No abstract available.
Korea* ; Peritoneal Dialysis, Continuous Ambulatory*

No abstract available.
Peritoneal Dialysis*

No abstract available.
Humans* ; Insulin* ; Receptor, Insulin*

No abstract available.
Hepatitis B Surface Antigens* ; Interferons* ; Lymphocytes*

No abstract available.
Peritoneal Dialysis, Continuous Ambulatory* ; Peritonitis*

No abstract available.
Histamine* ; Pruritus*

A growing body of evidence indicates that epithelial-mesenchymal transition (EMT) of human peritoneal mesothelial cells (HPMC) may play an important role in the development and progression of peritoneal fibrosis during long-term peritoneal dialysis (PD) leading to failure of peritoneal membrane function. Here, we review our own observations and those of others on the mechanisms of EMT of HPMC and suggest potential therapeutic strategies to prevent EMT and peritoneal fibrosis during long-term PD. We found that high glucose and H2O2 as well as transforming growth factor-beta1 (TGF-beta1) induced EMT in HPMC and that high glucoseinduced EMT was blocked not only by inhibition of TGF-beta1 but also by antioxidants or inhibitors of mitogen-activated protein kinases (MAPK). Since MAPKs are downstream target molecules of reactive oxygen species (ROS), these data suggest that high glucose-induced generation of ROS and subsequent MAPK activation mediate high glucose-induced EMT in HPMC. We and others also observed that bone morphogenetic protein-7 (BMP-7) prevented EMT in HPMC. Glucose degradation products (GDP) were shown to play a role in inducing EMT. Involvement of a mammalian target of rapamycin (mTOR) in TGF-beta1-induced EMT has also been proposed in cultured HPMC. A better understanding of the precise mechanisms involved in EMT of HPMC may provide new therapeutic strategies for inhibiting peritoneal fibrosis in long-term PD patients.
Epithelial Cells/*pathology ; Fibrosis ; Humans ; Mesoderm/*pathology ; Peritoneal Dialysis/*adverse effects ; Peritoneum/*pathology

Cytomegalovirus (CMV) is a ubiquitous virus and its infections occur commonly after renal transplantation and immunosuppressive therapy. Early and accurate laboratory diagnosis of CMV infection in renal transplant is necessary but often difficult. To find optimal diagnostic methods for CMV infection, we compared shell vial culture and polymerase chain reaction (PCR) and Southern blot of PCR products. A total of 301 specimens of urine, blood neutrophils, tissues, or body fluids were obtained from 75 renal transplant recipients and were submitted to shell vial culture for CMV as well as DNA PCR using primers for immediate early(IE) gene of CMV. The human fibroblast cell line (MRC-5) was used to culture CMV and were examined with immunofluorescence staining using monoclonal antibody to the early antigen of CMV. The PCR products (274 and 379 bp) were detected by gel electrophoresis and ethidium bromide staining. When PCR products were not clearly visible on electrophoresis, PCR products were analyzed by Southern blot using IE gene probe. Sixty four(85.3%) of 75 renal transplant recipients showed CMV infection as analyzed by PCR and Southern blot as well as shell vial culture. On shell vial culture, CMV were detected in 81 specimens from 30(40%) renal transplant recipients in viremic state. On PCR and Southern blot analysis CMV were detected in 55 and 26 specimens, respectively from 59 patients. The sensitivity of culture and PCR to detect CMV infection were 42.4% and 83.3%, respectively. The results of two studies were concordant in 48%. PCR and Southern blot did not detect CMV in 10 and 5 culture proven CMV positive samples, respectively. Mutant CMV were found in 3 patients which showed 5-10 bp deletion in IE gene. Moreover, DNA sequencing analysis showed 5 mutant strains among 11 strains which appeared same by PCR prodcut. These results suggest that PCR followed by Southern blot may be more sensitive, but less specific than shell vial culture in the diagnosis of CMV disease. PCR followed by Southern blot may not detect mutant CMV. Combined analysis using both shell vial culture and PCR followed by Southern blot may be necessary to diagnose CMV infection in renal transplant recipients.
Blotting, Southern ; Body Fluids ; Cell Line ; Clinical Laboratory Techniques ; Cytomegalovirus Infections* ; Cytomegalovirus* ; Diagnosis ; DNA* ; Electrophoresis ; Ethidium ; Fibroblasts ; Fluorescent Antibody Technique ; Humans ; Kidney Transplantation ; Neutrophils ; Polymerase Chain Reaction ; Sequence Analysis, DNA ; Transplantation*

No abstract available.
Catheterization* ; Catheters* ; Edema* ; Subclavian Vein* ; Upper Extremity*

BACKGROUND: High glucose upregulates MCP-1 expression in rat glomerular mesangial cells and in human peritoneal mesothelial cells. However, the role of high glucose-induced MCP-1 on the development and progression of diabetic renal injury and peritoneal injury during peritoneal dialysis(PD) using high glucose PD solutions are not clear. Since MCP-1 was shown to upregulate transforming growth factor-beta1(TGF-beta1) and collagen expression in lung fibroblasts, the present study investigated the effects of MCP-1 on fibronectin secretion by mouse mesangial cells(MMC), human peritoneal mesothelial cells (HPMC), and human peritoneal fibroblasts(HPFB). METHODS: Synchronized cells were stimulated by different concentrations of MCP-1(0.1-100 ng/mL) or TGF-beta1(0.1-10 ng/mL) for 48 hours. Fibronectin protein secreted into the media was analyzed by Western blot analysis. RESULTS: MCP-1 up to 100 ng/mL did not affect fibronectin secretion by MMC. TGF-beta1 10 ng/mL, however, increased fibronectin secretion by MMC 2.8 fold that of control. MCP-1 up to 100 ng/mL did not affect fibronectin secretion by HPMC. But, TGF-beta1 0.1 ng/mL increased fibronectin secretion by HPMC 1.8 fold compared to control. On the other hand, MCP-1 increased fibronectin secretion by HPFB in a dose-dependent manner. MCP-1 at 1-10 ng/mL significantly increased fibronectin when compared to M199 control. 100 ng/mL MCP-1 further increased fibronectin secretion by HPFB compared to 0.1-10 ng/mL MCP-1. CONCLUSION: These results suggest a possible role for MCP-1 in the development and progression of peritoneal fibrosis and support the view that in addition to recruiting inflammatory cells MCP-1 may play a role in tissue fibrosis in other organs.
Animals ; Blotting, Western ; Chemokine CCL2* ; Collagen ; Fibroblasts* ; Fibronectins* ; Fibrosis ; Glucose ; Hand ; Humans* ; Lung ; Mesangial Cells ; Mice ; Monocytes* ; Peritoneal Fibrosis ; Rats ; Transforming Growth Factor beta1