Expression of a mammalian aquaporin 3 homolog in the anterior pituitary gonadotrophs of the tree frog, Hyla japonica

Sato, Megumi; Nakakura, Takashi; Ogushi, Yuji; Akabane, Gen; Kurabuchi, Shingo; Suzuki, Masakazu; Tanaka, Shigeyasu

doi:10.1007/s00441-010-1122-1

Cited by 6 publications

(3 citation statements)

References 31 publications

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“…Therefore, it would not be able to translocate passively into the nucleus without the aid of channel proteins or transporters. Aquaporin proteins are a family of water-channel proteins that are known to transport urea, and they have been shown to reside partially on the nuclear membrane (Srivastava et al 2014;Sato et al 2011). Therefore, it is possible for urea to accumulate inside the nucleus, but as we have shown, the amount of nuclear urea is insufficient to significantly affect NFAT binding to DNA.…”

Section: Discussionmentioning

confidence: 99%

Regulation of gene expression by NFAT transcription factors in hibernating ground squirrels is dependent on the cellular environment

Zhang

2016

Cell Stress and Chaperones

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Calcineurin is a calmodulin-stimulated phosphatase that regulates the nuclear translocation of nuclear factor of activated T cell (NFAT) c1-4 through dephosphorylation. We believe that this mechanism plays various roles in the remodeling and maintenance of Ictidomys tridecemlineatus skeletal muscle. During hibernation, bouts of torpor and arousal take place, and squirrels do not lose muscle mass despite being inactive. Protein expression of Ca 2+ signaling proteins were studied using immunoblotting. A DNA-protein interaction ELISA technique was created to test the binding of NFATs in the nucleus to DNA probes containing the NFAT response element under environmental conditions reflective of those during hibernation. Calcineurin protein levels increased by 3.08-fold during torpor (compared to euthermic control), whereas calpain1 levels also rose by 3.66-fold during torpor. Calmodulin levels were elevated upon entering torpor. NFATc4 binding to DNA showed a 1.4-fold increase during torpor, and we found that this binding was further enhanced when 600 nM of Ca 2+ was supplemented. We also found that decreasing the temperature of ELISAs resulted in progressive decreases in the binding of NFATs c1, c3, and c4 to DNA. In summary, calmodulin and calpain1 appear to activate calcineurin and NFATc4 during torpor. NFAT binding to target promoters is affected by intranuclear [Ca 2+ ] and environmental temperatures. Therefore, Ca 2+ signaling and temperature changes play key roles in regulation of the NFAT-calcineurin pathway in skeletal muscle of hibernating 13-lined ground squirrels over the torpor-arousal cycle, and they may contribute to the avoidance of disuse-induced muscle atrophy that occurs naturally in these animals.

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Section: Discussionmentioning

confidence: 99%

Regulation of gene expression by NFAT transcription factors in hibernating ground squirrels is dependent on the cellular environment

Zhang

2016

Cell Stress and Chaperones

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“…Cell typing with immunoelectron microscopy was performed according to the method described previously37. Briefly, the cryosections of oviducts were washed in PBS containing 0.1% Triton X-100 (PBST), sequentially treated with the rabbit anti-male-attracting peptide (1:2,000) in PBST containing 1% bovine serum albumin (1% BSA/PBST) overnight at 4 °C and then washed again with PBST.…”

Section: Methodsmentioning

confidence: 99%

Imorin: a sexual attractiveness pheromone in female red-bellied newts (Cynops pyrrhogaster)

Nakada

Toyoda

Matsuda

et al. 2017

Sci Rep

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The male red-bellied newt (Cynops pyrrhogaster) approaches the female’s cloaca prior to performing any courtship behaviour, as if he is using some released substance to gauge whether she is sexually receptive. Therefore, we investigated whether such a female sexual attractiveness pheromone exists. We found that a tripeptide with amino acid sequence Ala-Glu-Phe is secreted by the ciliary cells in the epithelium of the proximal portion of the oviduct of sexually developed newts and confirmed that this is the major active substance in water in which sexually developed female newts have been kept. This substance only attracted sexually developed male newts and acted by stimulating the vomeronasal epithelial cells. This is the first female sexual attractiveness peptide pheromone to be identified in a vertebrate.

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“…To determine iNOS mRNA localization, frozen vibratome sections were processed using a modification of the whole-mount method (Abdel-latief et al 2008) and one-step in situ RT-PCR (Sato et al 2011). Vibratome sections were immersion-fixed in 4% paraformaldehyde (in PBS buffer; pH 7.2) for 30 min at room temperature.…”

Section: Methodsmentioning

confidence: 99%

Expression and Cellular Localization of Inducible Nitric Oxide Synthase in Lipopolysaccharide-treated Rat Kidneys

Choi

Nam

Jin

et al. 2012

J Histochem Cytochem.

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Although inducible nitric oxide synthase (iNOS) is known to play significant roles in the kidney, its renal localization has long been controversial. To resolve this issue, the authors identified iNOS-positive cell types in rat kidneys using double immunohistochemistry and confirmed iNOS positivity using enzyme histochemistry with NADPH-diaphorase (NADPH-d) and in situ RT-PCR. Adult male Sprague-Dawley rats were injected intraperitoneally with lipopolysaccharide (LPS) or saline as a control and sacrificed at various time intervals after injection. Quantitative real-time reverse transcriptase polymerase chain reaction showed that iNOS was not expressed in control kidneys but was induced in LPS-treated kidneys. iNOS immunostaining was strongest 6 to 18 hr after injection and decreased gradually to control levels by day 7. Double immunohistochemistry and NADPH-d revealed that iNOS expression was induced in the interstitial cells, glomerular parietal epithelial cells, the proximal part of the short-looped descending thin limb, the upper and middle papillary parts of the long-looped descending thin limb, some inner medullary collecting duct cells, and almost all calyceal and papillary epithelial cells. The present study determines the precise localization of iNOS in LPS-treated rat kidneys and provides an important morphological basis for examining the roles of iNOS in sepsis-induced acute kidney injury.

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Expression of a mammalian aquaporin 3 homolog in the anterior pituitary gonadotrophs of the tree frog, Hyla japonica

Cited by 6 publications

References 31 publications

Regulation of gene expression by NFAT transcription factors in hibernating ground squirrels is dependent on the cellular environment

Regulation of gene expression by NFAT transcription factors in hibernating ground squirrels is dependent on the cellular environment

Imorin: a sexual attractiveness pheromone in female red-bellied newts (Cynops pyrrhogaster)

Expression and Cellular Localization of Inducible Nitric Oxide Synthase in Lipopolysaccharide-treated Rat Kidneys

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