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To elucidate the molecular mechanisms underling hydration during oocyte maturation, we characterized the structure of Japanese eel ( Anguilla japonica ) novel-water selective aquaporin 1 (AQP1b) that thought to be involved in oocyte hydration. The  aqp1b  cDNA encodes a 263 amino acid protein that includes the six potential transmembrane domains and two Asn-Pro-Ala motifs. Reverse transcription-polymerase chain reaction showed transcription of Japanese eel  aqp1b  in ovary and testis but not in the other tissues.  In situ  hybridization studies with the eel  aqp1b  cRNA probe revealed intense eel  aqp1b  signal in the oocytes at the perinucleolus stage and the signals became faint during the process of oocyte development. Light microscopic immunocytochemical analysis of ovary revealed that the Japanese eel AQP1b was expressed in the cytoplasm around the yolk globules which were located in the peripheral region of oocytes during the primary yolk globule stage; thereafter, the immunoreactivity was observed throughout the cytoplasm of oocyte as vitellogenesis progressed. The immunoreactivity became localized around the large membrane-limited yolk masses which were formed by the fusion of yolk globules during the oocyte maturation phase. These results together indicate that AQP1b, which is synthesized in the oocyte during the process of oocyte growth, is essential for mediating water uptake into eel oocytes.

Expression and localization of aquaporin 1b during oocyte development in the Japanese eel (Anguilla japonica)