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Dehydration-inducible changes in expression of two aquaporins in the sleeping chironomid, Polypedilum vanderplanki

Authors
  • Kikawada, Takahiro
  • Saito, Ayako
  • Kanamori, Yasushi
  • Fujita, Mika
  • Śnigórska, Katarzyna
  • Watanabe, Masahiko
  • Okuda, Takashi
Type
Published Article
Journal
Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher
Elsevier
Publication Date
Jan 01, 2007
Accepted Date
Nov 07, 2007
Volume
1778
Issue
2
Pages
514–520
Identifiers
DOI: 10.1016/j.bbamem.2007.11.009
Source
Elsevier
Keywords
License
Unknown

Abstract

Aquaporin, AQP, is a channel protein that allows water to permeate across cell membranes. Larvae of the sleeping chironomid, Polypedilum vanderplanki, can withstand complete dehydration by entering anhydrobiosis, a state of suspended animation; however, the mechanism by which water flows out of the larval body during dehydration is still unclear. We isolated two cDNAs ( PvAqp1 and PvAqp2) encoding water-selective aquaporins from the chironomid. When expressed in Xenopus oocytes, PvAQP1 and PvAQP2 facilitated permeation of water but not glycerol. Northern blots and in situ hybridization showed that expression of PvAqp1 was dehydration-inducible and ubiquitous whereas that of PvAqp2 was dehydration-repressive and fat body-specific. These data suggest distinct roles for these aquaporins in P. vanderplanki, i.e., PvAqp2 controls water homeostasis of fat body during normal conditions and PvAqp1 is involved in the removal of water during induction of anhydrobiosis.

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