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1.
Journal of Korean Medical Science ; : 402-408, 2013.
Article in English | WPRIM | ID: wpr-98486

ABSTRACT

Aquaporins (AQPs) are expressed in myocardium and the implication of AQPs in myocardial water balance has been suggested. We investigated the expression patterns of AQP subtypes in normal myocardium and their changes in the process of edema formation and cardiac dysfunction following myocardial infarction (MI). Immunostaining demonstrated abundant expression of AQP1, AQP4, and AQP6 in normal mouse heart; AQP1 in blood vessels and cardiac myocytes, AQP4 exclusively on the intercalated discs between cardiac myocytes and AQP6 inside the myocytes. However, neither AQP7 nor AQP9 proteins were expressed in CD1 mouse myocardium. Echocardiography revealed that cardiac function was reduced at 1 week and recovered at 4 weeks after MI, whereas myocardial water content determined by wet-to-dry weight ratio increased at 1 week and rather reduced below the normal at 4 weeks. The expression of cardiac AQPs was up-regulated in MI-induced groups compared with sham-operated control group, but their time-dependent patterns were different. The time course of AQP4 expression coincided with that of myocardial edema and cardiac dysfunction following MI. However, expression of both AQP1 and AQP6 increased persistently up to 4 weeks. Our findings suggest a different role for cardiac AQPs in the formation and reabsorption of myocardial edema after MI.


Subject(s)
Animals , Mice , Aquaporin 1/metabolism , Aquaporin 4/metabolism , Aquaporin 6/metabolism , Aquaporins/metabolism , Edema/pathology , Immunohistochemistry , Muscle Cells/metabolism , Myocardial Infarction/metabolism , Myocardium/metabolism , Time Factors
2.
Korean Journal of Anatomy ; : 21-28, 2008.
Article in English | WPRIM | ID: wpr-655040

ABSTRACT

Aquaporin-6 (AQP6) is a water channel protein located in intracellular vesicles of the proximal tubules and in intercalated cells (ICs) in the collecting duct (CD) of the rat kidney. The function of AQP6 is unknown. However, it colocalizes with vacuolar H+-ATPase in type-A ICs, indicating that it may be important for the function of proton pumps in these cells. The aims of this study were to compare the expression of AQP6 between rat and mouse kidneys, and to establish which types of IC express AQP6. Kidneys of adult male rats and mice were processed for immunohistochemistry using antibodies against AQP6, H+-ATPase, and anion exchanger 1 (AE1). AQP6 was expressed in the S1, S2, and S3 segments of the proximal tubule and in ICs of the CD and connecting tubule (CNT) in both rats and mice. In the rat proximal tubule, AQP6 immunoreactivity was present in intracellular vesicles, whereas in the mouse proximal tubule it was present in the brush border as well as in intracellular vesicles. Triple immunostaining for AQP6, AE1, and H+-ATPase revealed that AQP6 was expressed only in type-A ICs in the CDs and CNTs of both rats and mice, and that the staining was diffuse throughout. There was no AQP6 labeling of type-B ICs, non-A-non-B ICs, or principal cells. The functional significance of the expression of AQP6 in proximal tubule cells and type-A ICs remains to be established. We propose that AQP6 is involved in the retrieval and maintenance of H+-ATPasecontaining vesicles in acid-secreting epithelial cells in the kidney.


Subject(s)
Adult , Animals , Humans , Male , Mice , Rats , Antibodies , Aquaporin 6 , Epithelial Cells , Immunohistochemistry , Kidney , Microvilli , Proton Pumps , Vacuolar Proton-Translocating ATPases , Water
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