Cloning of an aquaporin‐like cDNA and <i>in situ</i> hybridization in adults of the mosquito <i>Aedes aegypti</i> (Diptera: Culicidae)

Pietrantonio, Patricia V.; Jagge, Christopher; Keeley, Larry L.; Ross, Linda S.

doi:10.1046/j.1365-2583.2000.00201.x

Cited by 57 publications

(77 citation statements)

References 69 publications

(91 reference statements)

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“…Beuron et al 1995;Le Caherec et al 1996a,b;Pietrantonio et al 2000). Aquaporins have been divided into two types: one subgroup is highly selective for the passage of water, and the other subgroup transports water as well as small neutral solutes such as glycerol.…”

Section: Introductionmentioning

confidence: 99%

Role of membrane transport of water and glycerol in the freeze tolerance of the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae)

Izumi

Sonoda

Yoshida

et al. 2006

Journal of Insect Physiology

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Overwintering larvae of the rice stem borer, Chilo suppressalis accumulate glycerol and are freezing tolerant to about -25°C. However, non-diapausing larvae cannot accumulate glycerol and are killed by freezing. We compared the extent of tissue damage, the effects of glycerol concentration, and the transport of glycerol and water in fat body tissues from these larvae at selected freezing temperatures. Tissues from overwintering larvae, but not non-diapausing larvae, survive when frozen at -20°C with 0.25M glycerol, but the protection afforded by glycerol is offset by the water-channel inhibitor mercuric chloride. Glycerol in higher concentration (0.75M) affords some protection even to the fat body of non-diapausing larvae. Radiotracer assays of overwintering larvae show that water leaves the tissues during freezing while glycerol enters, and that mercuric chloride disrupts this process. Transport is also disrupted after lethal freezing at -35°C. Therefore, membrane transport of water and glycerol is involved in the avoidance of freezing injury to fat body cells of the rice stem borer, apparently by mediating the replacement of water with glycerol in freezing-tolerant tissues.

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Section: Introductionmentioning

confidence: 99%

Role of membrane transport of water and glycerol in the freeze tolerance of the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae)

Izumi

Sonoda

Yoshida

et al. 2006

Journal of Insect Physiology

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“…Alternatively, at rest, the fluid volume increases and the rate of diffusion is slower. The aquaporin located in the tracheole ends has been called AeaAQP [24]. The water channel built by this aquaporin takes part in the regulation of the fluid volume in the respiratory system [24].…”

Section: Aquaporin Identified In Mosquito Aedes Aegyptimentioning

confidence: 99%

“…The aquaporin located in the tracheole ends has been called AeaAQP [24]. The water channel built by this aquaporin takes part in the regulation of the fluid volume in the respiratory system [24]. An important feature is that aquaporins have been found in the ends of tracheoles are closely associated with the Malpighian tubules.…”

Section: Aquaporin Identified In Mosquito Aedes Aegyptimentioning

confidence: 99%

“…AeaAQP is a protein composed of 249 residues (26.1kDa) [24]. Comparison of this amino acid sequence with well-known proteins of water channels in other organisms allows the following features to be concluded: (1) the sensitivity of the mercury ions, as previously mentioned, which can inhibit transport through the water pore, (2) responsibility of the binding of mercury ions, and as a consequence, the blockage of water permeability, is likely caused by a cysteine at position 79 localized near the NPA motif in loop B (Fig.…”

Section: Aquaporin Identified In Mosquito Aedes Aegyptimentioning

confidence: 99%

“…Based on the amino acid sequence, it can be concluded that this protein is kinase independent (lacks sequence Arg-Arg-X-Ser), as it lacks a phosphorylation site. On the other hand, there is a potential N-glycosylation site in loop E (Asn211-Trp212-Thr213) [24]. …”

Section: Aquaporin Identified In Mosquito Aedes Aegyptimentioning

confidence: 99%

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The Current Knowledge of Invertebrate Aquaporin Water Channels with Particular Emphasis on Insect AQPs

Tomkowiak¹,

Pieńkowska²

2010

Advances in Cell Biology

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Summary: Aquaporins (AQPs) or water channels are some of the most ubiquitous integral membrane proteins, and are present in all living organisms. Their presence in the lipid bilayer of cell membranes considerably increases their permeability to water and, in some cases, to other small solutes. All AQPs, identified thus far, share the same structure, comprising of six transmembrane segments and two conserved regions forming the pore. Depending on the transported solutes, AQPs can be divided into two classes: 'classical' aquaporins (permeable only to water) and aquaglyceroporins (permeable also to glycerol and/or other solutes). Many subtypes of AQPs coexist in a single organism. Localization of particular subtypes of AQPs is tissue-specific. AQPs have been well characterized in almost all vertebrate classes. However, little is known about their counterparts in invertebrates. Most of the water channels characterized in invertebrates are found in insects. Therefore, the knowledge of aquaporins in invertebrates is generally limited to the information concerning water channels in this class of organism. Insects are characterized by an astonishing variety of physiological adaptations, notable in their feeding strategies or survival strategies in hostile environments. An example of such, is feeding on blood, or tolerating extreme cold or drought. It is likely that many of these adaptation patterns emerged due to the expression and regulation of particular aquaporins. Here we review the current state of knowledge of invertebrate AQPs (of insects and nematodes) and compare their structure and function with mammalian water channels.

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Water channel proteins (later called aquaporins) and relatives: Past, present, and future

Benga

2009

IUBMB Life

119

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SummaryWater channels or water channel proteins (WCPs) are transmembrane proteins that have a specific three-dimensional structure with a pore that can be permeated by water molecules. WCPs are large families (over 450 members) that are present in all kingdoms of life. The first WCP was discovered in the human red blood cell (RBC) membrane in 1980s. In 1990s other WCPs were discovered in plants, microorganisms, various animals, and humans; and it became obvious that the WCPs belong to the superfamily of major intrinsic proteins (MIPs, over 800 members). WCPs include three subfamilies: (a) aquaporins (AQPs), which are water specific (or selective water channels); (b) aquaglyceroporins (and glycerol facilitators), which are permeable to water and/or other small molecules; and (c) ''superaquaporins'' or subcellular AQPs. WCPs (and MIPs) have several structural characteristics which were better understood after the atomic structure of some MIPs was deciphered. The structure-function relationships of MIPs expressed in microorganisms (bacteria, archaea, yeast, and protozoa), plants, and some multicellular animal species [nematodes, insects, fishes, amphibians, mammals (and humans)] are described. A synthetic overview on the WCPs from RBCs from various species is provided. The physiological roles of WCPs in kidney, gastrointestinal system, respiratory apparatus, central nervous system, eye, adipose tissue, skin are described, and some implications of WCPs in various diseases are briefly presented. References of detailed reviews on each topic are given. This is the first review providing in a condensed form an overview of the whole WCP field that became in the last 20 years a very hot area of research in biochemistry and molecular cell biology, with wide and increasing implications.

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Cloning of an aquaporin‐like cDNA and in situ hybridization in adults of the mosquito Aedes aegypti (Diptera: Culicidae)

Cited by 57 publications

References 69 publications

Role of membrane transport of water and glycerol in the freeze tolerance of the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae)

Role of membrane transport of water and glycerol in the freeze tolerance of the rice stem borer, Chilo suppressalis Walker (Lepidoptera: Pyralidae)

The Current Knowledge of Invertebrate Aquaporin Water Channels with Particular Emphasis on Insect AQPs

Water channel proteins (later called aquaporins) and relatives: Past, present, and future

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