesis that the transport of substrate and the non-stoichiometrical ion conductance are independent of each other. This study also emphasizes the importance of carbonic anhydrase activity and the presence of CO2-bicarbonate buffers for membrane transport processes.

scholarly journals Tissue accumulation and the effects of long-term dietary copper contamination on osmoregulation in the mudflat fiddler crab Minuca rapax (Crustacea, Ocypodidae)

2020 ◽  
Author(s):  
MV Capparelli ◽  
JC McNamara ◽  
MG Grosell
Keyword(s):  
Carbonic Anhydrase ◽  
Atpase Activity ◽  
Fiddler Crab ◽  
Carbonic Anhydrase Activity ◽  
Copper Accumulation ◽  
Acid Base Balance ◽  
Dietary Copper ◽  
Base Balance ◽  
Copper Delivery

AbstractWe examined copper accumulation in the hemolymph, gills and hepatopancreas, and hemolymph osmolality, Na+ and Cl- concentrations, together with gill Na+/K+-ATPase and carbonic anhydrase activities, after dietary copper delivery (0, 100 or 500 µg Cu/g) for 12 days in a fiddler crab, Minuca rapax. In contaminated crabs, copper concentration decreased in the hemolymph and hepatopancreas, but increased in the gills. Hemolymph osmolality and gill Na+/K+-ATPase activity increased while hemolymph [Na+] and [Cl-] and gill carbonic anhydrase activity decreased. Excretion likely accounts for the decreased hemolymph and hepatopancreas copper titers. Dietary copper clearly affects osmoregulatory ability and hemolymph Na+ and Cl- regulation in M. rapax. Gill copper accumulation decreased carbonic anhydrase activity, suggesting that dietary copper affects acid-base balance. Elevated gill Na+/K+-ATPase activity appears to compensate for the ion-regulatory disturbance. These effects of dietary copper illustrate likely impacts on semi-terrestrial species that feed on metal contaminated sediments.

Long-term acclimation to UV radiation: effects on growth, photosynthesis and carbonic anhydrase activity in marine diatoms

2005 ◽  
Vol 48 (5-6) ◽  
Author(s):  
Malko Rech ◽  
Jean-Luc Mouget ◽  
Annick Morant-Manceau ◽  
Rosa Philippe ◽  
Gérard Tremblin
Keyword(s):  
Carbonic Anhydrase ◽  
Uv Radiation ◽  
Radiation Effects ◽  
Carbonic Anhydrase Activity ◽  
Marine Diatoms

scholarly journals Branchial and Antennal Gland Na+/K+- Dependent ATPase and Carbonic Anhydrase Activity During Salinity Acclimation of the Euryhaline Crayfish Pacifastacus Leniusculus

1987 ◽  
Vol 133 (1) ◽  
pp. 73-86 ◽  
Author(s):  
MICHÈLE G. WHEATLY ◽  
RAYMOND P. HENRY
Keyword(s):  
Carbonic Anhydrase ◽  
Sea Water ◽  
Marine Species ◽  
Carbonic Anhydrase Activity ◽  
Pacifastacus Leniusculus ◽  
Activity Levels ◽  
Salinity Acclimation ◽  
Antennal Gland ◽  
The Difference ◽  
Uptake Mechanisms

Haemolymph and urine electrolyte status and branchial and antennal gland activities of Na+/K+-ATPase and carbonic anhydrase (CA) were determined in the crayfish Padfastacus leniusculus after 3 weeks acclimation in fresh water (FW) and 350 and 750mosmolkg−1 sea water (SW). In FW the crayfish maintained haemolymph osmolality around 370 mosmol kg−1 due to hyperionic regulation of the major electrolytes. Involved in this are ion uptake mechanisms situated on the gills, and mechanisms of ion reabsorption from the primary urinary filtrate in the antennal gland (AG). Both of these processes are associated with high activities of Na+/K+- ATPase and CA. The two enzymes are uniformly distributed on gill sets 2–7, unlike the situation in euryhaline marine species. Additionally, activity levels of both enzymes are extremely high in the AG and can be correlated with the ability to produce a hypo-osmotic urine. In comparison, enzyme activity is negligible in marine species which produce isosmotic urine. Crayfish continued to hyperosmoregulate in 350 mosmolkg−1 SW. High levels of Na+/K+-ATPase confirmed the presence of a component active in the uptake of major electrolytes in the gills and also in the AG, where ion reabsorption persisted. In 750 mosmolkg−1 SW crayfish became isosmotic. Since ATPase is regulated chiefly by deactivation/activation of pre-existing enzyme, overall activity was mostly unchanged. CA activity was significantly reduced in both 350 and 750 mosmol kg−1 SW and correlated with the transition from osmoregulation to osmoconformity, suggesting that it is regulated primarily by deinduction/induction of new enzyme. The difference in the mechanism of regulation exhibited by these two enzymes is believed to relate to their subcellular distribution.

scholarly journals Physiological effects of five different marine natural organic matters (NOMs) and three different metals (Cu, Pb, Zn) on early life stages of the blue mussel (Mytilus galloprovincialis)

PeerJ ◽  
2017 ◽  
Vol 5 ◽  
pp. e3141 ◽  
Author(s):  
Lygia Sega Nogueira ◽  
Adalto Bianchini ◽  
Scott Smith ◽  
Marianna Basso Jorge ◽  
Rachael L. Diamond ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Carbonic Anhydrase ◽  
Atpase Activity ◽  
Sea Water ◽  
Blue Mussel ◽  
Solid Phase ◽  
Marine Organism ◽  
Carbonic Anhydrase Activity ◽  
Whole Body ◽  
Physiological Effects

Metals are present in aquatic environments as a result of natural and anthropogenic inputs, and may induce toxicity to organisms. One of the main factors that influence this toxicity in fresh water is natural organic matter (NOM) but all NOMs are not the same in this regard. In sea water, possible protection by marine NOMs is not well understood. Thus, our study isolated marine NOMs by solid-phase extraction from five different sites and characterized them by excitation-emission fluorescence analysis—one inshore (terrigenous origin), two offshore (autochthonous origin), and two intermediate in composition (indicative of a mixed origin). The physiological effects of these five NOMS alone (at 8 mg/L), of three metals alone (copper, lead and zinc at 6 µg Cu/L, 20 µg Pb/L, and 25 µg Zn/L respectively), and of each metal in combination with each NOM, were evaluated in 48-h exposures of mussel larvae. Endpoints were whole body Ca2++Mg2+-ATPase activity, carbonic anhydrase activity and lipid peroxidation. By themselves, NOMs increased lipid peroxidation, Ca2++Mg2+-ATPase, and/or carbonic anhydrase activities (significant in seven of 15 NOM-endpoint combinations), whereas metals by themselves did not affect the first two endpoints, but Cu and Pb increased carbonic anhydrase activities. In combination, the effects of NOMs predominated, with the metal exerting no additional effect in 33 out of 45 combinations. While NOM effects varied amongst different isolates, there was no clear pattern with respect to optical or chemical properties. When NOMs were treated as a single source by data averaging, NOM had no effect on Ca2++Mg2+-ATPase activity but markedly stimulated carbonic anhydrase activity and lipid peroxidation, and there were no additional effects of any metal. Our results indicate that marine NOMs may have direct effects on this model marine organism, as well as protective effects against metal toxicity, and the quality of marine NOMs may be an important factor in these actions.

Sign in / Sign up

Export Citation Format

Share Document