Term of Award

Fall 2025

Degree Name

Master of Science in Biology (M.S.)

Document Type and Release Option

Thesis (open access)

Copyright Statement / License for Reuse

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.

Department

Department of Biology

Committee Chair

Christopher Cutler

Committee Member 1

John Scott Harrison

Committee Member 2

Johanne Lewis

Abstract

Aquaporins (AQPs) are integral membrane proteins that facilitate the selective transport of water and small solutes across cell membranes, playing essential roles in maintaining osmotic balance in vertebrates. Among them, aquaglyceroporins such as AQP10 are capable of transporting water, glycerol, and urea, contributing to osmoregulatory and metabolic processes. This study investigated the expression, localization, and potential physiological roles of two AQP10 paralogs, AQP10C1 and AQP10C2, in the spiny dogfish (Squalus acanthias), a marine elasmobranch that maintains osmotic equilibrium through urea retention and ion regulation. Using RT-PCR, quantitative PCR, Western blotting and immunohistochemistry the study identified tissue-specific expression patterns of both paralogs. AQP10C1 transcripts were predominantly detected in the gill, with expression levels increasing significantly under hypersaline (120% seawater) conditions, suggesting a role in osmotically driven water or solute transport across the gill epithelium. AQP10C2 expression was localized mainly to the kidney and intestinal tissues, with evidence of multiple splice variants, including an alternative 5′ end and a mid-splice form, indicating functional and regulatory diversity. Immunostaining revealed AQP10C2 localization in endocrine-like cells between nephrons and in large enteroendocrine and/or paneth cells of the intestinal epithelium, with a possible AQP10C2 peptide product potentially being secreted. Western blot analyses supported the presence of both paralogs at around the expected molecular weights, though potential post-translational modifications or oligomeric forms were also observed. Collectively, these findings suggest that AQP10C1 and AQP10C2 have distinct yet complementary roles in the osmoregulatory physiology of S. acanthias, likely contributing to water and solute transport and potentially regulating intestinal function.

Research Data and Supplementary Material

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