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Elucidation of the role of aquaporins and glyceroporins in freeze tolerance of Hyla chrysoscelis
Author(s) -
Wysong Robert,
Smith Aubrey,
Goldstein David
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.629.9
Subject(s) - aquaporin , biology , hyla , xenopus , tree frog , genetics , microbiology and biotechnology , gene , zoology
Cope's gray tree frog (Hyla chrysoscelis) can tolerate freezing of its extracellular water. While the exact mechanism of freeze tolerance is unknown, aquaporins may play a role by allowing water and solutes like glycerol to move between compartments prior to and during freezing. Previously, two aquaporins (HC1, HC2) and one glyceroporin (HC3) were identified in Hyla chrysoscelis in a tissue and temperature dependent manner. To further elucidate the role of aquaporins in freeze tolerance, three putative aquaporins (HC7, HC8 and HC0) have been identified. Degenerate PCR primers were developed using conserved amino acid regions from Xenopus tropicalis and compared to other species with high sequence homology. For the putative aquaporins, mRNA was isolated from the fat, large intestines, and the eye for HC7, HC8 and HC0 respectively. The templates were amplified using RT‐PCR and products (326 bp, 377 bp and 400 bp respectively) were examined by electrophoresis. Further experiments are underway to confirm these putative aquaporins, and to examine their tissue and temperature dependence. Supported by NSF IOB‐0517301.