Click here to close
Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly.
We suggest using a current version of Chrome,
FireFox, or Safari.
PLoS One
2020 Sep 21;159:e0236724. doi: 10.1371/journal.pone.0236724.
Show Gene links
Show Anatomy links
Aquaporin expression in the alimentary canal of the honey bee Apis mellifera L. (Hymenoptera: Apidae) and functional characterization of Am_Eglp 1.
Linhares Lino de Souza D
,
Serrão JE
,
Hansen IA
.
???displayArticle.abstract???
Aquaporins (AQP) are a family of plasma membrane proteins responsible for water transport through cell membranes. They are differentially expressed in different parts of the alimentary canal of insects where they regulate water transport. These proteins have been studied in detail in some insects, but few data are available for aquaporins of the honey bee, Apis mellifera. We used quantitative PCR to study the expression of six putative aquaporin genes in forager honey bees. We found differential expression of all putative AQP genes in crop, midgut, ileum, rectum and Malpighian tubules. We found the entomoglyceroporin Am_Eglp 1 expressed at extremely high levels in the midgut. We performed a functional characterization of Am_Eglp 1 using heterologous expression in Xenopus laevis oocyte followed by water uptake assays. Our results confirmed that the Am_Eglp 1 gene encodes a functional water transporter. This study shows that all putative honey bee aquaporin genes have complex expression patterns in the digestive and excretory organs of honey bee workers. Our results suggest that Am_Eglp 1 is the principal water transporter in the midgut of A. mellifera workers.
???displayArticle.pubmedLink???
32956406
???displayArticle.pmcLink???PMC7505460 ???displayArticle.link???PLoS One
Fig 1. Relative expression of aquaporins genes in the digestive tract and Malpighian tubules of A. mellifera forager workers.Shown are relative mRNA expression levels determined with qPCR. Values are means ± SD. Means separated by Tukey’s range test (p<0.05). Means which share the same letter are not significantly different. MT: Malpighian tubules.
Fig 2. Sequence analyses of Am_Eglp 1.A: Amino acid sequence alignment of aquaporins from different organisms with different mercury (HgCl2) sensitivity. Am_Eglp 1: A. mellifera entomoglyceroporin; Aquaporin 1: mammalian aquaporin; AQPcic: C. viridis aquaporin; AQP4: A. aegypti aquaporin. Amino acid residues identical to those in Am_Eglp 1 are shaded. NPA motifs are highlighted in a box. C: cysteine residues close to second NPA motif. B: Hydrophobicity profile of Am_Eglp 1. Numbers 1 through 6 are hydrophobic transmembrane domains. Arrow: NPA motifs. Arrowhead: cysteine position upstream to second NPA motif.
Fig 3. Functional characterization of Am_Eglp 1 via transient expression in Xenopus oocytes.A: Western Blot analysis of lysed oocytes, using anti myc-tag antibody. M: molecular weight. 1: Am_Eglp 1 cRNA injected oocytes. 2: water injected oocytes; 3: uninjected oocytes. Arrow: positive reaction of myc-tagged Am_Eglp 1. B: Permeability coefficient (Pf) analysis of oocytes expressing Am_Eglp 1 subjected to water uptake assay. Am_Eglp 1: oocytes expressing Am_Eglp 1 (n = 14). HgCl2: oocytes expressing Am_Eglp 1 and exposed to mercury prior to water uptake assay (n = 10). H2O: water injected oocytes (n = 6). Ø: non-injected oocytes (n = 9). Values are means ± SD. Means separated by Tukey (p<0.05). Means which share the same letter are not significantly different. C: Water uptake assay. Oocytes expressing Am_Eglp 1 submitted to hyposmotic schock demonstrated a gradual increase in volume due to water uptake throughout testing time. Arrow: cellular membrane rupture.
Azuma,
Two water-specific aquaporins at the apical and basal plasma membranes of insect epithelia: molecular basis for water recycling through the cryptonephric rectal complex of lepidopteran larvae.
2012, Pubmed,
Xenbase
Azuma,
Two water-specific aquaporins at the apical and basal plasma membranes of insect epithelia: molecular basis for water recycling through the cryptonephric rectal complex of lepidopteran larvae.
2012,
Pubmed
,
Xenbase
Benoit,
Aquaporins are critical for provision of water during lactation and intrauterine progeny hydration to maintain tsetse fly reproductive success.
2014,
Pubmed
Beyenbach,
Transport mechanisms of diuresis in Malpighian tubules of insects.
2003,
Pubmed
Campbell,
Invertebrate aquaporins: a review.
2008,
Pubmed
Denker,
Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules.
1988,
Pubmed
Doherty,
The Drosophila neurogenic gene big brain, which encodes a membrane-associated protein, acts cell autonomously and can act synergistically with Notch and Delta.
1997,
Pubmed
Douglas,
Phloem-sap feeding by animals: problems and solutions.
2006,
Pubmed
Drake,
Functional characterization of aquaporins and aquaglyceroporins of the yellow fever mosquito, Aedes aegypti.
2015,
Pubmed
,
Xenbase
Drake,
The Aquaporin gene family of the yellow fever mosquito, Aedes aegypti.
2010,
Pubmed
Duchesne,
Mosquito (Aedes aegypti ) aquaporin, present in tracheolar cells, transports water, not glycerol, and forms orthogonal arrays in Xenopus oocyte membranes.
2003,
Pubmed
,
Xenbase
Elsik,
Finding the missing honey bee genes: lessons learned from a genome upgrade.
2014,
Pubmed
Finn,
Insect glycerol transporters evolved by functional co-option and gene replacement.
2015,
Pubmed
,
Xenbase
Gonçalves,
Ultrastructure of the excretory organs of Bombus morio (Hymenoptera: Bombini): bee without rectal pads.
2014,
Pubmed
Gorin,
The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning.
1984,
Pubmed
Herraiz,
Identification and functional characterization of an ovarian aquaporin from the cockroach Blattella germanica L. (Dictyoptera, Blattellidae).
2011,
Pubmed
,
Xenbase
Jung,
Molecular structure of the water channel through aquaporin CHIP. The hourglass model.
1994,
Pubmed
,
Xenbase
Kataoka,
Aquaporin and aquaglyceroporin in silkworms, differently expressed in the hindgut and midgut of Bombyx mori.
2009,
Pubmed
,
Xenbase
Klatt,
Bee pollination improves crop quality, shelf life and commercial value.
2014,
Pubmed
Kumar,
MEGA7: Molecular Evolutionary Genetics Analysis Version 7.0 for Bigger Datasets.
2016,
Pubmed
Le Caherec,
Aquaporin-related proteins in the filter chamber of homopteran insects.
1997,
Pubmed
Le Cahérec,
Molecular cloning and characterization of an insect aquaporin functional comparison with aquaporin 1.
1996,
Pubmed
,
Xenbase
Liu,
Aquaporin water channel AgAQP1 in the malaria vector mosquito Anopheles gambiae during blood feeding and humidity adaptation.
2011,
Pubmed
,
Xenbase
Pfaffl,
A new mathematical model for relative quantification in real-time RT-PCR.
2001,
Pubmed
Philip,
The protective role of aquaporins in the freeze-tolerant insect Eurosta solidaginis: functional characterization and tissue abundance of EsAQP1.
2011,
Pubmed
,
Xenbase
Pieńkowska,
Molecular identification of first putative aquaporins in snails.
2014,
Pubmed
Preston,
Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.
1992,
Pubmed
,
Xenbase
Preston,
Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.
1991,
Pubmed
Preston,
The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel.
1993,
Pubmed
,
Xenbase
Rao,
Similarity of the product of the Drosophila neurogenic gene big brain to transmembrane channel proteins.
1990,
Pubmed
Savage,
Structural basis of aquaporin inhibition by mercury.
2007,
Pubmed
Serrão,
Aquaporins in the honeybee crop--a new function for an old organ.
2014,
Pubmed
Smith,
Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins.
1991,
Pubmed
Spring,
Localization of a Drosophila DRIP-like aquaporin in the Malpighian tubules of the house cricket, Acheta domesticus.
2007,
Pubmed
Tatsumi,
Drosophila big brain does not act as a water channel, but mediates cell adhesion.
2009,
Pubmed
Yanochko,
Regulated cationic channel function in Xenopus oocytes expressing Drosophila big brain.
2002,
Pubmed
,
Xenbase
