Transient hyperosmolality modulates expression of cardiac aquaporins

Rutkovskiy, Arkady; Mariero, Lars Henrik; Nygård, Ståle; Stensløkken, Kåre‐Olav; Valen, Guro; Vaage, Jarle

doi:10.1016/j.bbrc.2012.07.052

Cited by 16 publications

(10 citation statements)

References 27 publications

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“…8). The influence of NaCl on AQP function and expression has been tested especially for mammalian brain and heart (Cao et al 2012; Rutkovskiy et al 2012). It has been observed that NaCl can serve as a factor able to regulate AQP function.…”

Section: Discussionmentioning

confidence: 99%

Molecular Identification of First Putative Aquaporins in Snails

et al. 2014

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Aquaporins (AQPs), also known as water channel proteins, are members of a large protein family termed Major Intrinsic Proteins (MIP). The mammalian AQPs have been most comprehensively described, while knowledge about AQPs in invertebrates is limited mainly to insects. Not a single AQP protein has been described in snails to date. Consequently, we decided to search for the proteins in gastropod representatives, namely Lymnaea stagnalis, Catascopia occulta, and Stagnicola palustris (Mollusca; Gastropoda; Pulmonata; Lymnaeidae). Using the molecular approach, we identified L. stagnalis, C. occulta,and S. palustris open reading frames (ORFs) showing homology to AQP genes available in GenBank database, and characterized the encoded proteins, referred to as LsAQP1, CoAQP1, and SpAQP1, respectively. The putative snail aquaporins contain 299 amino acids, have a molecular mass of about 32 kDa, display the general AQP topology and three-dimensional structure congruent with orthodox AQPs, i.e., water-specific ones. Due to high levels of similarity in their characteristics, LsAQP1 was chosen for further studies, as the obtained results were supposed to be applicable for CoAQP1 and SpAQP1. Expression analysis revealed the presence of LsAQP1 transcript in the digestive tract, the cerebral ganglia, the kidney, the reproductive system, and the foot, suggesting that LsAQP1 as well as CoAQP1 and SpAQP1 are ubiquitous proteins and may play important roles in many essential water transport processes. The role appears to be confirmed by results of the yeast growth complementation assay pointing at functionality of LsAQP1. Thus, the obtained results support the AQP expression in gastropod tissues for the first time.Electronic supplementary materialThe online version of this article (doi:10.1007/s00232-014-9629-0) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Molecular Identification of First Putative Aquaporins in Snails

et al. 2014

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“…Glycosylation is a type of posttranslational protein modification, likely independent of the mRNA content. Recently, Rutkovskiy et al showed that hyperosmolarity increased myocardial AQP1 mRNA and protein glycosylation, but did not influence the total AQP1 protein (28). An isolated change in AQP1 glycosylation in the kidney was also recently reported by Sonoda et al (29).…”

Section: Discussionmentioning

confidence: 74%

The expression profile of aquaporin 1 in rat myocardium after severe burns

Li¹,

Zha²,

Li³

et al. 2015

Turk J Med Sci

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Background/aim: To investigate the myocardial expression profile of aquaporin 1 (AQP1) in rats after severe burns.Materials and methods: Ninety healthy male adult Wistar rats were randomly assigned to the following treatments: sham operation (control group, n = 6), immediate fluid resuscitation treatment post scalding (IF group, n = 42), and delayed fluid resuscitation treatment after scalding (DF group, n = 42). At 3, 6, 12, 24, 48, 72, and 120 h after scalding, myocardial water contents were assayed and AQP1 expressions were detected by real-time polymerase chain reaction and western blot. The AQP levels in the myocardium at 12 h after scalding were assayed by gene microarrays.Results: Scald injuries resulted in significantly synchronized increases in the myocardial water contents and the myocardial mRNA and protein expression of AQP1, with a peak at 12 h after scalding. Rats receiving delayed fluid resuscitation treatment had more severe myocardial edema and significantly higher myocardial AQP1 expressions than the rats receiving immediate fluid resuscitation treatment. The mRNAs of 6 other AQPs (AQP2, 3, 4, 6, 7, and 12b) were found to be changed in the myocardium among rats with different treatments. Conclusion:AQP1 may play a functional role in the development of myocardial edema after scalding. Targeting AQP1 may provide opportunities for therapeutic intervention in myocardial edema following severe burns.

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“…In this sense, it was demonstrated that hyperosmotic NaCl injections induce an up-regulation of AQP1 mRNA and the glycosylated fraction of the AQP1 protein in mice [12]. In the case of AQP4, it was demonstrated that both the mRNA and protein expression decreased in the mouse heart after hyperosmotic NaCl injections [12].…”

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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Transient hyperosmolality modulates expression of cardiac aquaporins

Cited by 16 publications

References 27 publications

Molecular Identification of First Putative Aquaporins in Snails

Molecular Identification of First Putative Aquaporins in Snails

The expression profile of aquaporin 1 in rat myocardium after severe burns

On the Role of Aquaporins in Myocardial Injury

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