Early Increase of Chondroitin Sulfate Glycosaminoglycan in the Glomerular Basement Membrane of Rats with Diabetic Glomerulopathy

Nephron ◽  
1997 ◽  
Vol 76 (1) ◽  
pp. 62-71 ◽  
Author(s):  
R. Karasawa ◽  
S. Nishi ◽  
Y. Suzuki ◽  
N. Imai ◽  
M. Arakawa
Keyword(s):  
Basement Membrane ◽  
Chondroitin Sulfate ◽  
Glomerular Basement Membrane ◽  
Diabetic Glomerulopathy ◽  
Early Increase

scholarly journals Partial characterization of newly synthesized proteoglycans isolated from the glomerular basement membrane.

1981 ◽  
Vol 90 (2) ◽  
pp. 527-532 ◽  
Author(s):  
Y S Kanwar ◽  
V C Hascall ◽  
M G Farquhar
Keyword(s):  
Basement Membrane ◽  
Heparan Sulfate ◽  
Chondroitin Sulfate ◽  
Density Gradient ◽  
Glomerular Basement Membrane ◽  
Chromatographic Behavior ◽  
Acid Oxidation ◽  
Sulfate Proteoglycan ◽  
Cartilage Proteoglycan ◽  
Core Proteins

Kidneys were perfused with [35S]sulfate at 4 h in vitro to radiolabel sulfated proteoglycans. Glomeruli were isolated from the labeled kidneys, and purified fractions of glomerular basement membrane (GBM) were prepared therefrom. Proteoglycans were extracted from GBM fractions by use of 4 M guanidine-HCl at 4 degrees C in the presence of protease inhibitors. The efficiency of extraction was approximately 55% based on 35S radioactivity. The extracted proteoglycans were characterized by gel-filtration chromatography (before and after degradative treatments) and by their behavior in dissociative CsCl gradients. A single peak of proteoglycans with an Mr of 130,000 (based on cartilage proteoglycan standards) was obtained on Sepharose CL-4B or CL-6B. Approximately 85% of the total proteoglycans were susceptible to nitrous acid oxidation (which degrades heparan sulfates), and approximately 15% were susceptible to digestion with chondroitinase ABC (degrades chondroitin-4 and -6 sulfates and dermatan sulfate). The released glycosaminoglycan (GAG) chains had an Mr of approximately 26,000. Density gradient centrifugation resulted in the partial separation of the extracted proteoglycans into two types with different densities: a heparan sulfate proteoglycan that was enriched in the heavier fraction (p greater than 1.43 g/ml), and a chondroitin sulfate proteoglycan that was concentrated in the lighter fractions (p less than 1.41). The results indicate that two types of proteoglycans are synthesized and incorporated into the GBM that are similar in size and consist of four to five GAG chains (based on cartilage proteoglycan standards). The chromatographic behavior of the extracted proteoglycans and the derived GAG, together with the fact that the two types of proteoglycans can be partially separated into the density gradient, suggest that the heparan sulfate and chondroitin sulfate(s) are located on different core proteins.

Electron microscopic radioautographic studies on the incorporation of 3H proline in the glomerular basement membrane (GBM) in antistreptococcal-cell-membrane (SCM) injected mice

1984 ◽  
Vol 42 ◽  
pp. 188-189
Author(s):  
R.P. Nayyar ◽  
C.F. Lange ◽  
J. L. Borke
Keyword(s):  
Body Weight ◽  
Cell Membrane ◽  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Mesangial Matrix ◽  
Electron Microscopic ◽  
Group A ◽  
Injection Protocol

Streptococcal cell membrane (SCM) antiserum injected mice show a significant thickening of glomerular basement membrane (GBM) and an increase in mesangial matrix within 4 to 24 hours of antiserum administration (1,2,3). This study was undertaken to evaluate the incorporation of 3H proline into glomerular cells and GBM under normal and anti-SCM induced conditions. Mice were administered, intraperitoneally, 0.1 ml of normal or anti-SCM serum followed by a 10 µC/g body weight injection of 3H proline. Details of the preparation of anti-SCM (Group A type 12 streptococcal pyogenes) and other sera and injection protocol have been described elsewhere (2). After 15 minutes of isotope injection a chase of cold proline was given and animal sacrificed at 20 minutes, 1,2,4,8,24 and 48 hours. One of the removed kidneys was processed for immunofluorescence, light and electron microscopic radioautographic studies; second kidney was used for GBM isolation and aminoacid analysis.

Fibronectin binding to glomerular basement membrane is altered in diabetes

Diabetes ◽  
1987 ◽  
Vol 36 (6) ◽  
pp. 758-763 ◽  
Author(s):  
M. P. Cohen ◽  
R. Saini ◽  
H. Klepser ◽  
L. G. Vasanthi
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Fibronectin Binding

Removal of elevated circulating angiopoietin-2 by plasma exchange – A pilot study in critically ill patients with thrombotic microangiopathy and anti-glomerular basement membrane disease

2010 ◽  
Vol 104 (11) ◽  
pp. 1038-1043 ◽  
Author(s):  
Carsten Hafer ◽  
Jan Kielstein ◽  
Marion Haubitz ◽  
Hermann Haller ◽  
Svjetlana Lovric ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Plasma Exchange ◽  
Critically Ill ◽  
Glomerular Basement Membrane ◽  
Critically Ill Patients ◽  
Plasma Levels ◽  
Vascular Inflammation ◽  
Endothelial Damage ◽  
Healthy Controls ◽  
Angiopoietin 2

SummaryIn critically ill patients, the massive release of angiopoietin-2 (Ang-2) from Weibel-Palade bodies interferes with protective angiopoietin-1 (Ang-1)/Tie2 signalling in endothelial cells, thus leading to vascular inflammation and subsequent organ-dysfunction. We hypothesised that plasma exchange (PE) is efficient for lowering excess Ang-2 levels in critically ill patients with thrombocytic microangiopathy (TMA) or anti-glomerular basement membrane (anti-GBM) disease. Plasma Ang-1 and Ang-2 were measured by immuno-luminometric assays in patients with TMA (n=9) or anti-GBM disease (n=4) before and after up to four PE sessions. Twenty apparently healthy volunteers served as controls. Median (IQR) plasma levels of Ang-2 were markedly increased in patients with TMA (7.3 (2.4–21.1) ng/ml) and anti-GBM disease (5.8 (3.4–7.0) ng/ml) compared to healthy controls (1.0 (0.9–1.4) ng/ml, p <0.001). Moreover, Ang-1 plasma levels were decreased in both, TMA (1.02 (0.62–1.62) ng/ml) and anti-GBM disease patients (0.74 (0.59–3.62) ng/ml) compared to healthy controls (2.5 (1.93–3.47) ng/ ml, p <0.005). During a total of 32 treatments, PE effectively lowered elevated mean (SD) Ang-2 plasma levels by 36.7 ± 19.6 % per treatment (p <0.0001), whereas low Ang-1 plasma levels remained unchanged (0.3 ± 58.5 %; p =0.147). Ang-2 levels declined to almost normal values during ≤4 PE treatments (Friedman´s test p <0.0001). PE is an effective method to remove excess circulating Ang-2. It remains to be elucidated if the removal of Ang-2 is crucial to ameliorate endothelial damage in critically ill patients with severely altered endothelial integrity.

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