New isoforms of rat Aquaporin-4.

Svein Erik Moe; Jan Gunnar Sorbo; Rikke Søgaard; Thomas Zeuthen; Ole Petter Ottersen; Torgeir Holen

doi:10.1016/j.ygeno.2007.12.003

New isoforms of rat Aquaporin-4.

Svein Erik Moe, Jan Gunnar Sorbo, Rikke Søgaard, Thomas Zeuthen, Ole Petter Ottersen, Torgeir Holen

79 Citations (Scopus)

Abstract

Aquaporin-4 (AQP4) is a brain aquaporin implicated in the pathophysiology of numerous clinical conditions including brain edema. Here we show that rat AQP4 has six cDNA isoforms, formed by alternative splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond to the two classical M1 and M23 isoforms, respectively. The various isoforms are differentially expressed in kidney and brain, and their prevalence does not correspond to the level of the respective mRNAs, pointing to posttranscriptional regulation. The three isoforms lacking exon 2, AQP4b, AQP4d, and AQP4f, have an intracellular localization when expressed in cell lines and do not transport water when expressed in Xenopus oocytes. In contrast, the largest of the new isoforms, AQP4e, which contains a novel N-terminal domain, is localized at the plasma membrane in cell lines and functions as a water transporter in Xenopus oocytes.

Original language	English
Journal	Genomics
Volume	91
Issue number	4
Pages (from-to)	367-77
Number of pages	10
ISSN	0888-7543
DOIs	https://doi.org/10.1016/j.ygeno.2007.12.003
Publication status	Published - 2008

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title = "New isoforms of rat Aquaporin-4.",

abstract = "Aquaporin-4 (AQP4) is a brain aquaporin implicated in the pathophysiology of numerous clinical conditions including brain edema. Here we show that rat AQP4 has six cDNA isoforms, formed by alternative splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond to the two classical M1 and M23 isoforms, respectively. The various isoforms are differentially expressed in kidney and brain, and their prevalence does not correspond to the level of the respective mRNAs, pointing to posttranscriptional regulation. The three isoforms lacking exon 2, AQP4b, AQP4d, and AQP4f, have an intracellular localization when expressed in cell lines and do not transport water when expressed in Xenopus oocytes. In contrast, the largest of the new isoforms, AQP4e, which contains a novel N-terminal domain, is localized at the plasma membrane in cell lines and functions as a water transporter in Xenopus oocytes.",

author = "Moe, {Svein Erik} and Sorbo, {Jan Gunnar} and Rikke S{\o}gaard and Thomas Zeuthen and {Petter Ottersen}, Ole and Torgeir Holen",

note = "Keywords: Alternative Splicing; Animals; Aquaporin 4; Base Sequence; Cell Line; DNA Primers; DNA, Complementary; Hela Cells; Humans; Protein Isoforms; RNA, Messenger; Rats; Subcellular Fractions",

year = "2008",

doi = "10.1016/j.ygeno.2007.12.003",

language = "English",

volume = "91",

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T1 - New isoforms of rat Aquaporin-4.

AU - Moe, Svein Erik

AU - Sorbo, Jan Gunnar

AU - Søgaard, Rikke

AU - Zeuthen, Thomas

AU - Petter Ottersen, Ole

AU - Holen, Torgeir

N1 - Keywords: Alternative Splicing; Animals; Aquaporin 4; Base Sequence; Cell Line; DNA Primers; DNA, Complementary; Hela Cells; Humans; Protein Isoforms; RNA, Messenger; Rats; Subcellular Fractions

PY - 2008

Y1 - 2008

N2 - Aquaporin-4 (AQP4) is a brain aquaporin implicated in the pathophysiology of numerous clinical conditions including brain edema. Here we show that rat AQP4 has six cDNA isoforms, formed by alternative splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond to the two classical M1 and M23 isoforms, respectively. The various isoforms are differentially expressed in kidney and brain, and their prevalence does not correspond to the level of the respective mRNAs, pointing to posttranscriptional regulation. The three isoforms lacking exon 2, AQP4b, AQP4d, and AQP4f, have an intracellular localization when expressed in cell lines and do not transport water when expressed in Xenopus oocytes. In contrast, the largest of the new isoforms, AQP4e, which contains a novel N-terminal domain, is localized at the plasma membrane in cell lines and functions as a water transporter in Xenopus oocytes.

AB - Aquaporin-4 (AQP4) is a brain aquaporin implicated in the pathophysiology of numerous clinical conditions including brain edema. Here we show that rat AQP4 has six cDNA isoforms, formed by alternative splicing. These are named AQP4a-f, where AQP4a and AQP4c correspond to the two classical M1 and M23 isoforms, respectively. The various isoforms are differentially expressed in kidney and brain, and their prevalence does not correspond to the level of the respective mRNAs, pointing to posttranscriptional regulation. The three isoforms lacking exon 2, AQP4b, AQP4d, and AQP4f, have an intracellular localization when expressed in cell lines and do not transport water when expressed in Xenopus oocytes. In contrast, the largest of the new isoforms, AQP4e, which contains a novel N-terminal domain, is localized at the plasma membrane in cell lines and functions as a water transporter in Xenopus oocytes.

U2 - 10.1016/j.ygeno.2007.12.003

DO - 10.1016/j.ygeno.2007.12.003

M3 - Journal article

C2 - 18255256

SN - 0888-7543

VL - 91

SP - 367

EP - 377

JO - Genomics

JF - Genomics

IS - 4

ER -

New isoforms of rat Aquaporin-4.

Abstract

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