Journal of Comparative Physiology B

, Volume 188, Issue 3, pp 409–419 | Cite as

Enhanced hemoglobin–oxygen unloading in migratory salmonids

  • Jacelyn J. Shu
  • Till S. Harter
  • Phillip R. Morrison
  • Colin J. Brauner
Original Paper
First Online:
Received:
Revised:
Accepted:

Abstract

Recent findings indicate that some teleost fishes may be able to greatly enhance hemoglobin–oxygen (Hb–O2) unloading at the tissues under conditions that result in catecholamine release. The putative mechanism relies on the high pH sensitivity of teleost hemoglobin (Hb), intracellular red blood cell (RBC) pH regulation via β-adrenergic Na+/H+ exchanger (β-NHE) activity, and plasma-accessible carbonic anhydrase at the tissues that short-circuits RBC pH regulation. Previous studies have shown that in rainbow trout, this system may double Hb–O2 unloading to red muscle compared to a situation without short-circuiting. The present study determined that: (1) in rainbow trout this system may be functional even at low concentrations of circulating catecholamines, as shown by conducting a dose–response analysis; (2) Atlantic and coho salmon also possess β-NHE activity, as shown by changes in hematocrit in adrenergically stimulated cells; and (3) with β-NHE short-circuiting, Atlantic and coho salmon may be able to increase Hb–O2 unloading by up to 74 and 159%, respectively, as determined by modeling based on O2 equilibrium curves. Together, these results indicate that a system to enhance Hb–O2 unloading may be common among salmonids and may be operational even under routine conditions. In view of the life histories of Atlantic and coho salmon, a system to enhance Hb–O2 unloading during exercise may help determine a successful spawning migration and thus reproductive success.

Keywords

Red blood cell Root effect Rainbow trout Catecholamines Isoproterenol 

Abbreviations

β-NHE

β-adrenergically stimulated sodium/proton exchanger

CA

Carbonic anhydrase

CO2

Carbon dioxide

H+

Proton

Hb

Hemoglobin

Hct

Hematocrit

ISO

Isoproterenol

MCHC

Mean corpuscular hemoglobin concentration

MS-222

Tricaine methanesulphonate

Na+

Sodium ion

nH

Hill coefficient

O2

Oxygen

OEC

Oxygen equilibrium curve

PO2

Partial pressure of oxygen

P50

PO2 at which 50% of the hemoglobin is saturated with oxygen

∆Pa−vO2

Arterio–venous difference in partial pressure of O2

PCO2

Partial pressure of CO2

pHe

Extracellular, plasma pH

pHi

Intracellular, red blood cell pH

∆pHa−v

Arterio–venous difference in pH units

RBC

Red blood cell

S

Saturation of blood with oxygen

TCO2

Total dissolved CO2 content

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Notes

Acknowledgements

We thank Patrick Tamkee for animal care support. This study was supported by the Natural Science and Engineering Research Council of Canada (NSERC) Accelerator Supplement (446005-13) and Discovery Grant (261924-13) to CB.

Supplementary material

360_2017_1139_MOESM1_ESM.pdf (190 kb)
Supplementary material 1 (PDF 189 KB)

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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2017

Authors and Affiliations

  • Jacelyn J. Shu
    • 1
  • Till S. Harter
    • 1
  • Phillip R. Morrison
    • 1
  • Colin J. Brauner
    • 1
  1. 1.Department of ZoologyUniversity of British ColumbiaVancouverCanada

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