Aquaporin-1 in cardiac endothelial cells is downregulated in ischemia, hypoxia and cardioplegia

Rutkovskiy, Arkady; Bliksøen, Marte; Hillestad, Vigdis; Amin, Mubashar Mohammad; Czibik, Gabor; Valen, Guro; Vaage, Jarle; Amiry-Moghaddam, Mahmood; Stensløkken, Kåre‐Olav

doi:10.1016/j.yjmcc.2012.12.002

Cited by 39 publications

(32 citation statements)

References 39 publications

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“…Colocalization of immunoreactivity with hSGLT1comAb and AQP1-Ab (Fig. 11k) confirmed that hSGLT1 is colocalized in the AQP1-positive [40,41] endothelial cells of the heart capillaries.…”

Section: Localization Of Hsglt1 In Capillaries Of Human Heartsupporting

confidence: 57%

“…In preliminary experiments using different organs, we observed that the immunostaining efficiency and specificity of hSGLT1-comAb were comparable to that obtained with hSGLT1-Ab and that hSGLT1-comAb immunoreactivity could be blocked with the antigenic peptide EBP09310 supplied by the company (data not shown). Polyclonal antibody to rat water channel aquaporin 1 (AQP1-Ab), which cross-reacts with the human protein, was noncommercial [43]; in heart, AQP1 is expressed in endothelial cells of the microvasculature [40,41]. Commercial monoclonal antibodies to pan-actin (actin-Ab), α-tubulin (tubulin-Ab), and human Na/K-ATPase α1-subunit (Na/K-ATPase-Ab) were from Merck Millipore (Darmstadt, Germany; MAB1501R), Sigma (St. Louis, MO; T5168), and Santa Cruz Biotechnology (Santa Cruz, CA; sc-48345), respectively.…”

Section: Antibodiesmentioning

confidence: 99%

“…11a, b, arrows). Double staining with AQP1-Ab and Na/K-ATPase-Ab showed that the elongated structures between myocytes were also positive for AQP1 which binds to endothelial cells of heart capillaries [40,41] (Fig. 11c-e, large arrows), whereas Na/K-ATPase-positive sarcolemma and intercalated discs (Fig.…”

Section: Localization Of Hsglt1 In Capillaries Of Human Heartmentioning

confidence: 99%

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Localizations of Na+-d-glucose cotransporters SGLT1 and SGLT2 in human kidney and of SGLT1 in human small intestine, liver, lung, and heart

Vrhovac

Eror

Klessen

et al. 2014

Pflugers Arch - Eur J Physiol

251

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Novel affinity-purified antibodies against human SGLT1 (hSGLT1) and SGLT2 (hSGLT2) were used to localize hSGLT2 in human kidney and hSGLT1 in human kidney, small intestine, liver, lung, and heart. The renal locations of both transporters largely resembled those in rats and mice; hSGLT2 and SGLT1 were localized to the brush border membrane (BBM) of proximal tubule S1/S2 and S3 segments, respectively. Different to rodents, the renal expression of hSGLT1 was absent in thick ascending limb of Henle (TALH) and macula densa, and the expression of both hSGLTs was sex-independent. In small intestinal enterocytes, hSGLT1 was localized to the BBM and subapical vesicles. Performing double labeling with glucagon-like peptide 1 (GLP-1) or glucose-dependent insulinotropic peptide (GIP), hSGLT1 was localized to GLP-1-secreting L cells and GIP-secreting K cells as has been shown in mice. In liver, hSGLT1 was localized to biliary duct cells as has been shown in rats. In lung, hSGLT1 was localized to alveolar epithelial type 2 cells and to bronchiolar Clara cells. Expression of hSGLT1 in Clara cells was verified by double labeling with the Clara cell secretory protein CC10. Double labeling of human heart with aquaporin 1 immunolocalized the hSGLT1 protein in heart capillaries rather than in previously assumed myocyte sarcolemma. The newly identified locations of hSGLT1 implicate several extra renal functions of this transporter, such as fluid absorption in the lung, energy supply to Clara cells, regulation of enteroendocrine cells secretion, and release of glucose from heart capillaries. These functions may be blocked by reversible SGLT1 inhibitors which are under development.

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“…Colocalization of immunoreactivity with hSGLT1comAb and AQP1-Ab (Fig. 11k) confirmed that hSGLT1 is colocalized in the AQP1-positive [40,41] endothelial cells of the heart capillaries.…”

Section: Localization Of Hsglt1 In Capillaries Of Human Heartsupporting

confidence: 57%

Section: Antibodiesmentioning

confidence: 99%

Section: Localization Of Hsglt1 In Capillaries Of Human Heartmentioning

confidence: 99%

See 1 more Smart Citation

Localizations of Na+-d-glucose cotransporters SGLT1 and SGLT2 in human kidney and of SGLT1 in human small intestine, liver, lung, and heart

Vrhovac

Eror

Klessen

et al. 2014

Pflugers Arch - Eur J Physiol

251

View full text Add to dashboard Cite

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“…In cardiac muscle, AQP1 is mostly located in microvasculature and t-tubules of myocardial cells [20,24]. It has been shown that cardiac AQP1 level is reduced by ischemia, hypoxia, and cardioplegia [25]. The modulation of AQP1 expression during early phase of dietinduced cardiac dysfunction has not been investigated.…”

Section: Introductionmentioning

confidence: 99%

Cardioprotective effect of valsartan in mice with short-term high-salt diet by regulating cardiac aquaporin 1 and angiogenic factor expression

Jiang

Wang

Zheng

et al. 2015

Cardiovascular Pathology

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“…Cardioplegia, ischemia and hypoxia decrease AQP1 mRNA as well as total protein expression and glycosylation [10]. In endothelium, AQP1 does not regulate the endothelium-derived hyperpolarizing factor (EDH (F)) or NOdependent relaxation, but its deletion increases prostanoids-dependent relaxation in resistance vessels [5].…”

Section: Editorial Textmentioning

confidence: 99%

On the Role of Aquaporins in Myocardial Injury

Ozu¹

2014

Biochem & Pharmacol

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The presence of aquaporins in the cardiovascular system has been well documented, however our knowledge about their role in myocardial pathophysiology is now being elucidated. A brief overview of the presence, function and regulation of aquaporins in myocardial injury is here presented. On the Role of Aquaporins in Myocardial InjuryMarcelo Ozu* Editorial TextCardiopulmonary bypass (CPB) renders the myocardium susceptible to water imbalance and subsequent Myocardial edema (ME) as a consequence of decreased cardiac energy supply [1]. Factors leading to ME include hemodilution, ischemia and reperfusion, as well as osmotic gradients arising from pathological changes of the physiological state.Several members of the aquaporin (AQP) family have been described in the myocardium [2]. The mRNA expression of AQP -1, -3, -5, -7, -9, -10, and -11 was detected in human hearts, while AQP -1, -4, -6, -7, -8, and -11 were detected in hearts from mice and rats [3]. The protein expression of AQP6 was detected inside the myocytes in mice, while AQP4 was exclusively observed on the intercalated discs between cardiac myocytes [4].Experiments with AQP1 knock-out mice showed microcardia, decreased myocyte dimensions and low blood pressure [5]. On the other hand, knock-out mice for AQP7 showed a conserved cardiac morphology, although low content of glycerol and ATP was observed [6].Nowadays, research is focused on the role that aquaporins play in myocardial injury. AQP -1, -4, and -6 seems to play different roles in myocardial infarction (MI) in mouse hearts. While the time dependent pattern of the observed up-regulated expression of AQP4 in MI coincides with that of ME and cardiac dysfunction, the expression of AQP1 and AQP6 persistently increase [4].One of the first reports of aquaporins in heart revealed that AQP1 colocalizes with Caveolin-3 at 20°C and 37°C in rats [7]. Interestingly, when rat cardiac myocytes were exposed to hypertonic media AQP1 was reversibly internalized [7]. In addition, a more recent report showed that AQP1 cosegragates with Caveolin-1 in mice [5]. Recent works demonstrated that the levels of AQP1 mRNA and protein increase 12 hours after global myocardial ischemia in goats following CPB [8]. Moreover, the treatment with HgCl2 reduced ME, indicating that AQP1 is involved in the development of edema [8]. Other works showed that AQP1 expression is inversely correlated with the protein expression of Connexin 43 in goats following CPB [9]. Altogether, these evidences suggest an important role of AQP1 in the regulation of Connexin 43 in the progression of ME, and a related localization of AQP1 and Caveolin-1.In mouse hearts AQP1 was shown to be localized at caveolae but also in endothelial cell membranes. Cardioplegia, ischemia and hypoxia decrease AQP1 mRNA as well as total protein expression and glycosylation [10]. In endothelium, AQP1 does not regulate the endothelium-derived hyperpolarizing factor (EDH (F)) or NOdependent relaxation, but its deletion increases prostanoids-dependent relaxation in resist...

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Aquaporin-1 in cardiac endothelial cells is downregulated in ischemia, hypoxia and cardioplegia

Cited by 39 publications

References 39 publications

Localizations of Na+-d-glucose cotransporters SGLT1 and SGLT2 in human kidney and of SGLT1 in human small intestine, liver, lung, and heart

Localizations of Na+-d-glucose cotransporters SGLT1 and SGLT2 in human kidney and of SGLT1 in human small intestine, liver, lung, and heart

Cardioprotective effect of valsartan in mice with short-term high-salt diet by regulating cardiac aquaporin 1 and angiogenic factor expression

On the Role of Aquaporins in Myocardial Injury

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