Dolan, E, Warren, DE, Harris, RC, Sale, C ORCID: https://orcid.org/0000-0002-5816-4169, Gualano, B and Saunders, B, 2021. Skeletal muscle histidine-containing dipeptide contents are increased in freshwater turtles (C. picta bellii) with cold-acclimation. Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 262: 111071. ISSN 1095-6433
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Abstract
Freshwater turtles found in higher latitudes can experience extreme challenges to acid-base homeostasis while overwintering, due to a combination of cold temperatures along with the potential for environmental hypoxia. Histidine-containing dipeptides (HCDs; carnosine, anserine and balenine) may facilitate pH regulation in response to these challenges, through their role as pH buffers. We measured the HCD content of three tissues (liver, cardiac and skeletal muscle) from the anoxia-tolerant painted turtle (C. picta bellii) acclimated to either 3 or 20 °C. HCDs were detected in all tissues, with the highest content shown in the skeletal muscle. Turtles acclimated to 3 °C had more HCD in their skeletal muscle than those acclimated to 20 °C (carnosine = 20.8 ± 4.5 vs 12.5 ± 5.9 mmol·kg DM−1; ES = 1.59 (95%CI: 0.16–3.00), P = 0.013). The higher HCD content shown in the skeletal muscle of the cold-acclimated turtles suggests a role in acid-base regulation in response to physiological challenges associated with living in the cold, with the increase possibly related to the temperature sensitivity of carnosine's dissociation constant.
Item Type: | Journal article |
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Publication Title: | Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology |
Creators: | Dolan, E., Warren, D.E., Harris, R.C., Sale, C., Gualano, B. and Saunders, B. |
Publisher: | Elsevier |
Date: | December 2021 |
Volume: | 262 |
ISSN: | 1095-6433 |
Identifiers: | Number Type 10.1016/j.cbpa.2021.111071 DOI 1473030 Other |
Divisions: | Schools > School of Science and Technology |
Record created by: | Jonathan Gallacher |
Date Added: | 06 Oct 2021 08:31 |
Last Modified: | 04 Sep 2022 03:00 |
URI: | https://irep.ntu.ac.uk/id/eprint/44313 |
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