Plasma membrane intrinsic proteins(PIPs)are conserved plant aquaporins that transport small molecules across the plasma membrane to trigger instant stress responses and maintain cellular homeostasis under biotic and a...Plasma membrane intrinsic proteins(PIPs)are conserved plant aquaporins that transport small molecules across the plasma membrane to trigger instant stress responses and maintain cellular homeostasis under biotic and abiotic stress.To elucidate their roles in plant immunity to pathogen attack,we characterized the expression patterns,subcellular localizations,and H_(2)O_(2)-transport ability of 11 OsPIPs in rice(Oryza sativa),and identified OsPIP2;6 as necessary for rice disease resistance.OsPIP2;6 resides on the plasma membrane and facilitates cytoplasmic import of the immune signaling molecule H_(2)O_(2).Knockout of OsPIP2;6 increases rice susceptibility to Magnaporthe oryzae,indicating a positive function in plant immunity.OsPIP2;6 interacts with OsPIP2;2,which has been reported to increase rice resistance to pathogens via H_(2)O_(2)transport.Our findings suggest that OsPIP2;6 cooperates with OsPIP2;2 as a defense signal transporter complex during plant–pathogen interaction.展开更多
Compared to other organisms,plants have evolved a greater number of aquaporins with diverse substrates and functions to adapt to ever-changing environmental and internal stimuli for growth and development.Although aqu...Compared to other organisms,plants have evolved a greater number of aquaporins with diverse substrates and functions to adapt to ever-changing environmental and internal stimuli for growth and development.Although aquaporins were initially identified as channels that allow water molecules to cross biological membranes,progress has been made in identifying various novel permeable substrates.Many studies have characterized the versatile physiological and biophysical functions of plant aquaporins.Here,we review the recent reports that highlight aquaporin-facilitated regulation of major physiological processes and stress tolerance throughout plant life cycles as well as the potential prospects and possibilities of applying aquaporins to improve agricultural productivity,food quality,environmental protection,and ecological conservation.展开更多
[Objective] This study was to explore the subcellular localization of aquaporins OsPIP2-6 in rice. [Method] A key rice aquaporins gene OsPIP2-6 was cloned and used for construction of a transient expression vector,whi...[Objective] This study was to explore the subcellular localization of aquaporins OsPIP2-6 in rice. [Method] A key rice aquaporins gene OsPIP2-6 was cloned and used for construction of a transient expression vector,which was then transformed into onion epidermis via particle bombardment for confocal microscopy analysis using YFP gene as a reporter gene. [Result] The results showed that rice aquaporins OsPIP2-6 was mainly located in the plasma membrane. [Conclusion] Our results provided theoretical basis for further understanding plant aquaporins.展开更多
AIM: To investigate whether the regulation of aquaporin 3 (AQP3) and AQP9 induced by Auphen and dibutyryl cAMP (dbcAMP) inhibits hepatic tumorigenesis.METHODS: Expression of AQP3 and AQP9 was detected by Western blot,...AIM: To investigate whether the regulation of aquaporin 3 (AQP3) and AQP9 induced by Auphen and dibutyryl cAMP (dbcAMP) inhibits hepatic tumorigenesis.METHODS: Expression of AQP3 and AQP9 was detected by Western blot, immunohistochemistry (IHC), and RT-PCR in HCC samples and paired non-cancerous liver tissue samples from 30 hepatocellular carcinoma (HCC) patients. A xenograft tumor model was used in vivo. Nine nude mice were divided into control, Auphen-treated, and dbcAMP-treated groups (n = 3 for each group). AQP3 and AQP9 protein expression after induction of xenograft tumors was detected by IHC and mRNA by RT-PCR analysis. The terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling assay and histological evaluation were used to detect apoptosis of tumor cells, and the concentration of serum α-fetoprotein (AFP) was measured using RT-PCR and an ELISA kit.RESULTS: The volumes and weights of tumors decreased significantly in the Auphen- and dbcAMP-treated mice compared with the control mice (P < 0.01). The levels of AQP3 were significantly lower in the Auphen treatment group, and levels of AQP9 were significantly higher in thedbcAMP treatment mice than in the control mice (P < 0.01). The reduction of AQP3 by Auphen and increase of AQP9 by dbcAMP in nude mice suppressed tumor growth of HCC, which resulted in reduced AFP levels in serum and tissues, and apoptosis of tumor cells in the Auphen- and dbcAMP-treated mice, when compared with control mice (P < 0.01). Compared with para-carcinoma tissues, AQP3 expression increased in tumor tissues whereas the expression of AQP9 decreased. By correlating clinicopathological and expression levels, we demonstrated that the expression of AQP3 and AQP9 was correlated with clinical progression of HCC and disease outcomes.CONCLUSION: AQP3 increases in HCC while AQP9 decreases. Regulation of AQP3 and AQP9 expression by Auphen and dbcAMP inhibits the development and growth of HCC.展开更多
Rotavirus diarrhea is a major worldwide cause of infantile gastroenteritis; however, the mechanism responsible for intestinal fluid loss remains unclear. Water transfer across the intestinal epithelial membrane seems ...Rotavirus diarrhea is a major worldwide cause of infantile gastroenteritis; however, the mechanism responsible for intestinal fluid loss remains unclear. Water transfer across the intestinal epithelial membrane seems to occur because of aquaporins(AQPs). Accumulating evidence indicates that alterations in AQPs may play an important role in pathogenesis. Here, we focus on changes in AQPs in a mouse model of rotavirus diarrhea. In the present study, 32 of 35 mice developed diarrhea and mild dehydration within 24 hours after infection with rotavirus strain SA11. Intestinal epithelial cells demonstrated cytoplasmic vacuolation, malaligned villi, and atrophy. AQP1 expression was significantly attenuated in the ileum and colon in comparison with controls; likewise, AQP4 and-8 protein expression were significantly decreased in the colon of rotavirus diarrhea-infected mice. In contrast, AQP3 protein expression was significantly increased in the colon of rotavirus-infected mice in comparison with controls. These results indicate that rotavirus diarrhea is associated with the downregulation of AQP1,-4, and-8 expression. Therefore, AQPs play an important role in rotavirus diarrhea.展开更多
This review focuses on current knowledge on hepato-cyte aquaporins(AQPs)and their significance in bile formation and cholestasis.Canalicular bile secretion results from a combined interaction of several solute transpo...This review focuses on current knowledge on hepato-cyte aquaporins(AQPs)and their significance in bile formation and cholestasis.Canalicular bile secretion results from a combined interaction of several solute transporters and AQP water channels that facilitate water flow in response to the osmotic gradients created. During choleresis,hepatocytes rapidly increase their canalicular membrane water permeability by modulating the abundance of AQP8.The question was raised as to whether the opposite process,i.e.a decreased canalicular AQP8 expression would contribute to the development of cholestasis.Studies in several experimental models of cholestasis,such as extrahepatic obstructive cholestasis,estrogen-induced cholestasis, and sepsis-induced cholestasis demonstrated that the protein expression of hepatocyte AQP8 was impaired. In addition,biophysical studies in canalicular plasma membranes revealed decreased water permeability associated with AQP8 protein downregulation.The combined alteration in hepatocyte solute transporters and AQP8 would hamper the efficient coupling of osmotic gradients and canalicular water flow.Thus cholestasis may result from a mutual occurrence of impaired solute transport and decreased water permeability.展开更多
Background:Aquaporins(AQPs)are a family of transmembrane water channels that includes orthodox AQPs,aquaglyceroporins(GLPs)and super AQPs.AQP3,AQP7,AQP9 and AQP11 have been identified in boar sperm,and they are crucia...Background:Aquaporins(AQPs)are a family of transmembrane water channels that includes orthodox AQPs,aquaglyceroporins(GLPs)and super AQPs.AQP3,AQP7,AQP9 and AQP11 have been identified in boar sperm,and they are crucial for sperm maturation and osmoregulation.Water exchange is an important event in cryopreservation,which is the most efficient method for long-term storage of sperm.However,the freezethaw process leads to sperm damage and a loss of fertilizing potential.Assuming that the quality of frozenthawed sperm partially depends on the regulation of osmolality variations during this process,AQPs might play a crucial role in boar semen freezability.In this context,the aim of this study was to unravel the functional relevance of the different groups of AQPs for boar sperm cryotolerance through three different inhibitors.Results:Inhibition of different groups of AQPs was found to have different effects on boar sperm cryotolerance.Whereas the use of 1,3-propanediol(PDO),an inhibitor of orthodox AQPs and GLPs,decreased total motility(P<0.05),it increased post-thaw sperm viability,lowered membrane lipid disorder and increased mitochondrial membrane potential(MMP)(P<0.05).When acetazolamide(AC)was used as an inhibitor of orthodox AQPs,the effects on post-thaw sperm quality were restricted to a mild increase in MMP in the presence of the intermediate concentration at 30 min post-thaw and an increase in superoxide levels(P<0.05).Finally,the addition of phloretin(PHL),a GLP inhibitor,had detrimental effects on post-thaw total and progressive sperm motilities,viability and lipid membrane disorder(P<0.05).Conclusions:The effects of the different inhibitors suggest that GLPs rather than orthodox AQPs are relevant for boar sperm freezability.Moreover,the positive effect of PDO on sperm quality suggests a cryoprotective role for this molecule.展开更多
Water channels or aquaporins are the main pathways of water transport. Both the existence and function of aquaporins in die guard cells of Vicia faba L. were investigated both by using RD28 cDNA and RD28 antibody as p...Water channels or aquaporins are the main pathways of water transport. Both the existence and function of aquaporins in die guard cells of Vicia faba L. were investigated both by using RD28 cDNA and RD28 antibody as probes, and by controlling stomatal movement as a parameter combined with antibody and inhibitor of aquaporins respectively. The results revealed that RD28 mRNA, encoding a plasma membrane aquaporin, expressed in ale mesophyll cells and vascular tissues of V. faba, especially in guard cells. And the location of RD28-like proteins was mainly on plasma membrane of guard cells. The addition of 25 mumol/L HgCl2, an aquaporin blocker, and antibody of RD28 as well, greatly suppressed the stomatal opening or guardcell protoplast swelling induced by fusicoccin and light, and closing induced by abscisic acid. However, 5 mmol/L, beta-mercaptoethanol, a reverse reagent of aquaporin blocker, reversed the inhibitory effect of HgCl2 Pretreatment oil stomatal opening ( i.e., HgCl2 was removed after HgCl2 pretreatment for 10 min). The results suggest that the aquaporins in V. faba are associated with stomatal movement.展开更多
[Objective] The aim of this study was to identify the roles of an aquaporin gene GhNIP5.1 in upland cotton （Gossypium hirsutum） by bioinformatics method, so as to provide theoretical basis for further research on aq...[Objective] The aim of this study was to identify the roles of an aquaporin gene GhNIP5.1 in upland cotton （Gossypium hirsutum） by bioinformatics method, so as to provide theoretical basis for further research on aquaporins in upland cotton. [Method] In silico molecular cloning was adopted to obtain an ORF sequence of GhNIP5.1 gene, which was then analyzed by the methods of bioinformatics. The coding region of GhNIP5.1 gene was obtained by analyzing the cotton genome se-quence published in NCBI. [Result] This cDNA sequence had a complete open reading frame of 897 bp and encoded 298 amino acid residues, including the con-served domain NPA （Asn-Pro-Ala） of MIP superfamily. The similarities of GhNIP5.1 deduced amino acid sequences from upland cotton with grape and Arabidopsis, were up to 89.3% and 83.2%, respectively. GhNIP5.1 was most similar in homology and 3-D structure of proteins to AtNIP5.1 among the nine members of NIP family in Arabidopsis. The coding region length of GhNIP5.1 gene was 2 067 bp, and it con-tained three introns and four exons. Al the exon-intron junctions of the gene con-tained the consensus splicing site pair GT-AG. [Conclusion] GhNIP5.1 gene probably has similar physiological functions with Arabidopsis AtNIP5.1.展开更多
[ Objective] The aim was to construct drought and saline-alkaline resistance plant expression vector with mannose as selective agent, and further breed unmarked resilient varieties. [ Method] The plant expression vect...[ Objective] The aim was to construct drought and saline-alkaline resistance plant expression vector with mannose as selective agent, and further breed unmarked resilient varieties. [ Method] The plant expression vector was constructed by using Chimonanthus praecox（ L. ）Link aquapor.in CpTIP cDNA and Escherichia coli pmi gene, combined stress resistance gene with mannose positive selection system. [ Result] The test successfully constructed the plant expression vector pPMI：：CpTIP. [ Conclusion] The constructed vector linked advantages of stress resistance gene and mannose positive selection system.展开更多
基金supported by the Guangdong Basic and Applied Basic Research Foundation(2020A1515111101,2022A1515110431).
文摘Plasma membrane intrinsic proteins(PIPs)are conserved plant aquaporins that transport small molecules across the plasma membrane to trigger instant stress responses and maintain cellular homeostasis under biotic and abiotic stress.To elucidate their roles in plant immunity to pathogen attack,we characterized the expression patterns,subcellular localizations,and H_(2)O_(2)-transport ability of 11 OsPIPs in rice(Oryza sativa),and identified OsPIP2;6 as necessary for rice disease resistance.OsPIP2;6 resides on the plasma membrane and facilitates cytoplasmic import of the immune signaling molecule H_(2)O_(2).Knockout of OsPIP2;6 increases rice susceptibility to Magnaporthe oryzae,indicating a positive function in plant immunity.OsPIP2;6 interacts with OsPIP2;2,which has been reported to increase rice resistance to pathogens via H_(2)O_(2)transport.Our findings suggest that OsPIP2;6 cooperates with OsPIP2;2 as a defense signal transporter complex during plant–pathogen interaction.
基金supported by the National Key Research and Development Program of China(2021YFD1201104-02)National Natural Science Foundation of China(32272048)to Xiaodong Ding。
文摘Compared to other organisms,plants have evolved a greater number of aquaporins with diverse substrates and functions to adapt to ever-changing environmental and internal stimuli for growth and development.Although aquaporins were initially identified as channels that allow water molecules to cross biological membranes,progress has been made in identifying various novel permeable substrates.Many studies have characterized the versatile physiological and biophysical functions of plant aquaporins.Here,we review the recent reports that highlight aquaporin-facilitated regulation of major physiological processes and stress tolerance throughout plant life cycles as well as the potential prospects and possibilities of applying aquaporins to improve agricultural productivity,food quality,environmental protection,and ecological conservation.
基金Supported by Program for Science and Technology Development in Shijiazhuang City(10120803)Doctoral Research Fund of Shijiazhuang University(2007012)~~
文摘[Objective] This study was to explore the subcellular localization of aquaporins OsPIP2-6 in rice. [Method] A key rice aquaporins gene OsPIP2-6 was cloned and used for construction of a transient expression vector,which was then transformed into onion epidermis via particle bombardment for confocal microscopy analysis using YFP gene as a reporter gene. [Result] The results showed that rice aquaporins OsPIP2-6 was mainly located in the plasma membrane. [Conclusion] Our results provided theoretical basis for further understanding plant aquaporins.
基金Supported by Science and Technology Commission of Shanghai,No.13ZR1406700 and No.13DZ1930908
文摘AIM: To investigate whether the regulation of aquaporin 3 (AQP3) and AQP9 induced by Auphen and dibutyryl cAMP (dbcAMP) inhibits hepatic tumorigenesis.METHODS: Expression of AQP3 and AQP9 was detected by Western blot, immunohistochemistry (IHC), and RT-PCR in HCC samples and paired non-cancerous liver tissue samples from 30 hepatocellular carcinoma (HCC) patients. A xenograft tumor model was used in vivo. Nine nude mice were divided into control, Auphen-treated, and dbcAMP-treated groups (n = 3 for each group). AQP3 and AQP9 protein expression after induction of xenograft tumors was detected by IHC and mRNA by RT-PCR analysis. The terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling assay and histological evaluation were used to detect apoptosis of tumor cells, and the concentration of serum α-fetoprotein (AFP) was measured using RT-PCR and an ELISA kit.RESULTS: The volumes and weights of tumors decreased significantly in the Auphen- and dbcAMP-treated mice compared with the control mice (P < 0.01). The levels of AQP3 were significantly lower in the Auphen treatment group, and levels of AQP9 were significantly higher in thedbcAMP treatment mice than in the control mice (P < 0.01). The reduction of AQP3 by Auphen and increase of AQP9 by dbcAMP in nude mice suppressed tumor growth of HCC, which resulted in reduced AFP levels in serum and tissues, and apoptosis of tumor cells in the Auphen- and dbcAMP-treated mice, when compared with control mice (P < 0.01). Compared with para-carcinoma tissues, AQP3 expression increased in tumor tissues whereas the expression of AQP9 decreased. By correlating clinicopathological and expression levels, we demonstrated that the expression of AQP3 and AQP9 was correlated with clinical progression of HCC and disease outcomes.CONCLUSION: AQP3 increases in HCC while AQP9 decreases. Regulation of AQP3 and AQP9 expression by Auphen and dbcAMP inhibits the development and growth of HCC.
基金supported by funding from Guangdong Natural Science Foundation (grants:S2012010009211,S2012010009538)Key Specialty Projects of Guangzhou Board of Health (grant:20121A021014)
文摘Rotavirus diarrhea is a major worldwide cause of infantile gastroenteritis; however, the mechanism responsible for intestinal fluid loss remains unclear. Water transfer across the intestinal epithelial membrane seems to occur because of aquaporins(AQPs). Accumulating evidence indicates that alterations in AQPs may play an important role in pathogenesis. Here, we focus on changes in AQPs in a mouse model of rotavirus diarrhea. In the present study, 32 of 35 mice developed diarrhea and mild dehydration within 24 hours after infection with rotavirus strain SA11. Intestinal epithelial cells demonstrated cytoplasmic vacuolation, malaligned villi, and atrophy. AQP1 expression was significantly attenuated in the ileum and colon in comparison with controls; likewise, AQP4 and-8 protein expression were significantly decreased in the colon of rotavirus diarrhea-infected mice. In contrast, AQP3 protein expression was significantly increased in the colon of rotavirus-infected mice in comparison with controls. These results indicate that rotavirus diarrhea is associated with the downregulation of AQP1,-4, and-8 expression. Therefore, AQPs play an important role in rotavirus diarrhea.
基金Grant PICT 05-31670(R.A.Marinelli) from Agencia Nacional de Promoción Científica y Tecnológicaby Grant PIP 6440 from Consejo Nacional de Investigaciones Científicas y Técnicas
文摘This review focuses on current knowledge on hepato-cyte aquaporins(AQPs)and their significance in bile formation and cholestasis.Canalicular bile secretion results from a combined interaction of several solute transporters and AQP water channels that facilitate water flow in response to the osmotic gradients created. During choleresis,hepatocytes rapidly increase their canalicular membrane water permeability by modulating the abundance of AQP8.The question was raised as to whether the opposite process,i.e.a decreased canalicular AQP8 expression would contribute to the development of cholestasis.Studies in several experimental models of cholestasis,such as extrahepatic obstructive cholestasis,estrogen-induced cholestasis, and sepsis-induced cholestasis demonstrated that the protein expression of hepatocyte AQP8 was impaired. In addition,biophysical studies in canalicular plasma membranes revealed decreased water permeability associated with AQP8 protein downregulation.The combined alteration in hepatocyte solute transporters and AQP8 would hamper the efficient coupling of osmotic gradients and canalicular water flow.Thus cholestasis may result from a mutual occurrence of impaired solute transport and decreased water permeability.
基金the European Commission(H2020-MSCA-IF-79212)the Ministry of Science,Innovation and Universities,Spain(Grants:RYC-2014-15581,AGL2016–81890-REDT,AGL2017–88329-R and FJCI-2017-31689)the Regional Government of Catalonia,Spain(2017-SGR-1229).
文摘Background:Aquaporins(AQPs)are a family of transmembrane water channels that includes orthodox AQPs,aquaglyceroporins(GLPs)and super AQPs.AQP3,AQP7,AQP9 and AQP11 have been identified in boar sperm,and they are crucial for sperm maturation and osmoregulation.Water exchange is an important event in cryopreservation,which is the most efficient method for long-term storage of sperm.However,the freezethaw process leads to sperm damage and a loss of fertilizing potential.Assuming that the quality of frozenthawed sperm partially depends on the regulation of osmolality variations during this process,AQPs might play a crucial role in boar semen freezability.In this context,the aim of this study was to unravel the functional relevance of the different groups of AQPs for boar sperm cryotolerance through three different inhibitors.Results:Inhibition of different groups of AQPs was found to have different effects on boar sperm cryotolerance.Whereas the use of 1,3-propanediol(PDO),an inhibitor of orthodox AQPs and GLPs,decreased total motility(P<0.05),it increased post-thaw sperm viability,lowered membrane lipid disorder and increased mitochondrial membrane potential(MMP)(P<0.05).When acetazolamide(AC)was used as an inhibitor of orthodox AQPs,the effects on post-thaw sperm quality were restricted to a mild increase in MMP in the presence of the intermediate concentration at 30 min post-thaw and an increase in superoxide levels(P<0.05).Finally,the addition of phloretin(PHL),a GLP inhibitor,had detrimental effects on post-thaw total and progressive sperm motilities,viability and lipid membrane disorder(P<0.05).Conclusions:The effects of the different inhibitors suggest that GLPs rather than orthodox AQPs are relevant for boar sperm freezability.Moreover,the positive effect of PDO on sperm quality suggests a cryoprotective role for this molecule.
文摘Water channels or aquaporins are the main pathways of water transport. Both the existence and function of aquaporins in die guard cells of Vicia faba L. were investigated both by using RD28 cDNA and RD28 antibody as probes, and by controlling stomatal movement as a parameter combined with antibody and inhibitor of aquaporins respectively. The results revealed that RD28 mRNA, encoding a plasma membrane aquaporin, expressed in ale mesophyll cells and vascular tissues of V. faba, especially in guard cells. And the location of RD28-like proteins was mainly on plasma membrane of guard cells. The addition of 25 mumol/L HgCl2, an aquaporin blocker, and antibody of RD28 as well, greatly suppressed the stomatal opening or guardcell protoplast swelling induced by fusicoccin and light, and closing induced by abscisic acid. However, 5 mmol/L, beta-mercaptoethanol, a reverse reagent of aquaporin blocker, reversed the inhibitory effect of HgCl2 Pretreatment oil stomatal opening ( i.e., HgCl2 was removed after HgCl2 pretreatment for 10 min). The results suggest that the aquaporins in V. faba are associated with stomatal movement.
基金Supported by National Natural Science Foundation of China(31301682)AgriculturalScience and Technology Innovation Program of Jiangsu Province[CX(12)3068]SpecialProject for Breeding and Cultivation of GMO Varieties(2011ZX08005-001)~~
文摘[Objective] The aim of this study was to identify the roles of an aquaporin gene GhNIP5.1 in upland cotton （Gossypium hirsutum） by bioinformatics method, so as to provide theoretical basis for further research on aquaporins in upland cotton. [Method] In silico molecular cloning was adopted to obtain an ORF sequence of GhNIP5.1 gene, which was then analyzed by the methods of bioinformatics. The coding region of GhNIP5.1 gene was obtained by analyzing the cotton genome se-quence published in NCBI. [Result] This cDNA sequence had a complete open reading frame of 897 bp and encoded 298 amino acid residues, including the con-served domain NPA （Asn-Pro-Ala） of MIP superfamily. The similarities of GhNIP5.1 deduced amino acid sequences from upland cotton with grape and Arabidopsis, were up to 89.3% and 83.2%, respectively. GhNIP5.1 was most similar in homology and 3-D structure of proteins to AtNIP5.1 among the nine members of NIP family in Arabidopsis. The coding region length of GhNIP5.1 gene was 2 067 bp, and it con-tained three introns and four exons. Al the exon-intron junctions of the gene con-tained the consensus splicing site pair GT-AG. [Conclusion] GhNIP5.1 gene probably has similar physiological functions with Arabidopsis AtNIP5.1.
基金Supported by Sub-project of Special Fund in Ministry of Agriculture of Transgenic Plants " Cultivation of New Varieties of Anti-adversity Transgenic Soybeans"(2008ZX08004-2)~~
文摘[ Objective] The aim was to construct drought and saline-alkaline resistance plant expression vector with mannose as selective agent, and further breed unmarked resilient varieties. [ Method] The plant expression vector was constructed by using Chimonanthus praecox（ L. ）Link aquapor.in CpTIP cDNA and Escherichia coli pmi gene, combined stress resistance gene with mannose positive selection system. [ Result] The test successfully constructed the plant expression vector pPMI：：CpTIP. [ Conclusion] The constructed vector linked advantages of stress resistance gene and mannose positive selection system.
