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  • 1
    Electronic Resource
    Electronic Resource
    Increased expression of selectins in kidneys of patients with diabetic nephropathy (1998)
    Springer
    Diabetologia 41 (1998), S. 185-192 
    Details
    ISSN: 1432-0428
    Keywords: Keywords P-selectin ; E-selectin ; diabetic nephropathy ; advanced glycation endproducts ; macrophage.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary In diabetic nephropathy leukocytes, mainly composed of monocytes/macrophages, which accumulate in the glomeruli and the interstitium, play an important part in the progression of glomerulosclerosis. The infiltration of leukocytes into inflammatory tissues or atherosclerotic lesions is mediated by adhesion molecules, which are expressed on the vascular endothelial cells, although little is known about the mechanism of leukocyte infiltration into diabetic renal tissues. P- and E-selectin are leukocyte adhesion molecules, which are expressed on the vascular endothelial cells and promote the adhesion of leukocytes to the endothelium. We investigated the expression of P- and E-selectin in the kidney tissue of patients with diabetic nephropathy and compared it with that of patients with other glomerular diseases (minimal change nephrotic syndrome, membranous nephropathy, IgA nephropathy, mesangioproliferative glomerulonephritis, and lupus nephritis). Expression of P- and E-selectin were both significantly increased in the glomeruli and the interstitium of patients with diabetic nephropathy as compared with those with other glomerular diseases. P- and E-selectin were both expressed along the glomerular capillaries and the peritubular capillaries in the interstitium. Neither P- nor E-selectin were correlated with the number of infiltrated leukocytes in the glomeruli, however, interestingly the E-selectin expression on peritubular capillaries was correlated with the number of infiltrated CD14 positive cells in the interstitium. These results suggest that E-selectin may play a key role in leukocyte infiltration into the renal interstitium in patients with diabetic nephropathy. [Diabetologia (1998) 41: 185–192]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250050888
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  • 2
    Electronic Resource
    Electronic Resource
    Increased expression of endothelial cell nitric oxide synthase (ecNOS) in afferent and glomerular endothelial cells is involved in glomerular hyperfiltration of diabetic nephropathy (1998)
    Springer
    Diabetologia 41 (1998), S. 1426-1434 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Nitric oxide (NO) ; endothelial cell nitric oxide synthase (ecNOS) ; diabetic nephropathy ; afferent arterioles ; glomerular hyperfiltration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The overproduction of nitric oxide (NO) is reported in the diabetic kidney and considered to be involved in glomerular hyperfiltration. The precise mechanism of NO production in the diabetic kidney is, however, not known. In this report, we compare the localization of endothelial cell nitric oxide synthase (ecNOS) isoform expression in the kidney tissue of streptozotocin (STZ)-induced diabetic rats and 5/6 nephrectomized rats and clarify the pivotal role of ecNOS for the glomerular hyperfiltration in the early stages of diabetic nephropathy. In diabetic rats, the diameters of afferent arterioles, the glomerular volume, creatinine clearance, and urinary NO2/NO3 were increased after the induction of diabetes. Efferent arterioles were, however, not altered. Insulin or L-NAME treatment returned the diameters of afferent arterioles, glomerular volume, creatinine clearance, and urinary NO2/NO3 to normal. The expression of ecNOS in afferent arterioles and glomeruli of diabetic rats increased during the early stages of the disease, but was not altered in efferent arterioles. Treatment with either insulin or L-NAME decreased ecNOS expression in afferent arterioles and in glomeruli. In contrast, the ecNOS expression was upregulated in both afferent and efferent arterioles and in the glomeruli of 5/6 nephrectomized rats, where the dilatation of afferent and efferent arterioles and glomerular enlargement were observed. Treatment with L-NAME ameliorated the ecNOS expression and dilatation of arterioles. We conclude that enhanced NO synthesis by ecNOS in afferent arterioles and glomerular endothelial cells in response to the hyperglycaemic state could cause preferential dilatation of afferent arterioles, which ultimately induces glomerular enlargement and glomerular hyperfiltration. [Diabetologia (1998) 41: 1426–1434]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250051088
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  • 3
    Electronic Resource
    Electronic Resource
    Advanced glycation end products-cytokine-nitric oxide sequence pathway in the development of diabetic nephropathy: aminoguanidine ameliorates the overexpression of tumour necrosis factor-α and inducible nitric oxide synthase in diabetic rat glomeruli (1999)
    Springer
    Diabetologia 42 (1999), S. 878-886 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Advanced glycation end products ; aminoguanidine ; nitric oxide ; diabetic nephropathy.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Aims/hypothesis. Advanced glycation end products are believed to contribute to diabetic microvascular complications by inducing glomerular damage but their role has not been fully clarified. In this study, we explain their central role in the induction of inducible nitric oxide synthase and production of nitric oxide (NO) in streptozotocin-induced diabetic rat glomeruli. Methods. Localization of carboxymethyllysine, which is one of the chemical components of advanced glycation end products, glomerular expression of inducible nitric oxide synthase and urinary excretion and glomerular production of NO2 –/NO3 – were examined at 0, 26, 51, and 52 weeks after the induction of diabetes. Therapeutic effects of aminoguanidine were also examined. Results. Carboxymethyllysine was detected in the mesangial area in glomeruli and it progressively accumulated during 52 weeks of observation. Immunohistochemistry and hybridization studies in situ showed that the number of inducible nitric oxide synthase-positive cells was notably increased in diabetic rat glomeruli at 52 weeks. Further, this augmented expression paralleled intraglomerular expression of TNF-α and NO2 –/NO3 – in diabetic rat glomeruli. Treatment with aminoguanidine reduced the expression of TNF-α, inducible nitric oxide synthase and intraglomerular NO2 –/NO3 – production. It also ameliorated proteinuria in diabetic rats. Conclusion/interpretation. This study showed that carboxymethyllysine possibly enhances the expression of inducible nitric oxide synthase by stimulating the expression of TNF-α in diabetic rat glomeruli. The carboxymethyllysine-cytokine-NO sequence pathway could be one of the major mechanisms in the development of diabetic nephropathy. [Diabetologia (1999) 42: 878–886]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s001250051241
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  • 4
    Electronic Resource
    Electronic Resource
    Two new genes, PHO86 and PHO87, involved in inorganic phosphate uptake in Saccharomyces cerevisiae (1996)
    Springer
    Current genetics 29 (1996), S. 344-351 
    Details
    ISSN: 1432-0983
    Keywords: Key words Arsenate resistance ; Phosphatase regulation ; Pi-transporter ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  The PHO84 gene in Saccharomyces cerevisiae encodes a Pi transporter, mutation of which confers constitutive synthesis of repressible acid phosphatase (rAPase), in medium containing repressible amounts of Pi, and an arsenate-resistant phenotype. We selected an arsenate-resistant mutant showing the constitutive synthesis of rAPase on nutrient plates containing 4.5 mM arsenate. This mutant has double mutations designated as pho86 and pho87. The mutant transcribes PHO84 even in the repressible condition but has a severe defect in Pi uptake. The constitutive rAPase+ phenotype of the pho86 pho87 mutant was partially suppressed by an increased dosage of the PHO84 gene. The PHO87 gene was found to be identical with YCR524, according to the published nucleotide sequence of chromosome III, which encodes a protein of 923 amino-acid residues with a highly charged N-terminal half followed by a C-terminal half consisting of 12 membrane-spanning segments as in Pho84p. These and the other findings suggest that the Pho86p and Pho87p proteins collaborate with Pho84p in Pi uptake.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050055
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  • 5
    Electronic Resource
    Electronic Resource
    Synthesis of 2(3H)-benzofuranone derivatives by copper (i)-promoted substitution reactions of active methylene carbanions
    Amsterdam : Elsevier
    Tetrahedron 42 (1986), S. 2647-2656 
    Details
    ISSN: 0040-4020
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0040-4020(01)90550-2
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  • 6
    Electronic Resource
    Electronic Resource
    The crystal and molecular structure of adenosine hydrochloride (1973)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 29 (1973), S. 31-38 
    Details
    ISSN: 1600-5740
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0567740873001937
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  • 7
    Electronic Resource
    Electronic Resource
    Immunoreactivity of the JK-132 monoclonal antibody directed against basement membrane collagen in normal and diabetic glomeruli (1994)
    Springer
    Virchows Archiv 424 (1994), S. 235-241 
    Details
    ISSN: 1432-2307
    Keywords: Diabetes mellitus ; Type IV collagen ; Glomerulus ; Extracellular matrix ; Monoclonal antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The possible involvement of basement membrane-associated collagen (recognized by the monoclonal antibody JK-132) in the evolution of diabetic nephropathy was studied in kidney specimens from seven patients with noninsulin-dependent diabetes mellitus, and its distribution was compared with those of antibodies against α1 to α4 chains of type IV collagen. JK-132, a monoclonal antibody against basement membrane-associated collagen, reacted immunohistochemically exclusively with the mesangial matrix of the glomerular capillary. In contrast, antibodies to the α1 and α2 chains (IV) reacted strongly with mesangial matrix, and less strongly with the glomerular basement membrane (GBM). Antibodies to the α3 and α4 chains (IV) reacted mainly with GBM. In diabetes, JK-132 reacted most extensively with the expanded mesangial matrix, its staining intensity increasing with progression of the diabetic glomerulosclerosis. Antibodies to the α1 and α2 chains (IV) reacted prominently with the expanded mesangial matrix but less strongly with the GBM. Antibodies to the α3 and α4 chains reacted intensely with the thickened GBM. These results suggest that basement membrane-associated collagen differs from α1 to α4 chains of type IV collagen and that basement membrane-associated collagen is a good marker of mesangial expansion in diabetic nephropathy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00194606
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