Identification and functional characterization of an ovarian aquaporin from the cockroach <i>Blattella germanica</i> L. (Dictyoptera, Blattellidae)

Herraiz, Alba; Chauvigné, François; Cerdà, Joan; Bellés, Xavier; Piulachs, María‐Dolors

doi:10.1242/jeb.067009

Cited by 8 publications

(8 citation statements)

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“…1 mM of urea was added to AQP3-expressing oocytes and after a 10 minute incubation, the oocytes had an intracellular urea concentration of ~75 μM (assuming an oocyte volume of 1 μL) [19]. This is ~10% of the expected equilibrium value, and the fact that it is still so far from equilibrium even after 10 minutes suggests that urea transport through AQP3, whilst non-zero, is very slow.…”

Section: Which Mammalian Aqps Are Urea Channels?mentioning

confidence: 99%

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Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

Kitchen

Day

Salman

et al. 2015

Biochimica et Biophysica Acta (BBA) - General Subjects

129

115

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BACKGROUND: Aquaporin (AQP) water channels are best known as passive transporters of water that are vital for water homeostasis. SCOPE OF REVIEW:AQP knockout studies in whole animals and cultured cells, along with naturally occurring human mutations suggest that the transport of neutral solutes through AQPs has important physiological roles. Emerging biophysical evidence suggests that AQPs may also facilitate gas (CO2) and cation transport. AQPs may be involved in cell signalling for volume regulation and controlling the subcellular localization of other proteins by forming macromolecular complexes. This review examines the evidence for these diverse functions of AQPs as well their physiological relevance. MAJOR CONCLUSIONS:As well as being crucial for water homeostasis, AQPs are involved in physiologically important transport of molecules other than water, regulation of surface expression of other membrane proteins, cell adhesion, and signalling in cell volume regulation. GENERAL SIGNIFICANCE:Elucidating the full range of functional roles of AQPs beyond the passive conduction of water will improve our understanding of mammalian physiology in health and disease. The functional variety of AQPs makes them an exciting drug target and could provide routes to a range of novel therapies.3

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Section: Which Mammalian Aqps Are Urea Channels?mentioning

confidence: 99%

“…human AQPs 7, 9 and 10) are also permeable to urea. The urea permeability of AQP3 is controversial, with some studies reporting urea transport and others no transport [15,[17][18][19]. This may be due to methodological differences, and is discussed in detail in section 4.2.1.…”

Section: The Principles Of Solute Selectivity By Aqps Remain To Be Esmentioning

confidence: 99%

Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

Kitchen

Day

Salman

et al. 2015

Biochimica et Biophysica Acta (BBA) - General Subjects

129

115

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“…AQP-Bom2 (GLP) showed sequence similarity with a different group of insect AQPs from the DRIP and PRIP subfamilies (see Fig.5; Kataoka et al, 2009a;Kambara et al, 2009) and is classified into the structurally miscellaneous AQPs in the Group 3 (or GLP-like) clade, which appears as the sister group of DRIP, PRIP and BIB, are functionally heterogeneous (Herraiz et al, 2011). Recently, a second AQP gene (ApAQP2) from the pea aphid, Acyrthosiphon pisum, has been identified and categorised into Group 3, in which the members bear novel structures, including irregular NPA boxes (Wallace et al, 2012).…”

Section: Aquaglyceroporin-like Aqp In the Midgut Of Anomala Cupreamentioning

confidence: 99%

Identification and characterisation of functional aquaporin water channel (Anomala cuprea DRIP) in a coleopteran insect

Nagae

Miyake

Kosaki

et al. 2013

Journal of Experimental Biology

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SUMMARYWater transport across the plasma membrane depends on the presence of the water channel aquaporin (AQP), which mediates the bulk movement of water through osmotic and pressure gradients. In terrestrial insects, which are solid and/or plant feeders, the entrance and exit of water is primarily executed along the alimentary tract, where the hindgut, particularly the rectum, is the major site of water conservation. A cDNA encoding the homologue of the water-specific Drosophila AQP [Drosophila integral protein ( Supplementary material available online at

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“…However, only a very small fraction of insect aquaporins have been functionally characterized by sensitivity to mercuric ions, knockout (aquaporin‐deficient) organisms and functional system assays (Kaufmann et al ., ; Cohen, ; Tzin et al ., ; Van Ekert et al ., ). Insect Drips (Kaufmann et al ., ; Raza et al ., ; Shakesby et al ., ; Tzin et al ., ; Van Ekert et al ., ), Prips (Kikawada et al ., ; Herraiz et al ., ; Tzin et al ., ; Van Ekert et al ., ) and Eglps (Van Ekert et al ., ) have been confirmed to be involved in water permeability. Moreover, using in vivo RNA interference (RNAi; knockdown) techniques, inhibitory or modified effects have been documented in plant sap‐sucking and blood‐feeding insect species (Cohen, ; Jing et al ., ; Van Ekert et al ., ; Tsujimoto et al ., ).…”

Section: Introductionmentioning

confidence: 99%

RNA interference‐mediated functional characterization of aquaporin genes in Tribolium castaneum

Yao

Meng

2017

Insect Molecular Biology

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An obvious challenge faced by most terrestrial insects is maintaining water homeostasis in an arid environment. Current research suggests aquaporins may be evolved to meet the challenge. However, up to now, this suggestion has not been verified in any insect that feeds upon solid food with mandibulate mouthparts. In the present paper, nine putative aquaporin genes [Tribolium castaneum big brain, T. castaneum Drosophila integral protein (TcDrip), T. castaneum Pyrocoelia rufa integral protein (TcPrip), T. castaneum aquaporin 12-like, T. castaneum entomoglyceroporin 1 (TcEglp1), TcEglp2, TcEglp3, TcEglp4 and TcEglp5] were identified in T. castaneum. The transcripts of the nine genes were easily detectable in the foregut, midgut, hindgut-Malpighian tubule complex, fat body and carcass (except gut and fat body). Amongst them TcDrip, TcPrip, TcEglp1, TcEglp3 and TcEglp5 were highly transcribed in the hindgut-Malpighian tubule complex; TcEglp4 was abundantly expressed in both the fat body and hindgut-Malpighian tubule complex. RNA interference (RNAi)-mediated knockdown of TcEglp3 caused a grey larval cuticle, in contrast to a smooth and bright cuticle in control larvae. Approximately 40% of the TcEglp3 RNAi larvae had their hindguts protruding from the anus; their fresh wet faeces were attached to the hindgut. Another 20% of these treated larvae did not defaecate normally; wet brown faeces were adhered to the anal area. As a result, the larval growth was inhibited and about 60% larval lethality occurred. Silencing of TcEglp4 or TcDrip exhibited similar but weaker defective phenotypes as those of the TcEglp3-silenced larvae. Therefore, Eglp3, Eglp4 and Drip may contribute to the conductance of water in the alimentary canal and Malpighian tubules in T. castaneum.

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Identification and functional characterization of an ovarian aquaporin from the cockroach Blattella germanica L. (Dictyoptera, Blattellidae)

Abstract: We apologise to authors and readers for any inconvenience this error may have caused.3895 Erratum

Cited by 8 publications

References 0 publications

Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

Beyond water homeostasis: Diverse functional roles of mammalian aquaporins

Identification and characterisation of functional aquaporin water channel (Anomala cuprea DRIP) in a coleopteran insect

RNA interference‐mediated functional characterization of aquaporin genes in Tribolium castaneum

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