Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 20 de 68
Filter
1.
Int. j. morphol ; 37(3): 815-820, Sept. 2019. graf
Article in English | LILACS | ID: biblio-1012358

ABSTRACT

One of the key functions of the hepatobiliary system is bile formation. Aquaporins (AQPs) are likely to play a role in water transport that is essential for appropriate hepatobiliary tract function. The increasing prevalence of fatty liver parallels the rise of obesity and its complications over the past several decades. In this paper, general morphology observation, histopathology and AQP1 immunohistochemical expression were observed in livers of the high-fat diet (HFD) rats. For the liver of HFD rats, immunolight microscopy revealed weak labeling of AQP1 on the surface of central veins and liver sinusoid compared with the normal diet (ND) rats. It was suggested that bile secreted by the liver of HFD rats was maybe abnormal, thereby causing abnormalities in the composition and secretion of bile. However, the deeper understanding of mechanisms involved to the fatty liver is still unclear, in particular AQPs in the liver of obesity, additional studies would be required to study the signalling cascades involved in these processes.


Una de las funciones clave del sistema hepatobiliar es la formación de bilis. Es probable que las acuaporinas (AQP) desempeñen un papel en el transporte de agua que es esencial para la función apropiada del tracto hepatobiliar. En las últimas décadas, la creciente prevalencia de hígado graso es paralela al aumento de la obesidad y sus complicaciones. En este trabajo, se identificaron características morfológicas generales, histopatología y expresión inmunohistoquímica de AQP1 en hígados de ratas con dieta rica en grasas (DRG). En el hígado de ratas con DRG, la expresión inmunohistoquímica determinó un marcaje débil de AQP1 en la superficie de las venas centrales y del sinusoide hepático en comparación con las ratas de dieta normal (DN). Se sugirió que la bilis secretada por el hígado de ratas con DRG era tal vez anormal, lo que causaba anomalías en la composición y secreción de la bilis. Sin embargo, se necesita un conocimiento mayor de los mecanismos involucrados en el hígado graso, en particular de las AQP y se requieren estudios adicionales para determinar las cascadas de señalización involucradas en estos procesos.


Subject(s)
Animals , Rats , Aquaporin 1/analysis , Fatty Liver/metabolism , Diet, High-Fat , Immunohistochemistry , Rats, Sprague-Dawley , Aquaporin 1/metabolism , Liver/chemistry
2.
Int. j. morphol ; 37(2): 406-411, June 2019. graf
Article in English | LILACS | ID: biblio-1002235

ABSTRACT

AQP1 plays an essential role in maintaining body water balance. In the kidney, AQP1 is localized to the apical and basolateral membrane of epithelial cells in the proximal tubule and descending thin limb of Ansa nephroni (Henle's loop) where it reabsorbs the vast majority of filtered water. The growing epidemic of obesity and metabolic diseases particularly obesity-related kidney disease is getting more and more attention in this century. However, a full understanding of mechanisms involved to the progressive renal disease is still unclear, in particular AQPs in the kidney of obesity. In this paper, we examined the localization of AQP1 in renal cortex and medulla of ND (normal diet) and HFD (high-fat diet) at rats. In the renal cortex and medulla, immunolight microscopy revealed weak expression of AQP1 in the apical and basolateral membrane of epithelial cells at the proximal straight/convoluted tubule of HFD compared with ND, respectively. The same result was confirmed in the thick descending limb and descending thin limb of Henle's loop. In the high-fat nutritional obesity of rats, decreased AQP1 levels may not directly cause serious obesity-related kidney disease, e.g. chronic kidney disease, even end-stage renal disease. But at least, AQPs (AQP1 in this study) was one of initially conditions to the incentive of obesity-related kidney disease.


Las acuoporinas tipo 1 (AQP1) constituyen una parte esencial en el mantenimiento del equilibrio del agua en el cuerpo. En el riñón, la AQP1 se localiza en la membrana apical y basolateral de las células epiteliales, en el túbulo proximal y en el segmento descendente del Ansa nephroni o asa nefrónica (asa de Henle), donde reabsorbe la gran mayoría de agua filtrada. La creciente epidemia de obesidad y enfermedades metabólicas en el siglo actual, hacen que la enfermedad renal relacionada con la obesidad esté recibiendo cada vez más atención. Sin embargo, aún no existe un conocimiento definitivo de los mecanismos implicados en la enfermedad renal progresiva, en particular los relacionados a las acuoporinas renales en la obesidad. En este trabajo, examinamos la localización de AQP1 en la corteza y la médula renales de la dieta normal (DN) y dieta alta en grasa (DAG) en ratas. En la corteza y médula renales, la microscopía de luz reveló una expresión débil de AQP1 en la membrana apical y basolateral de las células epiteliales en el túbulo contorneado proximal del grupo DAG en comparación con el grupo DN, respectivamente. El mismo resultado se confirmó en la porción descendente gruesa y en la porción descendente delgada del asa nefrónica. En ratas del grupo DAG, la disminución de los niveles de AQP1 pudo no ser la causa directa de una enfermedad renal grave relacionada con obesidad, como por ejemplo, enfermedad renal crónica, o una enfermedad renal terminal. No obstante, en este estudio, la expresión renal de AQP1 constituyó una de las condiciones iniciales para inducir la enfermedad renal relacionada con obesidad.


Subject(s)
Animals , Rats , Aquaporin 1/metabolism , Diet, High-Fat , Kidney/pathology , Immunohistochemistry , Rats, Sprague-Dawley , Kidney/metabolism , Kidney Medulla/pathology
3.
Int. j. morphol ; 37(2): 459-465, June 2019. tab, graf
Article in English | LILACS | ID: biblio-1002243

ABSTRACT

Recent evidence has indicated that adipose tissue produces bioactive substances that contribute to obesity-related kidney disease, altering the renal function and structure. Eight of the AQPs are expressed in the kidney, where several of them contribute to water absorption and maintenance of body water balance. In the study, we mainly examined the localization of AQP2, AQP3 and V2R in renal medulla of Normal Diet (ND) and High-fat Diet (HFD) of rats, respectively. In renal medulla of HFD, immunolight microscopy revealed weak expression of AQP2 at the apical plasma membrane and intracellular vesicles of principal cells of the IMCD and OMCD. AQP3 and V2R expression also observed a decrease in immunolabelling in the IMCD and OMCD. It was suggested that excess lipid accumulation may lead to lipotoxicity and may be the major driver of organ dysfunction such as water reabsorption dysfunction, which may be resulted from abnormal response of rphan G-protein-coupled receptors in kidney.


La evidencia reciente ha indicado que el tejido adiposo produce sustancias bioactivas que contribuyen a la enfermedad renal relacionada con la obesidad, alterando la función y la estructura renal. Ocho de los AQP se expresan en el riñón, donde varios de ellos contribuyen a la absorción de agua y al mantenimiento del equilibrio hídrico corporal. En el estudio, examinamos principalmente la localización de AQP2, AQP3 y V2R en la médula renal de ratas con dieta normal (ND) y ratas con dieta alta en grasas (HFD). En la médula renal del grupo HFD, la microscopía electrónica de barrido reveló una expresión débil de AQP2 en la membrana plasmática apical y las vesículas intracelulares de las células principales de IMCD y OMCD. La expresión de AQP3 y V2R también observó una disminución en el inmunomarcador en IMCD y OMCD. Se sugiere que el exceso de acumulación de lípidos puede conducir a lipotoxicidad y ser el principal impulsor de la disfunción orgánica, como la disfunción de reabsorción de agua, que puede ser el resultado de la respuesta anormal de los receptores acoplados a proteína rphan G en el riñón.


Subject(s)
Animals , Rats , Receptors, Vasopressin/metabolism , Aquaporins/metabolism , Diet, High-Fat , Kidney Diseases/metabolism , Kidney Medulla/pathology , Obesity , Immunohistochemistry , Rats, Sprague-Dawley , Aquaporin 1/metabolism , Aquaporin 2/metabolism , Kidney Medulla/metabolism , Microscopy
4.
Int. j. morphol ; 37(2): 706-711, June 2019. graf
Article in English | LILACS | ID: biblio-1002281

ABSTRACT

A serous membrane covering the liver and the hepatic parenchyma, consists of hepatocytes, arteries, veins, hepatic sinusoids and biliary ductuli. There are erythrocytes, thrombocytes, melanin particles and Kupffer cell in the hepatic sinusoids and the blood vessels. The gall bladder wall consists of a mucous layer a muscle layer and a serous layer. The bottom of the epithelium abounds with round or oval secretory. In liver, immunohistochemistry results show that AQP1 have intense reaction in hepatic lobule, Kupffer cells (Macrophagocytus stellatus), hepatocytes, portal tract, blood islands, vein and artery, but almost no reaction of AQP2 was detected. In gallbladder, mucous epithelium, endothelial cells from vein and artery all have strong AQP1 expression, AQP2 showed minor diffused positive reaction in gallbladder, which suggesting that AQP1 may have the main role in the absorption and transportation of fluid in hepatobiliary system of Qinghai Lizard.


Una membrana serosa cubre el hígado y el parénquima hepático el cual está formado por hepatocitos, arterias, venas, sinusoides hepáticos y conductos biliares. Se encuentran eritrocitos, trombocitos, partículas de melanina y células de Kupffer en los sinusoides hepáticos y en los vasos sanguíneos. La pared de la vesícula biliar presenta tres capas: mucosa, muscular y serosa. En el hígado, la inmunohistoquímica mostró que AQP1 tiene una reacción intensa en el lóbulo hepático, células de Kupffer, hepatocitos, tracto portal e islotes sanguíneos. En venas y arterias, no se detectó reacción alguna de AQP2. En la vesícula biliar, el epitelio mucoso, las células endoteliales venosas y arteriales tuvieron una importante expresión de AQP1, sin embargo, AQP2 mostró una reacción positiva difusa menor, lo que sugiere que la AQP1 podría tener una función principal en la absorción y transporte de líquido en el sistema hepatobiliar del Lagarto Qinghai.


Subject(s)
Animals , Aquaporins/metabolism , Gallbladder/metabolism , Liver/metabolism , Lizards , Immunohistochemistry , Aquaporin 1/metabolism , Aquaporin 2/metabolism , Gallbladder/ultrastructure , Liver/ultrastructure
5.
Rev. bras. parasitol. vet ; 26(1): 60-66, Jan.-Mar. 2017. tab, graf
Article in English | LILACS | ID: biblio-844136

ABSTRACT

Abstract This study evaluated a recombinant aquaporin 1 protein of Rhipicephalus (Boophilus) microplus (RmAQP1) as antigen in a vaccine against R. sanguineus. Five dogs were immunized with RmAQP1 (10 µg) + adjuvant (Montanide) (G1), and five were inoculated with adjuvant only (G2), three times. Twenty-one days after the last immunization, animals of both groups were challenged with R. sanguineus larvae, nymphs and adults, and their biotic potential was compared. Blood samples were collected before each immunization and every 28 days after the last immunization for 10 weeks. Serum antibody titers (IgG) were assessed by ELISA. We observed that: engorgement period of adult females from G1 was 12% shorter than G2; larvae from G1 had 8.7% longer engorgement period than G2 and weighed 7.2% less; nymphs from G1 had 4.5% shorter engorgement period than G2 and weighed 3.6% less; although the antibody titers increased following the second immunization, they rapidly decreased after the third immunization. Results indicated low immunoprotection of RmAQP1 against adult R. sanguineus ticks, and possible efficacy on larvae and nymphs fed on immunized dogs. Further studies should be performed for a full evaluation of the immunoprotection of RmAQP1 against R. sanguineus infestations in dogs.


Resumo Este estudo avaliou a proteína recombinante (aquaporina) do carrapato Rhipicephalus (Boophilus) microplus como antígeno em vacina contra Rhipicephalus sanguineus. Cinco cães foram imunizados com RmAQP1 (10 µg) + adjuvante (G1) e cinco foram inoculados apenas com adjuvante (G2), três vezes. 21 dias após a última imunização todos os animais foram desafiados com larvas, ninfas e adultos de R. sanguineus, e potencial biótico dos carrapatos foi comparado. Amostras de sangue foram coletadas antes de cada imunização e a cada 28 dias após a última imunização, durante 10 semanas. Títulos de anticorpos dos soros dos cães foram avaliados por ELISA. Resultados: o período de ingurgitamento das fêmeas do G1 foi 12% mais curto que o período de ingurgitamento de G2; o período de ingurgitamento das larvas do G1 8,7% foi mais longo e o peso 7,2% menor que no caso de G2; o período de ingurgitamento das ninfas do G1 4,5% foi mais curto e peso 3,6% menor que no caso do G2; aumento dos títulos de anticorpos do G1 após a segunda imunização e declínio após a terceira imunização. Os resultados indicaram baixo potencial de imunoproteção de RmAQP1 contra R. sanguineus adultos, e possível eficácia contra larvas e ninfas, na dose testada. Sugere-se desenvolver novos estudos para melhor avaliação da eficácia de RmAQP1 contra R. sanguineus em cães.


Subject(s)
Animals , Female , Dogs , Tick Infestations/veterinary , Immunoglobulin G/blood , Immunization/veterinary , Rhipicephalus/immunology , Rhipicephalus sanguineus/immunology , Dog Diseases/prevention & control , Aquaporin 1/immunology , Tick Infestations/immunology , Tick Infestations/prevention & control , Recombinant Proteins/immunology , Immunoglobulin G/immunology , Immunization/methods , Dog Diseases/immunology
6.
Article in English | WPRIM | ID: wpr-80645

ABSTRACT

OBJECTIVE: Aquaporin (AQP) is a recently discovered protein that regulates water homeostasis. The present study examines changes in AQP 1 and 4 in kaolin induced experimental hydrocephalic rats to elucidate the pathophysiology of water homeostasis in the disease. METHODS: Hydrocephalus was induced by percutaneous intracisternal injection of kaolin. The brain parenchyma and choroid plexus were obtained at 3, 7, 14 and 30 days after injection. Protein expressions of AQP 1 and 4 were measured by western blot, immunohistochemistry (IHC) and immunofluorescence (IF) stains. RESULTS: In the choroid plexus of the kaolin-induced hydrocephalus group, AQP 1 expression identified by western blot exhibited sharp decrease in the early stage (55% by the 3rd day and 22% by the 7th day), but indicated a 2.2-fold increase in the later stage (30th day) in comparison with control groups. In the parenchyma, a quantitative measurement of AQP 4 expression revealed variable results on the 3rd and 7th days, but indicated expression 2.1 times higher than the control in the later stage (30th day). In addition, the IHC and IF findings supported the patterns of expression of AQP 1 in the choroid plexus and AQP 4 in the parenchyma. CONCLUSION: Expression of AQP 1 decreased sharply in the choroid plexus of acute hydrocephalus rats and increased at later stages. Expression of AQP 4 in the brain parenchyma was variable in the early stage in the hydrocephalus group, but was higher than in the control in the later stage. These findings suggest a compensating role of AQPs in water physiology in hydrocephalus.


Subject(s)
Animals , Aquaporin 1 , Aquaporins , Blotting, Western , Brain , Choroid Plexus , Choroid , Coloring Agents , Fluorescent Antibody Technique , Homeostasis , Hydrocephalus , Immunohistochemistry , Kaolin , Physiology , Rats , Water
7.
Immune Network ; : 103-109, 2017.
Article in English | WPRIM | ID: wpr-51911

ABSTRACT

The pathophysiology of glandular dysfunction in Sjögren's syndrome (SS) has not been fully elucidated. Previously, we reported the presence of autoantibodies to AQP-5 in patients with SS, which was associated with a low resting salivary flow. The purpose of this study was to investigate the presence of anti-AQP1 autoantibodies. To detect anti-AQP1 autoantibodies, cell-based indirect immunofluorescence assay was developed using MDCK cells that overexpressed human AQP1. By screening 112 SS and 52 control sera, anti-AQP1 autoantibodies were detected in 27.7% of the SS but in none of the control sera. Interestingly, the sera that were positive for anti-AQP1 autoantibodies also contained anti-AQP5 autoantibodies in the previous study. Different from anti-AQP5 autoantibodies, the presence of anti-AQP1 autoantibodies was not associated with the salivary flow rate. Although anti-AQP1 autoantibodies are not useful as a diagnostic marker, the presence of autoantibodies to AQP1 may be an obstacle to AQP1 gene therapy for SS.


Subject(s)
Aquaporin 1 , Autoantibodies , Fluorescent Antibody Technique , Fluorescent Antibody Technique, Indirect , Genetic Therapy , Humans , Madin Darby Canine Kidney Cells , Mass Screening
8.
Int. j. morphol ; 34(4): 1218-1222, Dec. 2016. ilus
Article in English | LILACS | ID: biblio-840870

ABSTRACT

Spermatogenesis is associated with considerable fluid secretion or absorption in the male reproductive tract. Aquaporins (AQPs) are membrane protein channels that allow the rapid movement of water through epithelium. In the present study, immunohistochemistry was utilized to localize the expression of AQP 1, AQP2 in the testis and prostate of adult bactrian camel (Camelus bactrianus). Results show that AQP1 have intense reaction in rete testis, efferent ducts, vessels, seminiferous duct and in the prostate, AQP2 was found minor expression in the rete testis, vessels and prostate, which suggesting that AQP1 may have the main role in the absorption of the large amount of testicular fluid in male camel reproductive tract. Investigations of AQPs biology in camel could be relevant with technologies for assisted procreation in animal husbandry and aquaculture.


La espermatogénesis se asocia con la secreción de una cantidad considerable de líquido o absorción en el tracto reproductor masculino. Las acuaporinas (ACPs) son canales de proteínas de membrana que permiten el movimiento rápido de agua a través del epitelio. En el presente estudio, se utilizó inmunohistoquímica para localizar la expresión de ACP 1, ACP2 en el testículo y la próstata del camello bactriano adulto (Camelus bactrianus). Los resultados muestran que ACP1 tiene una reacción intensa en la rete testis, conductos eferentes, vasos, conductos seminíferos y en la próstata. La expresión ACP2, de menor importancia, se observó en la rete testis, vasos y próstata, lo que sugiere que ACP1 puede tener el papel principal en la absorción de gran cantidad de líquido testicular en el tracto reproductivo masculino del camello. Las investigaciones de la biología del ACP en camello podrían ser relevantes para las tecnologías de reproducción asistida de la ganadería y la acuicultura.


Subject(s)
Animals , Male , Aquaporin 1/metabolism , Aquaporin 2/metabolism , Camelus , Genitalia, Male/metabolism , Genitalia, Male/anatomy & histology , Immunohistochemistry , Prostate/metabolism , Testis/metabolism
9.
Article in English | WPRIM | ID: wpr-32750

ABSTRACT

BACKGROUND: Aquaporin 1 (AQP1) overexpression has been shown to be associated with uncontrolled cell replication, invasion, migration, and tumor metastasis. We aimed to evaluate AQP1 expression in lung adenocarcinomas and to examine its association with clinicopathological features and prognostic significance. We also investigated the association between AQP1 overexpression and epithelial-mesenchymal transition (EMT) markers. METHODS: We examined AQP1 expression in 505 cases of surgically resected lung adenocarcinomas acquired at the Seoul National University Bundang Hospital from 2003 to 2012. Expression of AQP1 and EMT-related markers, including Ecadherin and vimentin, were analyzed by immunohistochemistry and tissue microarray. RESULTS: AQP1 overexpression was associated with several aggressive pathological parameters, including venous invasion, lymphatic invasion, and tumor recurrence. AQP1 overexpression tended to be associated with higher histological grade, advanced pathological stage, and anaplastic lymphoma kinase (ALK) translocation; however, these differences were not statistically significant. In addition, AQP1 overexpression positively correlated with loss of E-cadherin expression and acquired expression of vimentin. Lung adenocarcinoma patients with AQP1 overexpression showed shorter progression-free survival (PFS, 46.1 months vs. 56.2 months) compared to patients without AQP1 overexpression. Multivariate analysis confirmed that AQP1 overexpression was significantly associated with shorter PFS (hazard ratio, 1.429; 95% confidence interval, 1.033 to 1.977; p=.031). CONCLUSIONS: AQP1 overexpression was thereby concluded to be an independent factor of poor prognosis associated with shorter PFS in lung adenocarcinoma. These results suggested that AQP1 overexpression might be considered as a prognostic biomarker of lung adenocarcinoma.


Subject(s)
Adenocarcinoma , Aquaporin 1 , Cadherins , Disease-Free Survival , Epithelial-Mesenchymal Transition , Humans , Immunohistochemistry , Lung , Lymphoma , Multivariate Analysis , Neoplasm Metastasis , Phosphotransferases , Prognosis , Recurrence , Seoul , Tissue Array Analysis , Vimentin
10.
Article in Chinese | WPRIM | ID: wpr-353117

ABSTRACT

<p><b>OBJECTIVE</b>To determine the effect of AQP1 gene on facial nerve edema following injury through investigation of the relationship between the expression of AQP1 gene and Schwann cells swelling.</p><p><b>METHODS</b>The AQP1 expression in Schwann cells of mouse facial nerve tissues was detected by immunofluorescent staining. The transgenic protocol by lentivirus transduction was used to specifically upregulate AQP1 expression in Schwann cells. Lenti-AQP1 and CTRL (empty vector) transduced cells were observed during gene overexpression every 24 h for 6 days by using phase contrast microscopy. Cell volume of CTRL and Lenti-AQP1 treated cells was measured daily from the day of treatment, through day 6.</p><p><b>RESULTS</b>Schwann cell primary cultures maintained a high level of AQP1 water channels, representing an ideal cell model to study the role of AQP1 in the facial nerve. The expression of AQP1 mRNA and protein in Schwann cells infected with the Lenti-AQP1 was increased significantly compared with CTRL lentivirus (P < 0.05). Lenti-AQP1 caused cell swelling in cultured Schwann cells, as validated by cell volume determinations (P < 0.01).</p><p><b>CONCLUSIONS</b>AQP1 is an important factor responsible for the fast water transport of cultured Schwann cells. It plays an important role in facial nerve edema.</p>


Subject(s)
Animals , Aquaporin 1 , Genetics , Metabolism , Cell Size , Edema , Facial Nerve , Metabolism , Facial Nerve Diseases , Lentivirus , Mice , RNA, Messenger , Metabolism , Schwann Cells , Cell Biology , Metabolism , Virology , Time Factors , Transduction, Genetic , Methods , Up-Regulation
11.
Article in Chinese | WPRIM | ID: wpr-746903

ABSTRACT

OBJECTIVE@#To construct a kind of recombinant plasmid PGCsi-AQP1 delivery with DOPC and explore the inhibit effect of laryngeal carcinoma by RNAi targeting AQP1 in vivo.@*METHOD@#Male BALB/c mice, 6 weeks of age transplanted with laryngeal carcinoma cell line Hep-2, four groups were divided randomly: Tail vein injection group (TVIG), Carcinoma around injection group (CAIG), negative control group (NCG) and blank control group (BCG). The recombinant plasmid PGCsi-AQP1 delivery with DOPC were inject into tail vein or surrounding tumor. HE pathological slides and tumor size were observed and inhibitory rate was figured up. The level of AQP1 protein expression and high microvessel density were detected by Immunohistochemical staining (IHC).@*RESULT@#We constructed BALB/c mice models of laryngeal carcinoma successfully (1) HE staining: cell putrescence, nuclear pyknosis and apoptotic bodies were more in the tumor tissues of experimental groups than two control groups. (2) The total volumes of tumor in experimental group were both smaller than in two control groups (P 0.05). (3) IHC: the AQP1 positive cells and microvessel density in TVIG and CAIG were both less than in two control groups (P < 0.01).@*CONCLUSION@#Neutral lipsomes DOPC could help carriaging the recombinant plasmid PGCsi-AQP1 to tumor and then play an inhibit role in laryngeal carcinoma tissue by RNAi targeting AQP1 in vivo.


Subject(s)
Animals , Aquaporin 1 , Therapeutic Uses , Cell Line, Tumor , Laryngeal Neoplasms , Therapeutics , Liposomes , Male , Mice , Mice, Inbred BALB C , Neoplasm Transplantation , Plasmids , RNA Interference , RNA, Small Interfering , Random Allocation , Transfection
12.
Article in English | WPRIM | ID: wpr-190711

ABSTRACT

Ischemic stroke results in the diverse phathophysiologies including blood brain barrier (BBB) disruption, brain edema, neuronal cell death, and synaptic loss in brain. Vitamin C has known as the potent anti-oxidant having multiple functions in various organs, as well as in brain. Dehydroascorbic acid (DHA) as the oxidized form of ascorbic acid (AA) acts as a cellular protector against oxidative stress and easily enters into the brain compared to AA. To determine the role of DHA on edema formation, neuronal cell death, and synaptic dysfunction following cerebral ischemia, we investigated the infarct size of ischemic brain tissue and measured the expression of aquaporin 1 (AQP-1) as the water channel protein. We also examined the expression of claudin 5 for confirming the BBB breakdown, and the expression of bcl 2 associated X protein (Bax), caspase-3, inducible nitric oxide synthase (iNOS) for checking the effect of DHA on the neurotoxicity. Finally, we examined postsynaptic density protein-95 (PSD-95) expression to confirm the effect of DHA on synaptic dysfunction following ischemic stroke. Based on our findings, we propose that DHA might alleviate the pathogenesis of ischemic brain injury by attenuating edema, neuronal loss, and by improving synaptic connection.


Subject(s)
Aquaporins , Aquaporin 1 , Ascorbic Acid , bcl-2-Associated X Protein , Blood-Brain Barrier , Brain , Brain Edema , Brain Injuries , Brain Ischemia , Caspase 3 , Cell Death , Claudin-5 , Dehydroascorbic Acid , Edema , Neurons , Nitric Oxide Synthase Type II , Oxidative Stress , Post-Synaptic Density , Stroke
13.
Article in English | WPRIM | ID: wpr-145430

ABSTRACT

PURPOSE: It is suggested that caveolin and aquaporin might be closely associated with bladder signal activity. We investigated the effect of the deletion of caveolin 1, using caveolin 1 knockout mice, on the expression of aquaporin 1 in order to identify their relation in the urothelium of the urinary bladder. METHODS: The cellular localization and expressions of aquaporin 1 and caveolin 1, in the wild type and caveolin 1 knockout mice urinary bladder, were examined by Western blot and immunofluorescence techniques. RESULTS: Aquaporin 1 and caveolin 1 were coexpressed in the arterioles, venules, and capillaries of the suburothelial layer in the wild type controls. Aquaporin 1 protein expression was significantly higher in the caveolin 1 knockout mice than in the wild type controls (P <0.05). CONCLUSIONS: The results imply that aquaporin 1 and caveolin 1 may share a distinct relation with the bladder signal activity. This might play a specific role in bladder dysfunction.


Subject(s)
Animals , Aquaporin 1 , Arterioles , Blotting, Western , Capillaries , Caveolin 1 , Fluorescent Antibody Technique , Mice , Mice, Knockout , Urinary Bladder , Urothelium , Venules
14.
Article in Chinese | WPRIM | ID: wpr-239219

ABSTRACT

<p><b>OBJECTIVE</b>To investigate the differentiation capability of kidney stem cells (KSCs) into renal tubular epithelial cells (RTECs).</p><p><b>METHODS</b>KSCs isolated from the renal papilla of 4-week-old SD rats were co-cultured with hypoxia-exposed RTEC in induced medium (containing activin A, BMP-7, and retinoic acid) and renal epithelial cell growth medium (REGM) alternately. The KSCs cultured in MSC medium served as the control. The KSC differentiation rates in both groups were determined using flow cytometry, immunofluorescence assay and qRT-PCR.</p><p><b>RESULTS</b>Flow cytometry showed a CK-18 positive rate of 6.5Percnt; in the control KSC group and of 44.2% in the induced group. Immunofluorescence assay detected the positivity for mature epithelial cell markers CK-18, E-cadherin, and ZO-1 in the induced cells. The results of qRT-PCR showed significantly increased expression of E-cadherin and AQP-1 mRNAs in the induced cells compared with the control cells (P<0.01).</p><p><b>CONCLUSION</b>Rat KSCs can be induced to differentiate into RTECs in vitro.</p>


Subject(s)
Activins , Chemistry , Animals , Aquaporin 1 , Metabolism , Bone Morphogenetic Protein 7 , Chemistry , Cadherins , Metabolism , Cell Differentiation , Coculture Techniques , Culture Media , Chemistry , Epithelial Cells , Cell Biology , Keratin-18 , Metabolism , Kidney Tubules , Cell Biology , Rats , Rats, Sprague-Dawley , Stem Cells , Cell Biology , Tretinoin , Chemistry , Zonula Occludens-1 Protein , Metabolism
15.
Article in English | WPRIM | ID: wpr-250358

ABSTRACT

This study aims to elucidate the mechanisms by which dexmedetomidine alleviates pulmonary edema in rats with acute lung injury induced by lipopolysaccharide (LPS). Male Wistar rats were randomly divided into five groups: normal saline control (NS) group, receiving intravenous 0.9% normal saline (5 mL/kg); LPS group, receiving intravenous LPS (10 mg/kg); small-dose dexmedetomidine (S) group, treated with a small dose of dexmedetomidine (0.5 μg · kg(-1) · h(-1)); medium-dose dexmedetomidine (M) group, treated with a medium dose of dexmedetomidine (2.5 μg · kg(-1) · h(-1)); high-dose dexmedetomidine (H) group, treated with a high dose of dexmedetomidine (5 μg · kg(-1) · h(-1)). The rats were sacrificed 6 h after intravenous injection of LPS or NS, and the lungs were removed for evaluating histological characteristics and determining the lung wet/dry weight ratio (W/D). The levels of tumor necrosis factor-alpha (TNF-α) and interleukin-1β (IL-1β) in the lung tissues were assessed by enzyme- linked immunosorbent assay (ELISA). The mRNA and protein expression levels of aquaporin-1 (AQP1) and aquaporin-5 (AQP5) were detected by RT-PCR, immunohistochemistry, and Western blotting. The lung tissues from the LPS groups were significantly damaged, which were less pronounced in the H group but not in the small-dose dexmedetomidine group or medium-dose dexmedetomidine group. The W/D and the concentrations of TNF-α and IL-1β in the pulmonary tissues were increased in the LPS group as compared with those in NS group, which were reduced in the H group but not in S group or M group (P<0.01). The expression of AQP1 and AQP5 was lower in the LPS group than in the NS group, and significantly increased in the H group but not in the S group or M group (P<0.01). Our findings suggest that dexmedetomidine may alleviate pulmonary edema by increasing the expression of AQP-1 and AQP-5.


Subject(s)
Acute Lung Injury , Drug Therapy , Genetics , Pathology , Adrenergic alpha-2 Receptor Agonists , Pharmacology , Animals , Aquaporin 1 , Genetics , Allergy and Immunology , Aquaporin 5 , Genetics , Allergy and Immunology , Dexmedetomidine , Pharmacology , Dose-Response Relationship, Drug , Drug Administration Schedule , Gene Expression Regulation , Injections, Intravenous , Interleukin-1beta , Genetics , Allergy and Immunology , Lipopolysaccharides , Lung , Allergy and Immunology , Pathology , Male , Organ Size , Pulmonary Edema , Drug Therapy , Genetics , Pathology , Rats , Rats, Wistar , Signal Transduction , Transcription, Genetic , Tumor Necrosis Factor-alpha , Genetics , Allergy and Immunology
16.
Egyptian Journal of Histology [The]. 2014; 37 (1): 220-232
in English | IMEMR | ID: emr-160202

ABSTRACT

In the retina, glial cells control ionic concentrations by mediation of transmembrane water fluxes through aquaporin [AQP] water channels. The risk factor of a high-salt diet on renal and cardiovascular systems is pretty well known. However, it is not yet known whether a high-salt diet alone can affect the retina. The aim of this study was to determine whether a high-salt diet alone can induce changes in the retina and whether it may be accompanied by changes in the expression and immunolocalization of water channel aquaporin1 [AQP1]. Forty-two adult male albino rats were used. They were divided into three equal groups. Group I served as the control group. Rats in group II were administered 2 ml of a high-salt solution [8% NaCl concentration] once daily by means of a gastric tube. Group III was the recovery group. Retinal tissues were collected and examined by means of light and electron microscopy. Immunohistochemical analysis using AQP1 and glial fibrillary acidic protein [GFAP] antibodies was performed and the results were statistically analyzed. The retina of rats given a high-salt diet [group II] displayed obvious disorganization of the outer segment of photoreceptors, together with cytoplasmic vacuolations in the cells of the inner nuclear and ganglionic layers. Furthermore, significant increase in AQP1 and GFAP immunoexpression was detected. In the recovery group [group III] the retinae of some rats regained their normal histological appearance, whereas others failed to do so. High salt loading might alter glial cell-mediated water transport through AQP1 channels in the retina


Subject(s)
Male , Animals, Laboratory , Aquaporin 1 , Retina/pathology , Retina/ultrastructure , Immunohistochemistry/statistics & numerical data , Microscopy, Polarization/statistics & numerical data , Rats
17.
Chinese Medical Journal ; (24): 4012-4018, 2014.
Article in English | WPRIM | ID: wpr-268431

ABSTRACT

<p><b>BACKGROUND</b>It has found that ischemic postconditioning (IPO) might decrease pulmonary ischemia/reperfusion (I/R) injury, which is one of the main reasons of lung injury caused by cardiopulmonary bypass (CPB). It was found that aquaporins (AQPs) play a role in the maintenance of fluid homeostasis. But it is still unclear whether IPO influences the expression of aquaporin-1 (AQP1). This study was designed to investigate whether IPO can reduce CPB-related lung injury and affect the expression of AQP1 of lungs.</p><p><b>METHODS</b>Twelve healthy dogs were divided into control group (C group) and ischemia postconditioning group (IPO group). CPB procedures were implemented. Ten minutes later, the left pulmonary artery was separated and blocked. Postconditioning consisted of two cycles of 5-minute pulmonary artery reperfusion/5-minute reocclusion starting at the beginning of reperfusion. The 2×4 cm tissues of both sides of pulmonary apex, superior, middle and inferior lobe were taken before CPB (T1), before occlusion and reopening of left pulmonary artery (T2, T3), and 2 hours after CPB (T4). Samples were used to evaluate lung injury degrees and to detect the expression of AQP1. At T1 and T4, blood was collected from femoral artery to calculate pulmonary function.</p><p><b>RESULTS</b>At T4, each pulmonary function showed significant deterioration compared with T1. Lung injury could be found at the onset of CPB. However, the expression of AQP1 decreased and wet to dry weight ratio (W/D) increased after T2. In the left lung of C group, the worst pulmonary function and structures were detected. The slightest changes were discovered in the right lung of C group. A close relationship between W/D and lung injury score was found. The lung injury score was negatively related with the expression of AQP1. It was found that the expression of AQP1 was negatively connected with W/D.</p><p><b>CONCLUSIONS</b>In dog CPB models, lung injury induced by CPB was related with down regulated expression of AQP1. AQP1 is believed to be involved in the mechanisms of lung ischemia/reperfusion (I/R) injury caused by CPB. IPO increases the expression of AQP1, provides a protective effect on lung suffering from CPB, and alleviates CPB-related lung injury.</p>


Subject(s)
Animals , Aquaporin 1 , Metabolism , Cardiopulmonary Bypass , Dogs , Humans , Ischemic Postconditioning , Methods , Lung Injury , Metabolism , Reperfusion Injury , Metabolism
18.
Article in Chinese | WPRIM | ID: wpr-330343

ABSTRACT

<p><b>OBJECTIVE</b>To observe the effect of alcohol extracts from Pharbitidis Semen on the proliferation and metastasis of Lewis lung cancer, and study its anti-tumor mechanism.</p><p><b>METHOD</b>In vitro, MTT assay and scratch assay were adopted to detect the effect of alcohol extracts from Pharbitidis Semen on the proliferation and metastasis of Lewis lung cancer cells. The cell autophagy was detected by the acridine orange staining. The gap-junction intercellular communication (GJIC) was investigated by the fluorescent yellow transfer. The expression of aquaporin 1 (AQP1) was analyzed by the Western blotting. In vivo, the subcutaneous implant model and the experimental pulmonary metastasis model of Lewis lung cancer in mice were established to evaluate the anti-tumor and anti-metastasis effects of alcohol extract from Pharbitidis Semen. The serum carcinoembryonic antigen (CEA) and beta2 microglobulin (beta2-MG) of mice bearing Lewis lung cancer were detected by the electrochemiluminesence immunoassay. The expressions of lung AQP1 and Connexin 43 (Cx43) were examined by the immunohistochemical method.</p><p><b>RESULT</b>In vitro, alcohol extracts from Pharbitidis Semen inhibited the cell proliferation in a dose-dependent matter, significantly prevented the cell migration, down-regulated AQP1 proteins of cells, promoted GJIC, and decreased the serum-free autophagy of tumor cells. In vivo, compared with untreated model mice, alcohol extracts from Pharbitidis Semen inhibited the tumor growth in a dose-dependent matter, prevented the tumor metastasis and prolonged the life span of mice bearing Lewis lung cancer, while decreasing serum CEA and beta2-MG of mice bearing Lewis lung cancer, enhancing the immumohistochemical staining intensity of Cx43 and weakening aquaporins AQP1 positive intensity.</p><p><b>CONCLUSION</b>Alcohol extracts from Pharbitidis Semen could prevent the proliferation and metastasis in Lewis lung cancer cells. Its mechanism may be related to the promotion of GJIC and the down-regulation of AQP1.</p>


Subject(s)
Animals , Antineoplastic Agents , Aquaporin 1 , Genetics , Metabolism , Carcinoma, Lewis Lung , Drug Therapy , Genetics , Metabolism , Pathology , Cell Line, Tumor , Connexin 43 , Genetics , Metabolism , Disease Models, Animal , Drugs, Chinese Herbal , Humans , Ipomoea , Chemistry , Lung Neoplasms , Drug Therapy , Genetics , Metabolism , Pathology , Male , Mice , Mice, Inbred C57BL , Neoplasm Metastasis , Seeds , Chemistry
19.
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 , Aquaporin 1/metabolism , Aquaporin 4/metabolism , Aquaporin 6/metabolism , Aquaporins/metabolism , Edema/pathology , Immunohistochemistry , Mice , Muscle Cells/metabolism , Myocardial Infarction/metabolism , Myocardium/metabolism , Time Factors
20.
Article in English | WPRIM | ID: wpr-166293

ABSTRACT

PURPOSE: This study was designed to investigate the effect of detrusor overactivity induced by partial bladder outlet obstruction (BOO) on the expression of aquaporin 1 (AQP1) and caveolin 1 (CAV1) in the rat urinary bladder, and to determine the role of these molecules in detrusor overactivity. METHODS: Female Sprague-Dawley rats were divided into control (n=30) and experimental (n=30) groups. The BOO group underwent partial BOO, and the control group underwent a sham operation. After 4 weeks, an urodynamic study was performed to measure the contraction interval and contraction pressure. The expression and cellular localization of AQP1 and CAV1 were determined by western blot and immunofluorescence experiments in the rat urinary bladder. RESULTS: In cystometrograms, the contraction interval was significantly lower in the BOO group (2.9+/-1.5 minutes) than in the control group (6.7+/-1.0 minutes) (P<0.05). Conversely, the average contraction pressure was significantly higher in the BOO group (21.2+/-3.3 mmHg) than in the control group (13.0+/-2.5 mmHg) (P<0.05). AQP1 and CAV1 were coexpressed in the capillaries, arterioles, and venules of the suburothelial layer. AQP1 and CAV1 protein expression was significantly increased in the BOO rats compared to the control rats (P<0.05). CONCLUSIONS: Detrusor overactivity induced by BOO causes a significant increase in the expression of AQP1 and CAV1, which were coexpressed in the suburothelial microvasculature. This finding suggests that AQP1 and CAV1 might be closely related to bladder signal activity and may have a functional role in BOO-associated detrusor overactivity.


Subject(s)
Animals , Aquaporin 1 , Arterioles , Blotting, Western , Capillaries , Caveolin 1 , Female , Fluorescent Antibody Technique , Humans , Microvessels , Rats , Rats, Sprague-Dawley , Urinary Bladder Neck Obstruction , Urinary Bladder , Urodynamics , Urothelium , Venules
SELECTION OF CITATIONS
SEARCH DETAIL