UpToDate Contents
全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.
- 1. 腎でのマグネシウム処理における利尿剤の有効性effect of diuretics on magnesium handling by the kidney [show details]
…exit. The thiazide-type diuretics decrease NaCl reabsorption in the distal tubule by inhibiting electroneutral Na-Cl cotransporters in the apical membrane that are responsible for the entry of luminal sodium…
- 2. 赤血球水分量の制御control of red blood cell hydration [show details]
…monotonic decrease in Ca-ATPase activity . Several passive, gradient-driven systems, including electroneutral cotransporters and ion- or water-specific channels, utilize the inward sodium and outward potassium …
- 3. 小児における急性下痢症の病因pathogenesis of acute diarrhea in children [show details]
…(SGLT1 [SLC5A1]), and Cl–/HCO3– exchangers (DRA [SLC26A3] and PAT1 [SLC26A6]). Electroneutral fluid absorption is carried out by the coordinated activity of NHE3 with Cl–/HCO3– …
- 4. バーター症候群およびギテルマン症候群bartter and gitelman syndromes [show details]
…cotransporter that is present in the luminal membrane. Ion reabsorption by the cotransporter is electroneutral. A large fraction of the absorbed potassium reenters the lumen via potassium channels (ROMK)…
English Journal
- PAT4 is abundantly expressed in excitatory and inhibitory neurons as well as epithelial cells.
- Roshanbin S1, Hellsten SV2, Tafreshiha A3, Zhu Y4, Raine A5, Fredriksson R6.Author information 1Department of Neuroscience, Functional Pharmacology, Uppsala University, Uppsala, SE 75124, Sweden. Electronic address: Sahar.Roshanbin@neuro.uu.se.2Department of Neuroscience, Functional Pharmacology, Uppsala University, Uppsala, SE 75124, Sweden. Electronic address: Sofie.Hellsten@neuro.uu.se.3Department of Neuroscience, Functional Pharmacology, Uppsala University, Uppsala, SE 75124, Sweden. Electronic address: atieh.tafreshiha@gmail.com.4Department of Neuroscience, Functional Pharmacology, Uppsala University, Uppsala, SE 75124, Sweden. Electronic address: zhuyinan0108@gmail.com.5Department of Neuroscience, Functional Pharmacology, Uppsala University, Uppsala, SE 75124, Sweden. Electronic address: Amanda.raine@medsci.uu.se.6Department of Neuroscience, Functional Pharmacology, Uppsala University, Uppsala, SE 75124, Sweden. Electronic address: Robert.Fredriksson@neuro.uu.se.AbstractPAT4, the fourth member of the SLC36/proton dependent amino acid transporter (PAT) family, is a high-affinity, low capacity electroneutral transporter of neutral amino acids like proline and tryptophan. It has also been associated with the function of mTORC1, a complex in the mammalian target of rapamycin (mTOR) pathway. We performed in situ hybridization and immunohistological analysis to determine the expression profile of PAT4, as well as an RT-PCR study on tissue from mice exposed to leucine. We performed a phylogenetic analysis to determine the evolutionary origin of PAT4. The in situ hybridization and the immunohistochemistry on mouse brain sections and hypothalamic cells showed abundant PAT4 expression in the mouse brain intracellularly in both inhibitory and excitatory neurons, partially co-localizing with lysosomal markers and epithelial cells lining the ventricles. Its location in epithelial cells around the ventricles indicates a transport of substrates across the blood brain barrier. Phylogenetic analysis showed that PAT4 belongs to an evolutionary old family most likely predating animals, and PAT4 is the oldest member of that family.
- Brain research.Brain Res.2014 Apr 4;1557:12-25. doi: 10.1016/j.brainres.2014.02.014. Epub 2014 Feb 14.
- PAT4, the fourth member of the SLC36/proton dependent amino acid transporter (PAT) family, is a high-affinity, low capacity electroneutral transporter of neutral amino acids like proline and tryptophan. It has also been associated with the function of mTORC1, a complex in the mammalian target of rap
- PMID 24530433
- Keeping it simple - Transport Mechanism and pH Regulation in Na+/H+ Exchangers.
- Călinescu O1, Paulino C, Kühlbrandt W, Fendler K.Author information 1Max Planck Institute of Biophysics, Germany.AbstractNa+/H+ exchangers are essential for regulation of intracellular proton and sodium concentrations in all living organisms. We examine and experimentally verify a kinetic model for Na+/H+ exchangers, where a single binding site is alternatively occupied by Na+ or one or two H+ ions. The proposed transport mechanism inherently down-regulates Na+/H+ exchangers at extreme pH, preventing excessive cytoplasmic acidification or alkalinization. As experimental test system we present the first electrophysiological investigation of an electroneutral Na+/H+ exchanger, NhaP1 from Methanocaldococcus jannaschii (MjNhaP1), a close homologue of the medically important eukaryotic NHE Na+/H+ exchangers. The kinetic model describes the experimentally observed substrate dependencies of MjNhaP1, and the transport mechanism explains alkaline down-regulation of MjNhaP1. Since this model also accounts for acidic down-regulation of the electrogenic NhaA Na+/H+ exchanger from Escherichia coli (EcNhaA, shown in a previous publication) we conclude that it applies generally to all Na+/H+ exchangers, electrogenic as well as electroneutral, and elegantly explains their pH regulation. Furthermore, the electrophysiological analysis allows insight into the electrostatic structure of the translocation complex in electroneutral and electrogenic Na+/H+ exchangers.
- The Journal of biological chemistry.J Biol Chem.2014 Mar 18. [Epub ahead of print]
- Na+/H+ exchangers are essential for regulation of intracellular proton and sodium concentrations in all living organisms. We examine and experimentally verify a kinetic model for Na+/H+ exchangers, where a single binding site is alternatively occupied by Na+ or one or two H+ ions. The proposed trans
- PMID 24644283
- Berberine and Its Metabolites: Relationship between Physicochemical Properties and Plasma Levels after Administration to Human Subjects.
- Spinozzi S1, Colliva C, Camborata C, Roberti M, Ianni C, Neri F, Calvarese C, Lisotti A, Mazzella G, Roda A.Author information 1Department of Chemistry "G. Ciamician", University of Bologna , Via Selmi 2, 40126 Bologna, Italy.AbstractBerberine (1) is an alkaloid used widely in the treatment of several diseases. However, its physicochemical properties, pharmacokinetics, and metabolism remain unclear, and conflicting data have been reported. In this study, the main physicochemical properties of 1 and its metabolites were evaluated, including lipophilicity, solubility, pKa, and albumin binding. A sensitive HPLC-ESIMS/MS method was developed and validated to identify 1 and its main metabolites in human plasma. This method was used to quantify their levels in the plasma of healthy volunteers and hypercholesterolemic patients following a single dose and chronic administration, respectively. In both cases, berberrubine (2) was found to be the main metabolite. Surprisingly, 2 is more lipophilic than 1, which suggests that this compound tautomerizes to a highly conjugated, electroneutral quinoid structure. This was confirmed by NMR studies. These results indicate that the higher plasma concentration of 2 was a consequence of a more efficient intestinal absorption, suggesting that berberrubine is potentially more pharmacologically active than berberine.
- Journal of natural products.J Nat Prod.2014 Mar 5. [Epub ahead of print]
- Berberine (1) is an alkaloid used widely in the treatment of several diseases. However, its physicochemical properties, pharmacokinetics, and metabolism remain unclear, and conflicting data have been reported. In this study, the main physicochemical properties of 1 and its metabolites were evaluated
- PMID 24593257
Japanese Journal
- Relationship between sodium-dependent phosphate transporter (NaPi-IIc) function and cellular vacuole formation in opossum kidney cells
- ヒト赤血球膜タンパク質バンド3の構造:―膜貫通ドメインの二次元結晶構造解析―
- Inactivation of Escherichia coli using atmospheric-pressure plasma jet