Expression of sialidase and dystroglycan in human glomerular diseases.

@article{Vogtlnder2010ExpressionOS,
  title={Expression of sialidase and dystroglycan in human glomerular diseases.},
  author={Nils P. J. Vogtl{\"a}nder and Johan van der Vlag and Marinka A H Bakker and Henry B.P.M. Dijkman and Ron A. Wevers and Kevin P Campbell and Jack F. M. Wetzels and Jo H. M. Berden},
  journal={Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association},
  year={2010},
  volume={25 2},
  pages={
          478-84
        }
}
  • N. Vogtländer, J. van der Vlag, +5 authors J. Berden
  • Published 1 February 2010
  • Biology, Medicine
  • Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association
BACKGROUND alpha-Dystroglycan (alpha-DG) is a negatively charged glycoprotein that covers the surface of podocytes. A decreased glomerular expression of alpha-DG has been described in minimal change nephropathy (MCN), but not in focal segmental glomerulosclerosis (FSGS). This was suggested as a tool to distinguish these diseases. Sialic acid is a negatively charged carbohydrate extensively present on both alpha-DG and podocalyxin, which is also expressed on podocytes. Intrarenal perfusion with… 
View on PubMed
academic.oup.com
15 Citations
Highly Influential Citations
1
Background Citations
4
Results Citations
1

15 Citations

Citation Type

Citation Type

Podocyte-Specific Sialylation-Deficient Mice Serve as a Model for Human FSGS.
TLDR
The notion that loss of sialylation might be part of the complex process causing FSGS is supported and might provide a new therapeutic strategy to cure or delay FSGS and potentially other glomerulopathies.
The Gne M712T mouse as a model for human glomerulopathy.
Glycoprotein Hyposialylation Gives Rise to a Nephrotic-Like Syndrome That Is Prevented by Sialic Acid Administration in GNE V572L Point-Mutant Mice
TLDR
It is suggested that the nephrotic-like syndrome observed in these mutant mice resulted from impaired glomerular filtration due to the hyposialylation of podocyte glycoproteins, including podocalyxin.
Podocin and Beta Dystroglycan expression to study Podocyte-Podocyte and basement membrane matrix connections in adult protienuric states
TLDR
Immunohistochemical expression of podocin and β dystroglycan does not differ in nephropathies which have different site of injury depending on absence (MCD and FSGS) or presence of immune deposits and their localization (MGN and IgAN).
Glycosphingolipids and kidney disease.
TLDR
Evidence supporting a mechanistic role for glycosphingolipids in kidney disease is reviewed and data implicating a role for these lipids in kidneys disease resulting from metabolic syndrome is discussed.
Glycosylation patterns of kidney proteins differ in rat diabetic nephropathy.
TLDR
This study demonstrates the unexplored potential of protein glycosylation analysis in the discovery of molecules linked to diabetic kidney disease using orthogonal methods and confirms a substantial link between gly cosylation signature and diabetes progression.
The role of cell-extracellular matrix interactions in glomerular injury.
Detection of activated parietal epithelial cells on the glomerular tuft distinguishes early focal segmental glomerulosclerosis from minimal change disease.
Acute post-streptococcal glomerulonephritis: analysis of the pathogenesis
TLDR
The mechanisms reported for the APSGN pathogenesis, the interactions of streptococcal products with renal cells and leukocytes, the possible effects of different nephritogenic antigens in the renal environment and the possibility that APS GN is not just due to a single strePTococcal antigen and its antibody are described.
Accumulation of Long-Chain Glycosphingolipids during Aging Is Prevented by Caloric Restriction
TLDR
Accumulation of the glycosphingolipids HexCer and LacCer in several different organs in rodents and humans during aging is demonstrated, and caloric restriction, previously shown to prevent the declining kidney function seen in aging, inhibits accumulation of long-chain HexCers/LacCers and prevents the age-associated elevation of enzymes involved in their synthesis.
...
1
2
...

References

SHOWING 1-10 OF 44 REFERENCES
Glomerular expression of dystroglycans is reduced in minimal change nephrosis but not in focal segmental glomerulosclerosis.
TLDR
Ao- and 3-dystroglycan (DG) were detected at precisely the sa-ne location by immunoelectron microscopy and point to different potentially pathogenic mechanisms of foot process flattening in MCN and FSGS.
Reactive oxygen species deglycosilate glomerular alpha-dystroglycan.
TLDR
It is concluded that deglycosilation of glomerular alpha-DG by ROS leads to disruption of the agrin-dG complex, which in vivo may lead to the detachment of podocytes, and loss of negative charge in the filtration slit may Lead to foot process effacement of podocyte.
Reactive oxygen species deglycosilate glomerular α-dystroglycan
TLDR
It is concluded that deglycosilation of glomerular α -DG by ROS leads to disruption of the agrin–DG complex, which in vivo may lead to the detachment of podocytes, and loss of negative charge in the filtration slit may Lead to foot process effacement of podocyte.
Localization of alpha-dystroglycan on the podocyte: from top to toe.
TLDR
This localization suggests that alpha-DG plays a dual role in the maintenance of the unique architecture of podocytes by its binding to the glomerular basement membrane, and in the Maintenance of the integrity of the filtration slit, respectively.
Expression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathies.
Localization of α-Dystroglycan on the Podocyte: from Top to Toe
TLDR
This localization suggests that α-DG plays a dual role in the maintenance of the unique architecture of podocytes by its binding to the glomerular basement membrane, and in the Maintenance of the integrity of the filtration slit, respectively.
Modifications in glomerular polyanion distribution in adriamycin nephrosis.
TLDR
Kidneys of nephrotic rats induced by the injection of 7.5 mg/kg ADR exhibited severe proteinuria, hypoalbuminemia, and massive fusion of intercalated foot processes of the podocytes, indicating a gradual decrease in glomerular sialic acid content.
Distribution of GBM heparan sulfate proteoglycan core protein and side chains in human glomerular diseases.
TLDR
In human glomerulopathies the major alteration was a segmental or total absence of GBM staining with anti-HS mAb JM-403, which is most pronounced in lupus nephritis, membranousglomerulonephritis (GN), minimal change disease and diabetic nephropathy, whereas the HSPG-core staining by mAbJM-72 was unaltered.
Glomerular heparan sulfate alterations: mechanisms and relevance for proteinuria.
TLDR
Evidence was obtained that hyperglycemia led to a down-regulation of HS synthesis, accompanied by a reduction in the degree of HS sulfation, as well as in streptozotocin-induced diabetic nephropathy and during culture of glomerular cells under high glucose conditions.
Podocyte-Associated Molecules in Puromycin Aminonucleoside Nephrosis of the Rat
TLDR
The results show distinct differences in the different domains of podocytes during PA-induced proteinuria, including diminished protein levels of podocin and nephrin in the PA-treated group.
...
1
2
3
4
5
...