Animals ; Biopsy ; Disease Models, Animal ; Fluorescent Antibody Technique ; Glomerulonephritis, Membranoproliferative ; pathology ; Humans ; Kidney ; pathology ; Kidney Diseases ; pathology ; Plastic Embedding

Biopsy, Needle ; methods ; China ; Humans ; Kidney ; pathology ; Kidney Diseases ; pathology ; Kidney Neoplasms ; pathology ; Specimen Handling

Carcinoma, Renal Cell ; classification ; genetics ; pathology ; Humans ; Kidney Neoplasms ; classification ; genetics ; pathology ; World Health Organization

Biopsy ; methods ; Glomerulonephritis, IGA ; pathology ; Humans ; Kidney ; pathology ; Kidney Diseases ; pathology ; Lupus Nephritis ; pathology

Humans ; Immunoglobulin Light Chains ; genetics ; immunology ; Immunoglobulin kappa-Chains ; genetics ; immunology ; Kidney ; immunology ; metabolism ; pathology ; Kidney Diseases ; immunology ; pathology ; therapy ; Mutation ; Transforming Growth Factor beta ; metabolism

Aristolochic Acids ; adverse effects ; Child ; Drugs, Chinese Herbal ; adverse effects ; Female ; Humans ; Male ; Nephrosis ; chemically induced

Aged ; Diagnosis, Differential ; Fibronectins ; metabolism ; Glomerulonephritis, Membranoproliferative ; pathology ; Humans ; Immunohistochemistry ; Kidney Diseases ; metabolism ; pathology ; Kidney Glomerulus ; metabolism ; pathology ; ultrastructure ; Male ; Microscopy, Electron

OBJECTIVETo observe the transdifferentiation of renal tubular epithelial cells in tubulointerstitial fibrosis.

METHODSThe renal tubulointerstitial fibrosis model in Wistar rats was established by unilateral renal vein ligature. The rats were kept 25 days after renal vein ligature. The kidneys were dissected every 5 days by killing 5 rats. The morphological changes of the kidney were observed by light microscopy, electron microscopy, polarizing microscopy and immunohistochemistry method.

RESULTSThe histological changes showed tubular atrophy and disappearance, widening of intertubular spaces with increased lymphocytes and mononuclear cells infiltration and fibrosis. The CK marker in injured and atrophic epithelial cells gradually weakened, but the alpha-SMA, vimentin, TGF-beta(1), collagen I and III showed gradually stronger positivity for immunohistochemistry. Some interstitial cells became positive for CK. Electron microscopy revealed decreased mitochondria, increased endoplasmic reticulum and microfilament of the tubular epithelial cells which merged into the interstitium. During the early stage of tubulointerstitial fibrosis, there was proliferation of type III collagen and then followed by type I collagen at later stage when observing the Sirius Red stained sections under the polarizing microscope.

CONCLUSIONTubular epithelial cells can transdifferentiate to fibroblasts during the process of tubulointerstitial fibrosis.

Actins ; analysis ; Animals ; Cell Differentiation ; Collagen ; analysis ; Epithelial Cells ; cytology ; Fibrosis ; Immunohistochemistry ; Keratins ; analysis ; Kidney Tubules ; chemistry ; pathology ; ultrastructure ; Male ; Rats ; Rats, Wistar

Adult ; Biopsy, Needle ; Diagnosis, Differential ; Humans ; Kidney ; pathology ; Kidney Diseases ; pathology ; therapy ; Male ; Nephritis, Interstitial ; pathology ; Renal Dialysis ; Sarcoidosis ; pathology ; therapy ; Tuberculosis, Renal ; pathology

OBJECTIVETo clarify the regulation of p53 through telomere pathway by investigating the molecular interaction between p53 and the main telomere-associated protein Telomeric Repeat Factor 2 (TRF2) in vitro.

METHODSFour different p53-GST (glutathione S-transferase) fusion proteins and GST were expressed in E. coli and purified through glutathione sepharose 4B beads. The human recombinant p53s included wild type p53 (1-393), N terminus-truncated form p53 2C (95-393), C terminus-truncated form p53 N5 (2-293) and single amino acid mutant p53 R175H (175 arginine to histidine). Purified p53-GST fusion proteins and GST were mixed with cellular protein extracts of human breast cancer cells MCF-7 in vitro by pull down. The molecular interaction between p53 and TRF2 were detected by Western blot.

RESULTSSDS-PAGE and Coomassie brilliant blue staining showed that the molecular weights of all purified proteins were as expected, with purities over 90%. Western blot of TRF2 indicated that both wild type p53 and p53 R175H could bind with TRF2 of MCF-7 cells in similar capacity, while GST alone failed to do so. The molecular interaction between p53 2C and TRF2 was enhanced. In contrast, the interaction between p53 N5 and TRF2 was significantly reduced.

CONCLUSIONSp53 can interact with TRF2 directly and specifically in vitro, with C terminus of p53 (293-393) being the binding region for their interaction. This C terminus-dependent interaction between p53 and TRF2 may be related to the cellular activities induced by telomere alterations.

Breast Neoplasms ; metabolism ; pathology ; Cell Line, Tumor ; DNA-Binding Proteins ; metabolism ; Escherichia coli ; genetics ; metabolism ; Female ; Glutathione Transferase ; genetics ; metabolism ; Humans ; Protein Binding ; Recombinant Fusion Proteins ; isolation & purification ; metabolism ; Telomeric Repeat Binding Protein 2 ; metabolism ; Transformation, Genetic ; Tumor Suppressor Protein p53 ; genetics ; metabolism