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    Changes in glomerular extracellular matrices components in diabetic nephropathy
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    Keywords:
    Type IV collagen
    Immunofluorescence
    Polyclonal antibodies
    Glomerulosclerosis
    Membranous Nephropathy
    A 38-year-old man presented with nephrotic syndrome and hypertension for five years.He had normal visual acuity and hearing,and denied hereditary nephropathy in his family.Renal biopsy showed non-typical membranous nephropathy by the light microscope and immunofluorescence.In addition,there were several unusual clusters of foam cells in the renal interstitial area.Type IV collagen staining showed that the expression of the alpha3 was faint in the GBM(glomerular basement membrane) and normal in TBM(tubular basement membrane).Electron microscope indicated the splitting of the lamina densa of GBM,and subepithelial electron dense deposits.The final diagnosis was Alport syndrome associated with membranous nephropathy.
    Lamina densa
    Membranous Nephropathy
    Alport syndrome
    Type IV collagen
    Immunofluorescence
    Citations (0)
    Immunofluorescent distribution of basement membrane components laminin and collagen type IV was studied in 51 rat colon tumors induced by 1, 2-dimethylhydrazine. In normal colonic mucosa, adenomas and carcinomas in situ continuous basement membranes were present, while in adenocarcinomas they were altered to different extents. An uncoordinated loss, or dissociation, of the two markers studied was found: the degree of collagen type IV loss was often much higher than that of laminin in the same tumor. These data suggest that a reliable determination of cancer invasion by monitoring basement membrane alteration requires the use of several basement membrane markers.
    1,2-Dimethylhydrazine
    Type IV collagen
    Citations (9)
    Distribution of type IV collagen and laminin in the gingival capillary basement membrane from streptozotocin-induced diabetic rats was investigated using immunoelectron microscopy. Both type IV collagen and laminin were found throughout the basement membrane. Quantitative analysis revealed that the immunoreactive area for laminin did not change with age, and the width of laminin deposition remained constant, even when diabetes was induced in the animals. However, the immunoreactive area for type IV collagen thickened with age. Further, the width of type IV collagen in the basement membrane increased markedly 36 weeks after diabetes was induced. It was concluded that the thickening of the gingival capillary basement membrane in experimentally induced diabetic rats was due an increase of type IV collagen deposition.
    Type IV collagen
    Immunoelectron microscopy
    Lamina densa
    Citations (3)
    Abstract. Kidneys from mice, dogs, and humans with X-linked and autosomal-recessive forms of Alport syndrome were examined by immunofluorescence for expression of laminin α, β, and γ chains using monospecific antibodies. Laminin α2 chain was absent from glomerular basement membranes (GBM) in normal human, murine, and canine kidneys but was abnormally deposited in Alport GBM, regardless of species or inheritance pattern. In murine and canine Alport kidneys, laminin α2 seems to be deposited as part of both laminin-2 (α2β1γ1) and laminin-4 (α2β2γ1) but as part of only laminin-4 in human Alport kidneys. GBM laminin α2 chain deposition was not observed in a variety of non-Alport human glomerulopathies. This finding adds to the list of proteins that are aberrantly deposited in Alport GBM as a consequence of the absence of the α3, α4, and α5 chains of type IV collagen: ( 1 ) type IV collagen α1 and α2 chains, ( 2 ) type V collagen, ( 3 ) type VI collagen, and most recently ( 4 ) the laminin α2 chain and ( 5 ) the laminin α1 and β1 chains in mice and dogs. These findings emphasize further the critical role played by the α3, α4, and α5 chains of type IV collagen in establishing and maintaining the composition, structure, and function of mature GBM.
    Alport syndrome
    Type IV collagen
    Immunofluorescence
    Citations (85)
    Membranous nephropathy is a common primary glomerular disease.The pathological features is based on the deposition of immune complexes diffuse glomerular visceral epithelial cells and basement membrane thickening with spikes.Its pathogenesis is complicated.In recent years,the in-depth study of markers of podocytes confirmed that podocytes is closely related to the generation of abnormal proteinuria.This thesis overviewed the progress on podocyte abnormalities of membranous nephropathy development.
    Membranous Nephropathy
    Pathogenesis
    Citations (0)
    Human carcinomas of the pancreas are aggressive tumors which traverse basement membrane barriers during invasion and metastasis. In order to examine the relationship of pancreatic tumor cells to basement membranes, we analyzed and compared the capabilities of four biologically different human pancreatic adenocarcinoma lines to adhere to substrate coated with purified basement membrane constituents. Each of the four cell lines adhered readily to purified laminin in a dose-dependent manner, although differences were noted in the time required for optimum attachment. Significant variations in the abilities of the cell lines to attach to purified fibronectin were evident both in concentration dependence and in the time required for attachment and spreading. Adhesion to type IV collagen was negligible for two of the four tumor lines but addition of soluble laminin or fibronectin augmented attachment. The other two cell lines attached only moderately to type IV collagen and this attachment was not enhanced by soluble laminin or fibronectin. When laminin or fibronectin was coated directly over type IV collagen, attachment of all four cell lines was comparable to that for the glycoproteins alone. Although the tumor lines were all established from human neoplasms of similar histological origin and retained the ability to adhere to intact basement membranes prepared from human amnion, they exhibited various patterns of attachment to laminin, fibronectin, and type IV collagen.
    Type IV collagen
    Citations (9)