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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Am+J+Physiol+Renal+Physiol
2016 ; 310
(10
): F1123-35
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N-sulfation of heparan sulfate is critical for syndecan-4-mediated podocyte
cell-matrix interactions
#MMPMID26936875
Sugar T
; Wassenhove-McCarthy DJ
; Orr AW
; Green J
; van Kuppevelt TH
; McCarthy KJ
Am J Physiol Renal Physiol
2016[May]; 310
(10
): F1123-35
PMID26936875
show ga
Previous research has shown that podocytes unable to assemble heparan sulfate on
cell surface proteoglycan core proteins have compromised cell-matrix
interactions. This report further explores the role of N-sulfation of intact
heparan chains in podocyte-matrix interactions. For the purposes of this study, a
murine model in which the enzyme N-deacetylase/N-sulfotransferase 1 (NDST1) was
specifically deleted in podocytes and immortalized podocyte cell lines lacking
NDST1 were developed and used to explore the effects of such a mutation on
podocyte behavior in vitro. NDST1 is a bifunctional enzyme, ultimately
responsible for N-sulfation of heparan glycosaminoglycans produced by cells.
Immunostaining of glomeruli from mice whose podocytes were null for Ndst1
(Ndst1(-/-)) showed a disrupted pattern of localization for the cell surface
proteoglycan, syndecan-4, and for ?-actinin-4 compared with controls. The pattern
of immunostaining for synaptopodin and nephrin did not show as significant
alterations. In vitro studies showed that Ndst1(-/-) podocytes attached, spread,
and migrated less efficiently than Ndst1(+/+) podocytes. Immunostaining in vitro
for several markers for molecules involved in cell-matrix interactions showed
that Ndst1(-/-) cells had decreased clustering of syndecan-4 and decreased
recruitment of protein kinase-C?, ?-actinin-4, vinculin, and phospho-focal
adhesion kinase to focal adhesions. Total intracellular phospho-focal adhesion
kinase was decreased in Ndst1(-/-) compared with Ndst1(+/+) cells. A significant
decrease in the abundance of activated integrin ?5?1 on the cell surface of
Ndst1(-/-) cells compared with Ndst1(+/+) cells was observed. These results serve
to highlight the critical role of heparan sulfate N-sulfation in facilitating
normal podocyte-matrix interactions.
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