Two isoforms of aquaporin 2 responsive to hypertonic stress in the bottlenose dolphin

This study investigated the expression of aquaporin 2 (AQP2) and its newly found alternatively spliced isoform (alternative AQP2) and the functions of these AQP2 isoforms in the cellular hyperosmotic tolerance in the bottlenose dolphin, ITALIC! Tursiops truncatus mRNA sequencing revealed that altern...

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Bibliographic Details
Published in:	Journal of experimental biology Vol. 219; no. Pt 8; pp. 1249 - 1258
Main Authors:	Suzuki, Miwa, Wakui, Hitomi, Itou, Takuya, Segawa, Takao, Inoshima, Yasuo, Maeda, Ken, Kikuchi, Kiyoshi
Format:	Journal Article
Language:	English
Published:	England 15-04-2016
Subjects:	Amino Acid Sequence Animals Aquaporin 2 - chemistry Aquaporin 2 - genetics Aquaporin 2 - metabolism Bottle-Nosed Dolphin - physiology Cell Death - drug effects Cell Membrane Permeability - drug effects Cells, Cultured Conserved Sequence - genetics DNA, Complementary - genetics DNA, Complementary - isolation & purification Gene Expression Profiling Gene Knockdown Techniques Hypertonic Solutions - pharmacology Introns - genetics Kidney - drug effects Kidney - metabolism Mannitol - pharmacology Oocytes - drug effects Oocytes - metabolism Open Reading Frames - genetics Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - metabolism RNA Interference - drug effects RNA Splicing - drug effects RNA Splicing - genetics RNA, Small Interfering - metabolism Sodium Chloride - pharmacology Software Stress, Physiological - drug effects Transcription, Genetic - drug effects Water Alternative splicing Cellular osmoregulation Osmotic tolerance Cetacea
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Summary:	This study investigated the expression of aquaporin 2 (AQP2) and its newly found alternatively spliced isoform (alternative AQP2) and the functions of these AQP2 isoforms in the cellular hyperosmotic tolerance in the bottlenose dolphin, ITALIC! Tursiops truncatus mRNA sequencing revealed that alternative AQP2 lacks the fourth exon and instead has a longer third exon that includes a part of the original third intron. The portion of the third intron, now part of the coding region of alternative AQP2, is highly conserved among many species of the order Cetacea but not among terrestrial mammals. Semi-quantitative PCR revealed that AQP2 was expressed only in the kidney, similar to terrestrial mammals. In contrast, alternative AQP2 was expressed in all organs examined, with strong expression in the kidney. In cultured renal cells, expression of both AQP2 isoforms was upregulated by the addition to the medium of NaCl but not by the addition of mannitol, indicating that the expression of both isoforms is induced by hypersalinity. Treatment with small interfering RNA for both isoforms resulted in a decrease in cell viability in hypertonic medium (500 mOsm kg(-1)) when compared with controls. These findings indicate that the expression of alternatively spliced AQP2 is ubiquitous in cetacean species, and it may be one of the molecules important for cellular osmotic tolerance throughout the body.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0022-0949 1477-9145
DOI:	10.1242/jeb.132811