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Aquaporins ( AQP ) are among the most common cell membrane integral proteins present in all living organisms. Not built by the presence of water channels in the plasma membrane phospholipid bilayer greatly increases its permeability to water molecules and in some cases also for other small chemical compounds. All presently identified aquaporins are characterized by the same structure , which is typical for the presence of six transmembrane domains and two conserved motifs in the linings cf. Depending on the transported substance , aquaporins can be divided into two main classes : aquaporins (rear channels permeable to water only ) and aquaglyceroporin ( also permeable channels for glycerol and / or other compounds ) . In an organism , there are many different aquaporins simultaneously. It has been shown that the localization is tissue- specific. Most of the water channels previously characterized proteins insect invertebrates . Thus, and all knowledge of aquaporins in invertebrates essentially boils down to information on water channels in this group of animals. These animals are characterized by the astonishing variety of physiological adaptations , especially visible on the example of eating strategies or ways to survive in a hostile environment . An example of such adaptation may be , inter alia, feeding on large volumes of fluids (eg blood ) or tolerating extreme cold or drought. It seems to be obvious that many of these adjustments was made possible through adjustment of the relative expression and aquaporins . In this review presents the current state of knowledge of aquaporins located in invertebrates ( insects and nematodes ) and a comparison of their structure and function of the best ever audited mammalian aquaporins.
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The Editorial Board
Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

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