Upregulated Expression of AQP 7 in the Skeletal Muscles of Obese ob/ob Mice

Wakayama, Yoshihiro; Hirako, Satoshi; Ogawa, Tetsuo; Jimi, Takahiro; Shioda, Seiji

doi:10.1267/ahc.13032

Cited by 19 publications

(13 citation statements)

References 38 publications

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“…Even under the circumstances of the elevated concentrations of leptin and insulin, both of which suppress the expression of AQP7 [15,25,26] phosphatidylinositol 3 kinase pathway, the AQP7 expression of skeletal muscles of mice with DIO was up-regulated in our present study. Taking our findings of leptin deficient ob/ob mice [14] into consideration, the serum concentration of leptin seems to have no relation to the increased expression level of AQP7 in the skeletal muscles both in DIO and ob/ob mice. Since DIO is associated with hyperinsulinemia and insulin-resistance, it seems plausible that the increased AQP7 in myofibers is related to altered insulin signaling in the skeletal muscle.…”

Section: Discussionmentioning

confidence: 66%

“…We recently reported that the up-regulated expression of AQP7 at RNA and protein levels in the skeletal muscles of leptin deficient obese ob/ob mice [14]. Leptin is a 16kDa peptide hormone secreted by adipocytes and regulates several physiological processes such as glucose and lipid metabolism, blood pressure homeostasis, immunity and reproduction [12,20].…”

Section: Discussionmentioning

confidence: 99%

“…Previously we examined the aquaglyceroporins (such as AQP7 and AQP9) expression in the skeletal muscles of genetically obese leptindeficient ob/ob mice [14] and we found the up-regulated expression of AQP7 in the skeletal muscles of these mice [14]. The plausible mechanism of AQP7 up-regulation in the skeletal muscles of these mice may be due to the leptin deficiency, since the leptin down-regulates AQP7 expression through the phosphatidylinositol 3-kinase /Akt / mammalian target of rapamycin pathway [15].…”

Section: Introductionmentioning

confidence: 99%

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AQP7 Up-Regulation in the Skeletal Muscles of Mice with Diet Induced Obesity

Wakayama¹

2015

J Cell Sci Ther

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Aquaporin (AQP) 7 and AQP9 are membrane proteins and are the members of aquaglyceroporin which transports glycerol in addition to water molecule. Glycerol is a direct source of glycerol-3 phosphate for the synthesis of triglycerides. We thought that the expression of AQP7 and AQP9 would be altered in the skeletal myofibers in mice with diet-induced obesity (DIO) as compared with that of control chaw-fed mice. RNA and protein levels of AQP7 and AQP9 were studied in the quadriceps femoris muscles of mice with DIO and normal control mice. Real time quantitative RT-PCR analysis showed that mouse AQP7 mRNA levels in skeletal muscles were significantly higher in mice with DIO than in normal control mice (P<0.01); whereas mouse AQP9 mRNA levels were not different between the two groups (P>0.05). Histochemically the myofibers of mice with DIO contained numerous lipid droplets in oil red O stain samples. Immunohistochemical study of DIO mouse muscles showed enhanced expression of AQP7 at the myofiber surface membranes; while AQP9 expression appeared to be similar to that of normal control mice. These findings imply that the up-regulated expression of AQP7 in DIO mouse muscles facilitates the secretion of glycerol from myocytes.

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Section: Discussionmentioning

confidence: 66%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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AQP7 Up-Regulation in the Skeletal Muscles of Mice with Diet Induced Obesity

Wakayama¹

2015

J Cell Sci Ther

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“…Additionally, we think that the decrease of AQP3 expression could be used as an important prognostic marker. AQP7 is considered to represent the gateway for the efflux of lipolysis-derived glycerol from adipocytes, whereas AQP9 is considered to play a role in the influx of circulating glycerol into the hepatocytes [37]. Lacroix et al [38] reported that AQP7 expression increases in thyroid follicular carcinoma.…”

Section: Resultsmentioning

confidence: 99%

Can aquaporins be used as diagnostic and prognostic markers for uterine smooth muscle tumours?

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et al. 2016

Biotechnology & Biotechnological Equipment

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Generally, uterine leiomyosarcoma is easily diagnosed. However, uterine smooth muscle tumours which show atypical histological features and unusual growth patterns may mimic malignancy and may not be easily diagnosed. In this study, our aim is to show the expressions of Aquaporin3, Aquaporin7 and Aquaporin9 in uterine smooth muscle tumours, and to investigate if aquaglyceroporins can be used as diagnostic and prognostic markers to start rapidly an appropriate treatment for patients with these tumours in order to extend the survival time. We determined that there had been 74 patients diagnosed with uterine smooth muscle tumours. We divided patients into four groups based on the diagnosis: bizarre leiomyoma, smooth muscle tumour of uncertain malignant potential, leiomyosarcoma and leiomyoma. Aquaporin3, Aquaporin7 and Aquaporin9 were detected by using monoclonal anti-Aquaporin3, antiAquaporin7 and anti-Aquaporin9 antibodies, respectively. In leiomyosarcoma group, we observed a statistically significant relation of Aquaporin3 expression with survival time, grade, stage, mitotic index and Ki-67 score. A significant relation of both Aquaporin7 and Aquaporin9 expressions with survival time, grade, stage was not statistically detected in leiomyosarcoma group. The decrease of Aquaporin3 expression can be used as important diagnostic and prognostic marker. Aquaporin7 and Aquaporin9 expressions cannot be used as diagnostic and prognostic markers.

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“…In the seabream, however, the Aqp9b ortholog is not found in the epithelium of the spermatic duct but in the smooth muscle fibers, together with Aqp8bb. In contrast, in mammals AQP9 is reported to be expressed in normal skeletal muscle fibers (Inoue et al 2009;Wakayama et al 2014), but not in smooth muscle cells, and both AQP8 and -9 have been observed in the developing masseter muscle (Wang et al 2003). The roles of AQP9 and -8, and of the seabream Aqp9b and -8bb, in muscle cells are not known but they may be respectively involved in glycerol metabolism and the transport of reactive oxygen species (i.e.…”

Section: Discussionmentioning

confidence: 97%

The cellular localization and redistribution of multiple aquaporin paralogs in the spermatic duct epithelium of a maturing marine teleost

et al. 2018

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Aquaporin-mediated fluid transport in the mammalian efferent duct and epididymis is believed to play a role in sperm maturation and concentration. In fish, such as the marine teleost gilthead seabream (Sparus aurata), the control of fluid homeostasis in the spermatic duct seems also to be crucial for male fertility, but no information exists on the expression and distribution of aquaporins. In this study, reverse transcriptase-polymerase chain reaction and immunoblotting analyses, employing available and newly raised paralog-specific antibodies for seabream aquaporins, indicate that up to nine functional aquaporins, Aqp0a, -1aa, -1ab, -3a, -4a, -7, -8bb, -9b and -10b, are expressed in the spermatic duct. Immunolocalization of the channels in the resting spermatic duct reveals that Aqp0a, -1aa, -4a, -7 and -10b are expressed in the monolayered luminal epithelium, Aqp8b and -9b in smooth muscle fibers, and Aqp1ab and -3a in different interstitial lamina cells. In the epithelial cells, Aqp0a and -1aa are localized in the short apical microvilli, and Aqp4a and -10b show apical and basolateral staining, whereas Aqp7 is solely detected in vesicular compartments. Upon spermiation, an elongation of the epithelial cells sterocilia, as well as the folding of the epithelium, is observed. At this stage, single- and double-immunostaining, using two aquaporin paralogs or the Na /K -ATPase membrane marker, indicate that Aqp1ab, -3a, -7, -8bb and -9b staining remains unchanged, whereas in epithelial cells Aqp1aa translation is supressed, Aqp4a internalizes, and Aqp0a and -10b accumulate in the apical, lateral and basal plasma membrane. These findings uncover a cell type- and region-specific distribution of multiple aquaporins in the piscine spermatic duct, which shares conserved features of the mammalian system. The data therefore suggest that aquaporins may play different roles in the regulation of fluid homeostasis and sperm maturation in the male reproductive tract of fish.

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Upregulated Expression of AQP 7 in the Skeletal Muscles of Obese ob/ob Mice

Cited by 19 publications

References 38 publications

AQP7 Up-Regulation in the Skeletal Muscles of Mice with Diet Induced Obesity

AQP7 Up-Regulation in the Skeletal Muscles of Mice with Diet Induced Obesity

Can aquaporins be used as diagnostic and prognostic markers for uterine smooth muscle tumours?

The cellular localization and redistribution of multiple aquaporin paralogs in the spermatic duct epithelium of a maturing marine teleost

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