TY - JOUR
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 -