scholarly journals Acute and chronic influence of temperature on red blood cell anion exchange

2001 ◽  
Vol 204 (1) ◽  
pp. 39-45 ◽  
Author(s):  
F.B. Jensen ◽  
T. Wang ◽  
J. Brahm

Unidirectional (36)Cl(−) efflux via the red blood cell anion exchanger was measured under Cl(−) self-exchange conditions (i.e. no net flow of anions) in rainbow trout Oncorhynchus mykiss and red-eared freshwater turtle Trachemys scripta to examine the effects of acute temperature changes and acclimation temperature on this process. We also evaluated the possible adaptation of anion exchange to different temperature regimes by including our previously published data on other animals. An acute temperature increase caused a significant increase in the rate constant (k) for unidirectional Cl(−) efflux in rainbow trout and freshwater turtle. After 3 weeks of temperature acclimation, 5 degrees C-acclimated rainbow trout showed only marginally higher Cl(−) transport rates than 15 degrees C-acclimated trout when compared at the same temperature. Apparent activation energies for red blood cell Cl(−) exchange in trout and turtle were lower than values reported in endothermic animals. The Q(10) for red blood cell anion exchange was 2.0 in trout and 2.3 in turtle, values close to those for CO(2) excretion, suggesting that, in ectothermic animals, the temperature sensitivity of band-3-mediated anion exchange matches the temperature sensitivity of CO(2) transport (where red blood cell Cl(−)/HCO(3)(−) exchange is a rate-limiting step). In endotherms, such as man and chicken, Q(10) values for red blood cell anion exchange are considerably higher but are no obstacle to CO(2) transport, because body temperature is normally kept constant at values at which anion exchange rates are high. When compared at constant temperature, red blood cell Cl(−) permeability shows large differences among species (trout, carp, eel, cod, turtle, alligator, chicken and man). Cl(−) permeabilities are, however, remarkable similar when compared at preferred body temperatures, suggesting an appropriate evolutionary adaptation of red blood cell anion exchange function to the different thermal niches occupied by animals.

2018 ◽  
Vol 315 (2) ◽  
pp. R397-R407 ◽  
Author(s):  
Till S. Harter ◽  
Alexandra G. May ◽  
William J. Federspiel ◽  
Claudiu T. Supuran ◽  
Colin J. Brauner

Accumulating evidence is highlighting the importance of a system of enhanced hemoglobin-oxygen (Hb-O2) unloading for cardiovascular O2 transport in teleosts. Adrenergically stimulated sodium-proton exchangers (β-NHE) create H+ gradients across the red blood cell (RBC) membrane that are short-circuited in the presence of plasma-accessible carbonic anhydrase (paCA) at the tissues; the result is a large arterial-venous pH shift that greatly enhances O2 unloading from pH-sensitive Hb. However, RBC intracellular pH (pHi) must recover during venous transit (31–90 s) to enable O2 loading at the gills. The halftimes ( t1/2) and magnitudes of RBC β-adrenergic stimulation, short-circuiting with paCA and recovery of RBC pHi, were assessed in vitro, on rainbow trout whole blood, and using changes in closed-system partial pressure of O2 as a sensitive indicator for changes in RBC pHi. In addition, the recovery rate of RBC pHi was assessed in a continuous-flow apparatus that more closely mimics RBC transit through the circulation. Results indicate that: 1) the t1/2 of β-NHE short-circuiting is likely within the residence time of blood in the capillaries, 2) the t1/2 of RBC pHi recovery is 17 s and within the time of RBC venous transit, and 3) after short-circuiting, RBCs reestablish the initial H+ gradient across the membrane and can potentially undergo repeated cycles of short-circuiting and recovery. Thus, teleosts have evolved a system that greatly enhances O2 unloading from pH-sensitive Hb at the tissues, while protecting O2 loading at the gills; the resulting increase in O2 transport per unit of blood flow may enable the tremendous athletic ability of salmonids.


2001 ◽  
Vol 32 (4) ◽  
pp. 409-415 ◽  
Author(s):  
George L. Selden ◽  
Paul B. Brown ◽  
Anthony C. Ostrowski ◽  
Rolando A. Flores ◽  
Lawrence A. Johnson

1991 ◽  
Vol 156 (1) ◽  
pp. 233-248 ◽  
Author(s):  
S. THOMAS ◽  
R. KINKEAD ◽  
P. J. WALSH ◽  
C. M. WOOD ◽  
S. F. PERRY

The sensitivity of red blood cell Na+/H+ exchange to exogenous adrenaline was assessed in vitro using blood withdrawn from catheterized rainbow trout (Oncorhynchus mykiss) maintained under normoxic conditions [water PO2, (PwO2)=20.66 kPa] or after exposure to moderate hypoxia (PwO2=6.67-9.33 kPa) for 48 h, which chronically elevated plasma adrenaline, but not noradrenaline, levels. Peak changes in whole-blood extracellular pH over a 30 min period after adding 50–1000 nmoll−1 adrenaline were employed as an index of sensitivity; the blood was pre-equilibrated to simulate arterial blood gas tensions in severely hypoxic fish (PaO2=2.0 kPa, PaCO2=0.31 kPa). Blood pooled from normoxic fish displayed a dose-dependent reduction in whole-blood pH after addition of adrenaline. Blood pooled from three separate groups of hypoxic fish, however, displayed diminished sensitivity to adrenaline, ranging from complete desensitization to a 60%reduction of the response. Subsequent experiments performed on blood from individual (i.e. not pooled) normoxic or hypoxic fish demonstrated an inverse correlation between the intensity of H+ extrusion (induced by exogenous adrenaline addition) and endogenous plasma adrenaline levels at the time of blood withdrawal. However, acute increases in plasma adrenaline levels in vitro did not affect the responsiveness of the red blood cell to subsequent adrenergic stimulation. The intensity of H+ extrusion was inversely related to the PaO2in vivo between 2.67 and 10.66 kPa, and directly related to the logarithm of the endogenous plasma adrenaline level. The results suggest that desensitization of Na+/H+ exchange in chronically hypoxic fish is related to persistent elevation of levels of this catecholamine. This desensitization can be reversed in vitro as a function of time, but only when blood is maintained under sufficiently aerobic conditions.


1994 ◽  
Vol 189 (1) ◽  
pp. 279-284
Author(s):  
C Carter ◽  
S Owen ◽  
Z He ◽  
P Watt ◽  
C Scrimgeour ◽  
...  

It has been suggested (Houlihan, 1991) that the consumption of 1 g of protein in a variety of species of fish stimulates the synthesis of, approximately, an equal amount of protein. Although synthesis of protein may account for as much as 40 % of the whole-animal oxygen consumption (Lyndon et al. 1992), only about 30 % of the synthesized proteins are retained as growth (Houlihan et al. 1988; Carter et al. 1993a,b). Thus, one focus of attention is the potential advantage gained by fish in allocating a considerable proportion of assimilated energy to protein turnover in contrast to relatively low-cost, low-turnover protein growth (Houlihan et al. 1993). Rates of protein synthesis in several species of fish have been measured using radioactively labelled amino acids, frequently given as a flooding dose (reviewed by Fauconneau, 1985; Houlihan, 1991). These measurements cannot be made for longer than a few hours because of the decline in specific radioactivity in the amino acid free pool. However, as protein synthesis rates vary during the course of a day as a result of the post-prandial stimulation, and since radiolabelled amino acid methodology is invasive, short-term and terminal, it has been difficult to be certain of the relationship between protein growth measured in the long term and protein synthesis rates measured in the short term. This paper addresses these problems by developing a method using 15N in orally administered protein to measure protein synthesis rates in fish over relatively long periods, the aim being to use procedures that are as non-invasive and repeatable as possible. The use of stable isotopes to measure protein metabolism is well established in terrestrial mammals (see Rennie et al. 1991; Wolfe, 1992), but to our knowledge the only published data for aquatic ectotherms are on the blue mussel (Mytilus edulis L.) (Hawkins, 1985). In the present study, rates of protein synthesis of individual rainbow trout [Oncorhynchus mykiss (Walbaum)] were calculated from the enrichment of excreted ammonia with 15N over the 48 h following the feeding of a single meal (dose) containing protein uniformly labelled with 15N by use of an end-point stochastic model (Waterlow et al. 1978; Wolfe, 1992). Application of this type of modelling would appear to be ideal for measuring ammonotelic fish nitrogen metabolism since, unlike the situation in mammals, the catabolic flux of amino acids through urea is very small. Further, ammonia is excreted directly into the surrounding water via the gills and is not stored for any length of time, in contrast to the situation in mammals, so the rate of tracer appearance is easily measurable.


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