Expression and immunolocalization of water-channel aquaporins in the rat and mouse mammary gland

Matsuzaki, Toshiyuki; Machida, Natsuko; Tajika, Yuki; Ablimit, Abdushukur; Suzuki, Takeshi; Aoki, Takeo; Hagiwara, Haruo; Takata, Kuniaki

doi:10.1007/s00418-005-0753-x

Cited by 59 publications

(53 citation statements)

References 25 publications

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“…It was originally called GLIP (glycerol intrinsic protein) [29]. AQP3 is expressed in a wide variety of organs such as the kidney, digestive tract, respiratory tract, skin, eye, mammary gland, and brain [32,37].…”

Section: Distribution Of Aquaporins In the Bodymentioning

confidence: 99%

Aquaporin Water Channels in the Kidney

Takata

Matsuzaki

Tajika

et al. 2005

Acta Histochem. Cytochem

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Section: Distribution Of Aquaporins In the Bodymentioning

confidence: 99%

Aquaporin Water Channels in the Kidney

Takata

Matsuzaki

Tajika

et al. 2005

Acta Histochem. Cytochem

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“…Affinity-purified rabbit polyclonal antibodies to rat/ mouse AQP1 (AffRaTM31) and affinity-purified guinea pig polyclonal antibodies to rat/mouse AQP1 (AffGPTM31) were described previously [9]. Other antibodies to aquaporin isoforms were as described [19].…”

Section: Antibodiesmentioning

confidence: 99%

Water Channel Aquaporin 1 (AQP1) Is Present in the Perineurium and Perichondrium

Matsuzaki

Ablimit

Tajika

et al. 2005

Acta Histochem. Cytochem

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Aquaporin 1 (AQP1) is an isoform of membrane water channels. We examined the distribution of AQP1 in peripheral nerves. Immunofluorescence microscopy with specific antibodies to AQP1 was performed in the tissue sections of the rat tongue, esophagus, trachea, and sciatic nerve. AQP1 was present in the perineurium of nerve fiber bundles in the sciatic nerve and nerve fiber bundles in the tongue, esophagus, and trachea. Laser confocal microscopy of the double-labeled specimens for AQP1 and sugar transporter GLUT1 revealed that AQP1 was localized in the outer layer(s) of the perineurial cell layers, whereas GLUT1 was present throughout the entire perineurial cell layers. AQP1 and GLUT1 were also present in blood vessels inside the nerve fiber bundle. They were rarely found in the same blood vessels, namely, AQP1 was hardly detectable in GLUT1-positive blood vessels and GLUT1 was hardly detectable in AQP1-positive vessels. AQP1 in these sites of the blood-nerve barrier may participate in the water transfer across the barrier and contribute to the maintenance of the milieu of the nerve. In addition, we showed the presence of AQP1 in the perichondrium of the tracheal cartilage suggesting a possible role in water transfer between the cartilage and surrounding connective tissues.

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“…This Prl-Ncc link may contribute to hypertension in pregnant women (Rojas-Vega et al 2015). Moreover, Aqp3 was localized to secretory alveolar cells of the rat mammary gland, but functional regulation of Aqp3 in this context remains unresolved (Matsuzaki et al 2005). Future work in euryhaline fishes will thus continue to provide insight into how highly plastic osmoregulatory systems are regulated while simultaneously revealing conserved modes of hormone action in vertebrates.…”

Section: :3mentioning

confidence: 99%

Hormonal regulation of aquaporin 3: opposing actions of prolactin and cortisol in tilapia gill

Breves

Inokuchi

Yamaguchi

et al. 2016

Journal of Endocrinology

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Aquaporins (Aqps) are expressed within key osmoregulatory tissues where they mediate the movement of water and selected solutes across cell membranes. We leveraged the functional plasticity of Mozambique tilapia (Oreochromis mossambicus) gill epithelium to examine how Aqp3, an aquaglyceroporin, is regulated in response to osmoregulatory demands. Particular attention was paid to the actions of critical osmoregulatory hormones, namely, prolactin (Prl), growth hormone and cortisol. Branchial aqp3 mRNA levels were modulated following changes in environmental salinity, with enhanced aqp3 mRNA expression upon transfer from seawater to freshwater (FW). Accordingly, extensive Aqp3 immunoreactivity was localized to cell membranes of branchial epithelium in FW-acclimated animals. Upon transferring hypophysectomized tilapia to FW, we identified that a pituitary factor(s) is required for Aqp3 expression in FW. Replacement with ovine Prl (oPrl) was sufficient to stimulate Aqp3 expression in hypophysectomized animals held in FW, an effect blocked by coinjection with cortisol. Both oPrl and native tilapia Prls (tPrl 177 and tPrl 188 ) stimulated aqp3 in incubated gill filaments in a concentration-related manner. Consistent with in vivo responses, coincubation with cortisol blocked oPrl-stimulated aqp3 expression in vitro. Our data indicate that Prl and cortisol act directly upon branchial epithelium to regulate Aqp3 in tilapia. Thus, within the context of the diverse actions of Prl on hydromineral balance in vertebrates, we define a new role for Prl as a regulator of Aqp expression.

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Expression and immunolocalization of water-channel aquaporins in the rat and mouse mammary gland

Cited by 59 publications

References 25 publications

Aquaporin Water Channels in the Kidney

Aquaporin Water Channels in the Kidney

Water Channel Aquaporin 1 (AQP1) Is Present in the Perineurium and Perichondrium

Hormonal regulation of aquaporin 3: opposing actions of prolactin and cortisol in tilapia gill

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