Placental syndecan-1 and sulphated glycosaminoglycans are decreased in preeclampsia

2014 ◽  
Vol 42 (3) ◽  
Author(s):  
Narinda Heyer-Chauhan ◽  
Ihinosen J. Ovbude ◽  
Anne A. Hills ◽  
Mark H. Sullivan ◽  
Frank A. Hills
2015 ◽  
Vol 41 (4) ◽  
pp. 1029-1051 ◽  
Author(s):  
Kirsten O. Hannesson ◽  
Elisabeth Ytteborg ◽  
Harald Takle ◽  
Grethe Enersen ◽  
Grete Bæverfjord ◽  
...  

1987 ◽  
Vol 248 (3) ◽  
pp. 889-896 ◽  
Author(s):  
F A Ofosu ◽  
G J Modi ◽  
M A Blajchman ◽  
M R Buchanan ◽  
E A Johnson

Heparan sulphate and dermatan sulphate have both antithrombotic and anticoagulant properties. These are, however, significantly weaker than those of a comparable amount of standard pig mucosal heparin. Antithrombotic and anticoagulant effects of glycosaminoglycans depend on their ability to catalyse the inhibition of thrombin and/or to inhibit the activation of prothrombin. Since heparan sulphate and dermatan sulphate are less sulphated than unfractionated heparin, we investigated whether the decreased sulphation contributes to the lower antithrombotic and anticoagulant activities compared with standard heparin. To do this, we compared the anticoagulant activities of heparan sulphate and dermatan sulphate with those of their derivatives resulphated in vitro. The ratio of sulphate to carboxylate in these resulphated heparan sulphate and dermatan sulphate derivatives was approximately twice that of the parent compounds and similar to that of standard heparin. Anticoagulant effects were assessed by determining (a) the catalytic effects of each glycosaminoglycan on the inhibition of thrombin added to plasma, and (b) the ability of each glycosaminoglycan to inhibit the activation of 125I-prothrombin in plasma. The least sulphated glycosaminoglycans were least able to catalyse the inhibition of thrombin added to plasma and to inhibit the activation of prothrombin. Furthermore, increasing the degree of sulphation improved the catalytic effects of glycosaminoglycans on the inhibition of thrombin by heparin cofactor II in plasma. The degree of sulphation therefore appears to be an important functional property that contributes significantly to the anticoagulant effects of the two glycosaminoglycans.


Development ◽  
1995 ◽  
Vol 121 (5) ◽  
pp. 1507-1517 ◽  
Author(s):  
J. Davies ◽  
M. Lyon ◽  
J. Gallagher ◽  
D. Garrod

Kidney epithelia have separate origins; collecting ducts develop by ureteric bud growth and arborisation, nephrons by induced mesenchyme-epithelium transition. Both express sulphated glycosaminoglycans (GAGs) which are strikingly upregulated during nephron differentiation. However, sodium chlorate, an inhibitor of GAG sulphation, and the GAG-degrading enzymes heparitinase plus chondroitinase, did not prevent nephron development. In contrast, ureteric bud growth and branching were reversibly inhibited by the above reagents, the inhibition correlating quantitatively with sulphated GAG deprivation caused by a range of chlorate concentrations. Growth and branching could be independently restored during GAG deprivation by hepatocyte growth factor and phorbol-12-myristate acetate (PMA) respectively. Together these signalling effectors stimulated both branch initiation and growth. Thus growth and morphogenesis of ureteric bud involve distinct signalling pathways both regulated by GAGs.


Author(s):  
Agnieszka Jura-Półtorak ◽  
Paweł Olczyk ◽  
Aleksandra Chałas-Lipka ◽  
Katarzyna Komosińska-Vassev ◽  
Kornelia Kuźnik-Trocha ◽  
...  

1983 ◽  
Vol 215 (1) ◽  
pp. 107-116 ◽  
Author(s):  
J T Gallagher ◽  
N Gasiunas ◽  
S L Schor

Human skin fibroblasts cultured on collagen gels produced two dermatan sulphate species, one, enriched in iduronic acid residues, that bound specifically to the collagenous fibres of the gel, the other, enriched in glucuronic acid, that accumulated in the culture medium. Collagen-binding and collagen-non-binding dermatan sulphates were also produced by cells grown on plastic surfaces, but in these cultures each constituent was released into the growth medium. Net synthesis of dermatan sulphate was 3-fold higher in cells maintained on collagen gels. In contrast, heparan sulphate synthesis was not influenced by the nature of the culture surface. The concentration of heparan sulphate in surface-membrane extracts was similar for cells grown on plastic and on collagen gels, but cells cultured on collagen showed a notable increase in the content of surface-membrane dermatan sulphate. The patterns of synthesis and distribution of sulphated glycosaminoglycans observed in skin fibroblasts maintained on collagen gels may reflect differentiated cellular functions.


2011 ◽  
Vol 26 (7) ◽  
pp. 684-689 ◽  
Author(s):  
Siti Fathiah Masre ◽  
George W. Yip ◽  
K.N.S. Sirajudeen ◽  
Farid Che Ghazali

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