Elevated carboxyhemoglobin in a marine mammal, the northern elephant seal.
Low concentrations of endogenous carbon monoxide (CO), generated primarily through degradation of heme from heme-proteins, have been shown to maintain physiological function of organs and to exert cytoprotective effects. However, high concentrations of carboxyhemoglobin (COHb), formed by CO binding to hemoglobin, potentially prevent adequate O2 delivery to tissues by lowering arterial O2 content. Elevated heme-protein concentrations, as found in marine mammals, are likely associated with greater heme degradation, more endogenous CO production and, consequently, elevated COHb concentrations. Therefore, we measured COHb in elephant seals, a species with large blood volumes and elevated hemoglobin and myoglobin concentrations. The levels of COHb were positively related to the total hemoglobin concentration. The maximum COHb value was 10.4% of total hemoglobin concentration. The mean (± s.e.m.) value in adult seals was 8.7 ± 0.3% (N=6), while juveniles and pups (with lower heme-protein contents) had lower mean COHb values of 7.6 ± 0.2% and 7.1 ± 0.3%, respectively (N=9 and N=9, respectively). Serial samples over several hours revealed little to no fluctuation in COHb values. This consistent elevation in COHb suggests that the magnitude and/or rate of heme-protein turnover is much higher than in terrestrial mammals. The maximum COHb values from this study decrease total body O2 stores by 7%, thereby reducing the calculated aerobic dive limit for this species. However, the constant presence of elevated CO in blood may also protect against potential ischemia-reperfusion injury associated with the extreme breath-holds of elephant seals. We suggest the elephant seal represents an ideal model for understanding the potential cytoprotective effects, mechanisms of action and evolutionary adaptation associated with chronically elevated concentrations of endogenously produced CO.
Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92093-0204, USA Department of Biology, Sonoma State University, Rohnert Park, CA 94928, USA mtift@ucsd.edu.
Michael S
MS
Tift
Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego, La Jolla, CA 92093-0204, USA.
Paul J
PJ
Ponganis
Department of Biology, Sonoma State University, Rohnert Park, CA 94928, USA.
Daniel E
DE
Crocker
D000818:Animals; D002248:Carbon Monoxide / Q000097:blood / Q000378:metabolism; D002263:Carboxyhemoglobin / Q000032:analysis* / Q000378:metabolism*; D004242:Diving; D005260:Female; D006418:Heme / Q000378:metabolism; D010100:Oxygen / Q000097:blood / Q000378:metabolism; D046048:Seals, Earless / Q000097:blood* / Q000378:metabolism / Q000502:physiology*
D006418:Heme; D002248:Carbon Monoxide; D002263:Carboxyhemoglobin; D010100:Oxygen
Calculated aerobic dive limit; Carbon monoxide; Hemoglobin absorption spectra; Marine mammal; Oxygen stores