Heparan sulphate and the binding of lipoprotein lipase to porcine thoracic aorta endothelium

Williams, Monica P.; Streeter, Heather B.; Wusteman, Frederick S.; Cryer, Anthony

doi:10.1016/0304-4165(83)90027-2

Cited by 48 publications

(17 citation statements)

References 26 publications

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“…The concentration of proteoglycans on intact native endothelium has been estimated, by labelling with 35SO4 and also by X-ray microanalysis to be about 10 -12 mol polysaccharide chain per cm 2 or about 0.2 mM assuming the thickness of the glycocalyx to be 100 nm [17,18]. Of this concentration about half is heparan sulphate.…”

Section: Discussionmentioning

confidence: 99%

Heparan sulphate with no affinity for antithrombin III and the control of haemostasis

Scully¹,

Ellis²,

Kakkar³

1988

FEBS Letters

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Heparan sulphate with no affinity for antithrombin III (ATIII) was observed to cause acceleration of the factor Xa:ATIII interaction by 1100-fold (k2, 7 × 107 M-l.min -1) and the prothrombinase:ATllI interaction by 2900-fold (k2, 2.5 x l0 T M-1 .min-1). Although high-affinity heparan sulphate catalyzed higher acceleration and at lower concentration, in natural mixtures of the two forms the activity of the no affinity form predominated. Heparan sulphate had no significant effect on the thrombin:ATIII interaction but inhibited its potentiation by heparin (Kd 0.3/~M). From the estimated concentration of heparan sulphate on the endothelial cell surface it is proposed that the non-thrombogenic property of blood vessels is due to the acceleration of the factor Xa or prothrombinase:ATIIl interaction by the greater mass of surface-bound heparan sulphate rather than by the much smaller proportion of heparin-like molecules (with high affinity for antithrombin III) which may be present.

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Section: Discussionmentioning

confidence: 99%

Heparan sulphate with no affinity for antithrombin III and the control of haemostasis

Scully¹,

Ellis²,

Kakkar³

1988

FEBS Letters

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“…215 -216 - 217 Recently, Klinger et al 218 used a lipoprotein lipase-agarose affinity column to isolate an HSPG from a mixture of proteoglycans in rat brain and found it to be a membrane-associated proteoglycan of approximately 220 kd containing glycosaminoglycan chains of M r =14 000 to 15 000. The mechanism by which this proteoglycan interacts with the enzyme is not clear, but most probably involves the glycosaminoglycan portion of the molecule, since glycosaminoglycan chain length and the number of N-sulfate and N-acetyl groups on the glycosaminoglycan chain affect affinity for lipoprotein lipase.…”

Section: Lipid Metabolismmentioning

confidence: 99%

Cell biology of arterial proteoglycans.

1989

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“…The similiarity between exogenous lipoprotein lipase (Cheng et al, 1981; Williams et al, 1983), low density lipoprotein (Goldstein et al, 1976) The secretion of mitogens by endothelium could be counterbalanced in vivo by production and release of putative inhibitors of smooth muscle cell proliferation. Castellot et al (1982) demonstrated release of heparan sulfates by endothelium in vitro, induced by whole blood serum, owing to the proteolytic action of an endoglucosidase released from platelets.…”

Section: Discussionmentioning

confidence: 97%

Release of endothelial cell‐derived growth factor (ECDGAF) by heparin

Gajdusek

1984

Journal Cellular Physiology

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Endothelial cells in vitro produce potent growth-promoting activities collectively known as endothelial cell-derived growth factor (ECDGF). These mitogens (including platelet-derived growth factor [PDGF]-like and non-PDGF-like species) support DNA synthesis and proliferation of smooth muscle cells and fibroblasts in the absence of other defined mitogens. The current study examines interaction of heparin and heparin-related polysaccharides with bovine aortic endothelial (BAE) cells and the levels of secreted growth-promoting activity. Heparin, dextran sulfate, and carageenan rapidly release non-PDGF-like ECDGF from BAE cell monolayers. The effective heparin concentrations closely correlate with amounts of exogenous 3H-heparin required for maximal binding to BAE cells. Both heparin binding and ECDGF release occur independently of incubation temperature. Inhibition of heparin binding by dextran sulfate and carageenan and the lack of inhibition by dextran, chondroitin sulfate, and dermatan sulfate imply a high degree of specificity of the interaction. In contrast to quiescent monolayers of BAE cells, migrating cells release lower levels of growth-promoting activity, and no ECDGF is released in response to heparin, although migrating cells bind the same levels of 3H-heparin as confluent monolayers. Partial characterization of the endothelial cell released mitogens indicates that the non-PDGF-like mitogen is associated with endothelial cell surfaces in contrast to the apparent constitutive release of PDGF-like mitogens. These results indicate that endothelial cells modulate production and release of specific mitogens in response to growth state.

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Heparan sulphate and the binding of lipoprotein lipase to porcine thoracic aorta endothelium

Cited by 48 publications

References 26 publications

Heparan sulphate with no affinity for antithrombin III and the control of haemostasis

Heparan sulphate with no affinity for antithrombin III and the control of haemostasis

Cell biology of arterial proteoglycans.

Release of endothelial cell‐derived growth factor (ECDGAF) by heparin

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