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1.
J Cell Sci ; 135(6)2022 03 15.
Article in English | MEDLINE | ID: mdl-35237814

ABSTRACT

Osp94 (also known as HSPA4L or HSPH3), a member of the Hsp110/Sse1 family of heat-shock proteins, has a longer C-terminus than found in Hsc70/Hsp70 family proteins, composed of the loop region with a partial substrate-binding domain (SBD) ß (L), and the SBDα and the C-terminal extension (H), but the functions of these domains are poorly understood. Here, we found that Osp94 suppressed heat-induced aggregation of luciferase (Luc). Osp94-bound heat-inactivated Luc was reactivated in the presence of rabbit reticulocyte lysate (RRL) and/or a combination of Hsc70 and Hsp40 (also known as HSPA8 and DNAJB1, respectively). Targeted deletion mutagenesis revealed that the SBDß and H domains of Osp94 are critical for protein disaggregation and RRL-mediated refolding. Reactivation of Hsp90-bound heat-inactivated Luc was abolished in the absence of RRL but compensated for by PA28α (also known as PSME1), a proteasome activator. Interestingly, the LH domain also reactivated heat-inactivated Luc, independently of PA28α. Biotin-tag cross-linking experiments indicated that the LH domain and PA28α interact with Luc bound by Hsp90 during refolding. A chimeric protein in which the H domain was exchanged for PA28α also mediated disaggregation and reactivation of heat-inactivated Luc. These results indicate that Osp94 acts as a holdase, and that the C-terminal region plays a PA28α-like role in the refolding of unfolded proteins.


Subject(s)
HSP40 Heat-Shock Proteins , HSP70 Heat-Shock Proteins , Animals , Family , HSC70 Heat-Shock Proteins/metabolism , HSP40 Heat-Shock Proteins/genetics , HSP40 Heat-Shock Proteins/metabolism , HSP70 Heat-Shock Proteins/genetics , HSP70 Heat-Shock Proteins/metabolism , Heat-Shock Proteins/metabolism , Protein Refolding , Rabbits
2.
Cell Stress Chaperones ; 25(2): 303, 2020 Mar.
Article in English | MEDLINE | ID: mdl-32072442

ABSTRACT

In the original publication, the given name of the last author was incorrectly displayed as the name must read: Katsuyoshi Masuda.

3.
Cell Stress Chaperones ; 25(2): 287-301, 2020 03.
Article in English | MEDLINE | ID: mdl-31960264

ABSTRACT

Human αB-crystallin (HSPB5) is frequently modified post-translationally by UV radiation, oxidation, and age-associated processes, which complicates functional analyses of the protein using natural sources. Thus, determining the biological function of HSPB5 at the molecular structure level requires unmodified protein. Here, we employed an Escherichia coli cell-free protein synthesis system to prepare unmodified, functionally active human HSPB5. An S30 extract prepared from E. coli strain BL21 (DE3) was used for HSPB5 synthesis. The efficacy of protein synthesis was assessed by monitoring influencing factors, such as the concentrations of Mg2+ and other reaction mixture constituents, and by evaluating batch and/or dialysis synthesis systems. Chaperone-like activity of synthesized HSPB5 was assayed using alcohol dehydrogenase (ADH) under thermal stress. The amount of HSPB5 synthesized using the cell-free system depended significantly on the concentration of Mg2+ in the reaction mixture. Use of condensed S30 extract and increased levels of amino acids promoted HSPB5 production. Compared with the batch system, HSPB5 synthesis was markedly increased using the dialysis system. The construction vector played a critical role in regulating the efficacy of protein synthesis. HSPB5 synthesized using the cell-free system had a native molecular mass, as determined by mass spectrometry analysis. The co-presence of synthesized HSPB5 suppressed heat-associated denaturation of ADH. Human HSPB5 synthesized using the cell-free system thus retains functional activity as a molecular chaperone.


Subject(s)
Cell-Free System , alpha-Crystallin B Chain/biosynthesis , Escherichia coli
4.
Int Immunopharmacol ; 24(2): 267-275, 2015 Feb.
Article in English | MEDLINE | ID: mdl-25533502

ABSTRACT

Butein (3,4,2',4'-tetrahydroxychalcone), a flavonoid derivative, has been reported to show several biological actions, including anti-inflammatory and anti-cancer. However, the possible molecular mechanisms involved are poorly understood. Treatment of human umbilical vein endothelial cells (HUVECs) with butein significantly inhibited cell surface intercellular adhesion molecule-1 (ICAM-1) expression, ICAM-1 protein synthesis, and mRNA expression induced by tumor necrotic factor-α (TNF-α) and/or phorbol 12-myristate 13-acetate (PMA). Electrophoretic mobility shift assay revealed that butein blocked activation of transcription factors, nuclear factor-κB (NF-κB) and activator protein-1 (AP-1), induced by TNF-α and PMA. Moreover, butein abolished TNF-α- and PMA-induced IκBα phosphorylation, which participates in NF-κB activation, and PMA-induced phosphorylation of c-Jun, a subunit composed of AP-1. In vitro, butein inhibited the phosphorylation of c-Jun, binding to GST beads, mediated by JNK isolated from PMA-treated cells. The inhibitory action of butein on the JNK-mediated in vitro c-Jun phosphorylation was abrogated in the presence of ATP. These results indicate that in HUVECs, butein suppresses the expression of ICAM-1 mRNA and protein through the inhibition of the activation of NF-κB and AP-1 induced by TNF-α and PMA, that the inhibitory action of butein on NF-κB activation results from the inhibition of IκBα phosphorylation by IκB kinase (IKK), and that the inactivation of PMA-activated AP-1 by butein is due to the blocking of JNK-mediated c-Jun phosphorylation through the inhibition of ATP binding.


Subject(s)
Anti-Inflammatory Agents/pharmacology , Chalcones/pharmacology , Endothelial Cells/drug effects , Intercellular Adhesion Molecule-1/metabolism , Proto-Oncogene Proteins c-jun/metabolism , Cells, Cultured , Endothelial Cells/physiology , Gene Expression Regulation/drug effects , Humans , I-kappa B Proteins/metabolism , Immunosuppression Therapy , Intercellular Adhesion Molecule-1/genetics , Phosphorylation/drug effects , Proto-Oncogene Proteins c-jun/genetics , Tetradecanoylphorbol Acetate/analogs & derivatives , Tetradecanoylphorbol Acetate/immunology , Transcription Factor AP-1/metabolism , Tumor Necrosis Factor-alpha/immunology , Umbilical Cord/cytology
5.
J Immunol ; 184(9): 5253-62, 2010 May 01.
Article in English | MEDLINE | ID: mdl-20368270

ABSTRACT

MCP1 is upregulated by various stimuli, including LPS, high glucose, and hyperosmolality. However, the molecular mechanisms of transcriptional regulation of the MCP1 gene under hyperosmolar conditions are poorly understood. Treatment of NRK52E cells with NaCl or mannitol resulted in significant elevation of MCP1 mRNA and protein in a time- and dose-dependent manner. Treatment with a p38MAPK inhibitor (SB203580), an ERK inhibitor (PD98059), or an MEK inhibitor (U0126), suppressed the increase in MCP1 expression caused by hypertonic NaCl, whereas a JNK inhibitor (SP600125) and an AP1 inhibitor (curcumin) failed to attenuate MCP1 mRNA expression by NaCl. In the 5'-flanking region of the MCP1 gene, there is a sequence motif similar to the consensus TonE/ORE as well as the consensus C/E binding protein (BP), NF-kappaB, and AP1/Sp1 sites. Luciferase activity in cells transfected with reporter constructs containing a putative TonE/ORE element (MCP1-TonE/ORE) enhanced reporter gene expression under hypertonic stress. Results of electrophoretic gel mobility shift assay showed a slow migration of the MCP1-TonE/ORE probe, representing the binding of TonEBP/OREBP/NFAT5 to this enhancer element. These results indicate that the 5'-flanking region of MCP1 contains a hypertonicity-sensitive cis-acting element, MCP1-TonE/ORE, as a novel element in the MCP1 gene. Furthermore, p38MAPK and MEK-ERK pathways appear to be, at least in part, involved in hypertonic stress-mediated regulation of MCP1 expression through the MCP1-TonE/ORE.


Subject(s)
Chemokine CCL2/genetics , Enhancer Elements, Genetic/immunology , MAP Kinase Signaling System/genetics , MAP Kinase Signaling System/immunology , Transcription Factors/physiology , 5' Untranslated Regions/immunology , Animals , Cell Line , Chemokine CCL2/biosynthesis , Consensus Sequence/immunology , Enhancer Elements, Genetic/genetics , Gene Expression Regulation, Enzymologic/immunology , Hypertonic Solutions/pharmacology , Male , Mitogen-Activated Protein Kinase 1/genetics , Mitogen-Activated Protein Kinase 1/physiology , Mitogen-Activated Protein Kinase 3/genetics , Mitogen-Activated Protein Kinase 3/physiology , NFATC Transcription Factors/metabolism , Osmolar Concentration , Rats , Rats, Sprague-Dawley , Transcription Factors/metabolism , p38 Mitogen-Activated Protein Kinases/genetics , p38 Mitogen-Activated Protein Kinases/physiology
6.
Biol Pharm Bull ; 33(2): 223-9, 2010.
Article in English | MEDLINE | ID: mdl-20118544

ABSTRACT

The present study was designed to clarify the effects of an ethanol extract of artichoke leaf on acute gastric mucosal injury in rats. Oral administration of artichoke leaf extract dose-dependently prevented absolute ethanol-induced (125-500 mg/kg) or restraint plus water immersion stress-induced gastric mucosal injury (1000-2000 mg/kg). The artichoke leaf extract contains 1% cynaropicrin and 0.8% chlorogenic acid as main components and 70% dextrin as a vehicle. Cynaropicrin at doses of 1/100 of artichoke leaf extract [ethanol-induced mucosal injury: 5 mg/kg, per os (p.o.); stress-induced mucosal injury: 20 mg/kg, p.o.] also prevented gastric mucosal injury in both animal models. However, dextrin and chlorogenic acid at doses contained in the leaf extract were ineffective in both models. When artichoke leaf extract was given orally to normal rats, it (500-2000 mg/kg, p.o.) dose-dependently increased gastric mucus content. In addition, it (125-500 mg/kg, p.o.) dose-dependently prevented the decrease in gastric mucus content by absolute ethanol. When the effects of artichoke leaf extract on basal gastric acid secretion in rats were evaluated, it (500-2000 mg/kg, p.o.) dose-dependently increased the volume of gastric juice in normal rats. However, it was ineffective in decreasing basal gastric acid secretion in normal rats. These results indicate that artichoke leaf extract is effective against acute gastritis and its beneficial effect is due to that of cynaropicrin. The gastric mucus-increasing action of artichoke leaf extract may be, at least in part, related to the anti-gastritic action of the extract.


Subject(s)
Anti-Ulcer Agents/therapeutic use , Cynara scolymus , Gastric Mucosa/drug effects , Phytotherapy/methods , Plant Extracts/therapeutic use , Acute Disease , Animals , Anti-Ulcer Agents/isolation & purification , Cynara scolymus/chemistry , Cynara scolymus/physiology , Gastric Juice/drug effects , Gastric Juice/metabolism , Gastric Mucosa/metabolism , Gastric Mucosa/pathology , Gastritis/drug therapy , Gastritis/pathology , Male , Plant Extracts/isolation & purification , Plant Leaves , Rats , Rats, Sprague-Dawley
7.
Eur J Pharmacol ; 601(1-3): 143-7, 2008 Dec 28.
Article in English | MEDLINE | ID: mdl-18955044

ABSTRACT

In the present study, we compared the effects of alpha-tocopherol and probucol, antioxidants, on the healing of acetic acid-induced gastric ulcers in 8-, 48- and 96-week-old rats. The repeated oral administration of alpha-tocopherol (16 mg/kg twice daily) and probucol (1000 mg/kg twice daily) for 14 consecutive days markedly accelerated the gastric ulcer healing in 48- and 96-week-old rats as well as 8-week-old ones. The ulcer healing effects of both drugs were not significantly different among the rats at three different ages. The superoxide dismutase (SOD) activity in the ulcerated region of 8-, 48- and 96-week-old rats was markedly lower than that in the unulcerated region. In contrast, the thiobarbituric acid (TBA)-reactive substance content, an index of lipid peroxidation, in the ulcerated region of rats at three different ages markedly increased, as compared to that in the unulcerated region. The SOD activity tended to decrease with aging, while the TBA-reactive substance content gradually increased. The repeated administration of alpha-tocopherol and probucol accelerated the ulcer healing and inhibited the increase in the TBA-reactive substance content in the ulcerated region. These results suggest that alpha-tocopherol and probucol promote the ulcer healing by their potent antioxidant activities in 48- and 96-week-old rats as well as 8-week-old rats.


Subject(s)
Antioxidants/pharmacology , Probucol/pharmacology , Stomach Ulcer/drug therapy , alpha-Tocopherol/pharmacology , Acetic Acid , Administration, Oral , Aging , Animals , Anti-Ulcer Agents/pharmacology , Disease Models, Animal , Lipid Peroxidation/drug effects , Male , Rats , Rats, Wistar , Stomach Ulcer/physiopathology , Superoxide Dismutase/drug effects , Superoxide Dismutase/metabolism , Thiobarbituric Acid Reactive Substances/metabolism
8.
J Clin Immunol ; 27(4): 409-29, 2007 Jul.
Article in English | MEDLINE | ID: mdl-17516154

ABSTRACT

We investigated participation of monocyte chemoattractant protein-1 (MCP-1) in tubulointerstitial fibrosis and correlation between MCP-1 and proteinuria in Wistar-Kyoto (WKY) rats with glomerulonephritis induced by anti-glomerular basement membrane (anti-GBM) antibody. WKY rats showed marked proteinuria and severe glomerular crescent formation at 7 days post antibody injection. At 28 days, tubulointerstitial fibrotic lesions were observed, followed by sustained heavy proteinuria and severe tubulointerstitial fibrosis at 56 days. Histological examination revealed that the overlapped immunoreactivities of MCP-1, rat albumin, and p65NF-kappaB were detected in the same tubular segments of nephritic kidney, and a significant positive correlation was observed between proteinuria and MCP-1 expression in the tubulointerstitial fibrosis. ED-1- and CD8-positive cells were also abundant, and there was a good correlation between monocyte/macrophage recruitment and MCP-1 expression in the tubulointerstitial area. These results suggest that MCP-1 participates in the progression of tubulointerstitial fibrosis, through massive albuminuria, which is accompanied by marked monocyte/macrophage recruitment.


Subject(s)
Anti-Glomerular Basement Membrane Disease/immunology , Chemokine CCL2/immunology , Kidney/immunology , Nephritis, Interstitial/immunology , Proteinuria/immunology , Animals , Anti-Glomerular Basement Membrane Disease/chemically induced , Chemokine CCL2/genetics , Chemokine CCL2/urine , Creatinine/blood , Creatinine/urine , Disease Models, Animal , Disease Progression , Fibrosis/chemically induced , Fibrosis/immunology , Fibrosis/pathology , Gene Expression Regulation , Kidney/chemistry , Kidney/pathology , Male , Nephritis, Interstitial/chemically induced , Proteinuria/chemically induced , Proteinuria/urine , Rats , Rats, Inbred Lew , Rats, Inbred WKY , Rats, Wistar , Species Specificity , Transforming Growth Factor beta/genetics , Transforming Growth Factor beta/metabolism
9.
Biol Pharm Bull ; 29(11): 2206-13, 2006 Nov.
Article in English | MEDLINE | ID: mdl-17077516

ABSTRACT

Oral administration of tea catechin dose-dependently prevented absolute ethanol-induced (50, 100, 200 mg/kg) or restraint plus water immersion stress-induced acute gastric mucosal injury (300, 400 mg/kg) in rats. When the effect of test compound was evaluated on the 15th day after acetic acid injection to rats, repeated oral administration of tea catechin (25, 50, 100 mg/kg twice daily) dose-dependently accelerated the healing of acetic acid-induced chronic gastric ulcers. Tea catechin (10(-5)-10(-1) g/100 ml) concentration-dependently scavenged superoxide anions in vitro. Tea catechin (100, 200 mg/kg orally) markedly inhibited the increase in thiobarbituric acid-reactive substances in the injured mucosa of rats treated with 50% ethanol. Tea catechin (50, 100 mg/kg twice orally, daily) markedly inhibited the increase in content of thiobarbituric acid-reactive substances in the ulcerated region of acetic acid-induced gastric ulcers on the 7th and 15th days. In addition, at 50, 100 and 200 mg/kg orally, it dose-dependently prevented the decrease in gastric mucosal hexosamine content induced by absolute ethanol, although it failed to inhibit the basal gastric acid secretion. These results suggest that tea catechin may primarily protect gastric mucosa from acute gastric mucosal injury and promote the healing of chronic gastric ulcers by its antioxidant activity and gastric mucus-increasing actions.


Subject(s)
Anti-Ulcer Agents/therapeutic use , Camellia sinensis/chemistry , Catechin/therapeutic use , Stomach Ulcer/prevention & control , Tea/chemistry , Acetic Acid/administration & dosage , Acetic Acid/toxicity , Administration, Oral , Animals , Anti-Ulcer Agents/administration & dosage , Anti-Ulcer Agents/chemistry , Catechin/administration & dosage , Catechin/chemistry , Dose-Response Relationship, Drug , Ethanol/administration & dosage , Ethanol/toxicity , Free Radical Scavengers/antagonists & inhibitors , Free Radical Scavengers/metabolism , Gastric Acid/metabolism , Gastric Mucosa/drug effects , Gastric Mucosa/metabolism , Gastric Mucosa/pathology , Hexosamines/metabolism , Immersion/adverse effects , Male , Molecular Structure , Omeprazole/administration & dosage , Omeprazole/therapeutic use , Phytotherapy/methods , Rats , Rats, Sprague-Dawley , Reactive Oxygen Species/antagonists & inhibitors , Reactive Oxygen Species/metabolism , Restraint, Physical/adverse effects , Restraint, Physical/methods , Stomach Ulcer/chemically induced , Stomach Ulcer/metabolism , Sucralfate/administration & dosage , Sucralfate/therapeutic use , Thiobarbituric Acid Reactive Substances/metabolism
10.
J Am Soc Nephrol ; 17(3): 674-85, 2006 Mar.
Article in English | MEDLINE | ID: mdl-16452498

ABSTRACT

N-acetyl-seryl-aspartyl-lysyl-proline (Ac-SDKP), which is hydrolyzed by angiotensin-converting enzyme, is a natural regulator of hematopoiesis. Here it is shown that Ac-SDKP inhibits TGF-beta action in mesangial cells. Because TGF-beta is thought to play a pivotal role in the development and progression of glomerulonephritis, the therapeutic effects of Ac-SDKP on an established model of renal dysfunction and histologic alteration in Wistar-Kyoto rats with anti-glomerular basement membrane nephritis was examined. Fourteen days after the induction of anti-glomerular basement membrane nephritis, the rats were treated subcutaneously with Ac-SDKP at a dose of 1 mg/kg per d for 4 wk. Treatment with Ac-SDKP significantly improved proteinuria and renal dysfunction, including increased plasma blood urea nitrogen and creatinine levels and decreased creatinine clearance. Histologic examination showed severe glomerulosclerosis and interstitial fibrosis in the vehicle-treated rats, whereas these histologic injuries were significantly ameliorated in rats that were treated with Ac-SDKP. The histologic improvements were accompanied by the suppression of gene and protein expression of fibronectin, interstitial collagen, and TGF-beta1 in the nephritic kidney. Furthermore, treatment with Ac-SDKP resulted in the inhibition of Smad2 phosphorylation, an increase in Smad7 expression in the kidney, and reduction of macrophage accumulation into the glomeruli and tubulointerstitium in nephritic rats. In conclusion, Ac-SDKP significantly ameliorated the progression of renal dysfunction and fibrosis even after the establishment of nephritis. The inhibitory effect of Ac-SDKP was mediated in part by the inhibition of TGF-beta/Smad signal transduction and the inflammatory response. These findings suggest that Ac-SDKP treatment may be a novel and useful therapeutic strategy for the treatment of progressive renal diseases.


Subject(s)
Anti-Glomerular Basement Membrane Disease/drug therapy , Anti-Glomerular Basement Membrane Disease/pathology , Fibrosis/pathology , Oligopeptides/pharmacology , Transforming Growth Factor beta/metabolism , Analysis of Variance , Animals , Biopsy, Needle , Blood Chemical Analysis , Blotting, Western , Disease Models, Animal , Disease Progression , Dose-Response Relationship, Drug , Drug Administration Schedule , Immunohistochemistry , Injections, Subcutaneous , Kidney Function Tests , Male , Oligopeptides/pharmacokinetics , Probability , Random Allocation , Rats , Rats, Inbred WKY , Reverse Transcriptase Polymerase Chain Reaction , Sensitivity and Specificity , Statistics, Nonparametric , Transforming Growth Factor beta/drug effects , Urinalysis
11.
Biochem J ; 380(Pt 3): 783-94, 2004 Jun 15.
Article in English | MEDLINE | ID: mdl-15018608

ABSTRACT

Osp94 (osmotic stress protein of 94 kDa) is known to be up-regulated by hypertonic and heat-shock stresses in mouse renal inner medullary collecting duct (mIMCD3) cells. To investigate the molecular mechanism of transcriptional regulation of the Osp94 gene under these stresses, we cloned and characterized the 5'-flanking region of the gene. Sequence analysis of the proximal 4 kb 5'-flanking region revealed a TATA-less G/C-rich promoter region containing a cluster of Sp1 sites. We also identified upstream sequence motifs similar to the consensus TonE/ORE (tonicity-response element/osmotic response element) as well as the consensus HSE (heat-shock element). Luciferase activities in cells transfected with reporter constructs containing a TonE/ORE-like element (Osp94-TonE; 5'-TGGAAAGGACCAG-3') and HSE enhanced reporter gene expression under hypertonic stress and heat-shock stress respectively. Electrophoretic gel mobility-shift assay showed a slowly migrating band binding to the Osp94-TonE probe, probably representing binding of TonEBP (TonE binding protein) to this enhancer element. Furthermore, treatment of mIMCD3 cells with MAPK (mitogen-activated protein kinase) inhibitors (SB203580, PD98059, U0126 and SP600125) and a proteasome inhibitor (MG132) suppressed the increase in Osp94 gene expression caused by hypertonic NaCl. These results indicate that the 5'-flanking region of Osp94 gene contains a hypertonicity sensitive cis -acting element, Osp94-TonE, which is distinct from a functional HSE. Furthermore, the MAPK and proteasome systems appear to be, at least in part, involved in hypertonic-stressmediated regulation of Osp94 through Osp94-TonE.


Subject(s)
Gene Expression Regulation/genetics , HSP70 Heat-Shock Proteins/genetics , 5' Flanking Region/genetics , Amino Acid Sequence , Animals , Base Sequence , Cell Line , Enhancer Elements, Genetic/genetics , Heat-Shock Response/genetics , Hot Temperature/adverse effects , Hypertonic Solutions/adverse effects , Mice , Molecular Sequence Data , Signal Transduction/genetics , Trans-Activators/genetics
12.
J Am Soc Nephrol ; 13(4): 848-857, 2002 Apr.
Article in English | MEDLINE | ID: mdl-11912243

ABSTRACT

Recently, a family of multispecific organic anion transporters has been identified, and several isoforms have been reported. However, the physiologic and pharmacologic roles of each isoform, except OAT1, in the transepithelial transport of organic anions in the kidney remain to be elucidated. To address this issue, it is essential to determine the intrarenal distribution and membrane localization of each OAT isoform along the nephron. In this study, the intrarenal distributions of rOAT1, rOAT2, and rOAT3 were investigated by an immunofluorescence method that used frozen rat serial kidney sections. Confocal microscopic analysis showed that immunoreactivity for rOAT1 was detected exclusively in the proximal tubules (S1, S2, S3) in the cortex with basolateral membrane staining. rOAT2 was detected in the apical surface of the tubules in the medullary thick ascending limb of Henle's loop (MTAL) and cortical and medullary collecting ducts (CD). rOAT3 was localized in the basolateral digitation of the cell membrane in all the segments (S1, S2, and S3) of the proximal tubules, MTAL, cortical TAL, connecting tubules, and cortical and medullary CD. These results on the distribution of each OAT isoform will facilitate the understanding of the role of OATs in the renal processing of organic anions.


Subject(s)
Kidney/metabolism , Organic Anion Transport Protein 1/metabolism , Organic Anion Transporters, Sodium-Independent/metabolism , Animals , Blotting, Northern , Blotting, Western , Fluorescent Antibody Technique , Immunohistochemistry , Kidney Tubules/metabolism , Kidney Tubules, Collecting/metabolism , Kidney Tubules, Proximal/metabolism , Male , Organic Anion Transport Protein 1/genetics , Organic Anion Transporters, Sodium-Independent/genetics , RNA, Messenger/metabolism , Rats , Rats, Sprague-Dawley , Tissue Distribution
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