Wheat germ agglutinin inhibits thrombin‐induced rises in cytosolic free calcium and prostacyclin synthesis by human umbilical vein endothelial cells

Grulich‐Henn, Jürgen; Weksler, Babette B.; Watanabe, Kentaro; Jaffe, Eric

doi:10.1002/jcp.1041370322

Cited by 7 publications

(6 citation statements)

References 23 publications

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“…The effect of WGA is therefore consistent with many other endothelium-dependent vasodilators and suggests the relaxation is due to the release of EDRF (Furchgott, 1984). The relaxation to WGA was reversed by N-acetyl glucosamine which is specific for WGA recognition (Grulich-Henn et al, 1988). This sugar was ineffective against acetylcholine-induced relaxation.…”

supporting

confidence: 49%

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The effects of lectins on the release of EDRF from rabbit aorta

Kleha¹,

Devesly²,

Johns³

1991

British J Pharmacology

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The effects of the lectins, wheat germ agglutinin (WGA) and concanavalin A (Con A) on endothelium intact pre-contracted rabbit aorta were investigated. WGA (8.3pM) produced endothelium-dependent relaxations, while Con A (4.3 pM) produced a partially endothelium-dependent relaxation. The endothelium-dependent relaxations to WGA were completely reversed by N-acetylglucosamine, haemoglobin and methylene blue and were partially reversed by NG-monomethyl-L-arginine (L-NMMA). It is suggested that WGA works as an agonist in releasing endothelium-derived relaxing factor (EDRF) from the endothelium of rabbit aorta by interacting with a glycosylated receptor on endothelial cells.

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supporting

confidence: 49%

“…Lectins have the ability to bind to specific saccharide groups of glycoproteins and this binding can be reversed and blocked by specific sugars (Grulich-Henn et al, 1988). Some lectins have been used to label specifically the vascular endothelial cells without labelling the underlying smooth muscle cells (Raub et al, 1990).…”

mentioning

confidence: 99%

The effects of lectins on the release of EDRF from rabbit aorta

Kleha¹,

Devesly²,

Johns³

1991

British J Pharmacology

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“…Lectins can interact with specific saccharide groups of glycoproteins to influence diverse biological processes, such as cell-to-cell signalling, host defence and cell differentiation, although often their precise roles remain poorly understood (Van Damme et al 1998;Beisel et al 1999;Assreuy et al 2003). Such glycoprotein binding can be blocked by specific sugars inhibiting function (Grulich-Henn et al 1988).…”

Section: Introductionmentioning

confidence: 99%

Red marine alga Bryothamnion triquetrum lectin induces endothelium-dependent relaxation of the rat aorta via release of nitric oxide

Lima

Criddle

Souza

et al. 2004

Journal of Pharmacy and Pharmacology

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We have investigated the vascular relaxant effects of the lectin from a red marine alga Bryothamnion triquetrum (BTL), in particular, the endothelial-dependency and the participation of a specific glycoprotein-binding site. BTL (1-100 microg mL(-1)) was applied to rat isolated aortic rings, with or without endothelium, tonically precontracted with phenylephrine (0.1 microM). Endothelium-dependent relaxation was assessed in the presence of indometacin (10 microM), L-nitro arginine methyl ester (L-NAME, 100 microM) and tetraethylammonium (TEA, 500 microM). For the involvement of the glycoprotein-binding site, BTL was assayed in presence of mucin (300 microg mL(-1)) or N-acetyl D-glucosamine (GlcNAc; 300 microg mL(-1)), a specific and non-specific lectin-binding sugar, respectively. BTL fully and concentration dependently relaxed preparations that possessed an intact endothelium (IC50 (concn producing 50% contraction) = 12.1 +/- 1.6 microg mL(-1)), whereas no significant relaxation was observed in endothelial-denuded tissue. L-NAME, but not indometacin or TEA, completely inhibited the lectin relaxation, suggesting the involvement of nitric oxide (NO). The lectin in association with mucin, but not with GlcNAc, inhibited BTL-induced relaxation, implicating the involvement of the lectin binding site. Our data suggest that the relaxant effect of the red marine alga Bryothamnion triquetrumlectin on isolated aorta occurs via interaction with a specific lectin-binding site on the endothelium, resulting in a release of NO.

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“…Lectins have the ability to bind to saccharide groups of glycoproteins with this binding being reversed by specific sugars (Grulich-Henn et al, 1988) and have recently been shown to be important in mediating cell to cell interactions by regulating biological processes in living organisms (Sharon & Lis, 1989). The characterization of cell surface glycoproteins including growth factor receptors (Sinnett-Smith et al, 1988), and cell adhesion molecules on endothelial cells (Walz et al, 1990) have also used the unique properties of different lectins.…”

Section: Introductionmentioning

confidence: 99%

“…In cultured endothelial cells, the stimulation of the same receptors causes a coupled release of EDRF and prostacyclin (PGI2) which results in vasodilatation (De Nucci et al, 1988). Thrombin stimulates prostacyclin (PGI2) synthesis in human umbilical vein endothelial cells (HUVEC) (Weksler et al, 1978) and it has been shown that wheat germ agglutinin (WGA) blocks thrombin-induced stimulation of [Ca2+]i, [3H]-arachidonate release, and prostacyclin production in cultured HUVECs (Grulich-Henn et al, 1988). We have suggested that, in the rabbit aorta, WGA binds to a receptor or a cell surface glycoprotein which, via the release of EDRF from the endothelial cell, causes smooth muscle relaxation (Kleha et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

EDRF release from canine coronary artery by lectins

Kleha

Devesly

Johns

1993

British J Pharmacology

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1 The effect of wheat germ agglutinin (WGA), concanavalin A (Con A) and lentil lectin agglutinin (LCA) were investigated on pre-contracted canine coronary artery rings in vitro. 2 In endothelium-intact canine coronary artery, contracted with the thromboxane A2-analogue, U46619, WGA relaxed the tissue in a concentration-dependent manner, with an inhibitory concentration (ICm) of 112 ± 17 nM (n = 6). In the absence of an endothelium, WGA did not cause any relaxation of the tissue. 3 In endothelium-intact canine coronary artery, contracted with the thromboxane A2-analogue, U46619, LCA relaxed the tissue in a concentration-dependent manner, with an inhibitory concentration (ICso) of 423.1 ± 41 nM (n = 6). In the absence of an endothelium, LCA produced a 20.1 + 1.1% (n = 6) relaxation at the highest concentration tested (3 JAM).4 Concanavalin A (Con A) relaxed canine coronary artery in a partial endothelium-dependent manner with an IC50 of 104 ± 19 nM on endothelium-intact coronary artery and an ICs of 1.3 ± 0.3 JAM (n = 6) on endothelium-denuded tissues.5 The relaxation effects of WGA were attenuated by 1 mM N0-monomethyl L-arginine (L-NMMA) and completely inhibited by haemoglobin (3 JAM), methylene blue (10 JAM) and LY 83583 (30 JM). Ibuprofen had no effect on WGA-induced relaxation.6 The relaxant effects of WGA were reversed by addition of 20 mM N-acetyl-D-glucosamine (GlcNAc) and N-acetyl-D-galactosamine (GalNAc) but not by a-mannose, D-(+)-galactose, and P-lactose, whereas the endothelin-dependent relaxations to LCA and Con A were unaffected. 7 The endothelium-dependent relaxation induced by the lectins was unaffected by pretreatment of the tissue with 1 JAM atropine. 8 In the absence of extracellular calcium, WGA was also able to release EDRF suggesting that WGA acts through a second messenger system to release intracellular calcium. 9 We suggest that WGA acts as an agonist to release EDRF from endothelial cells possibly by binding to a sugar moiety, specific receptor or adhesion molecules on the endothelial cell surface.

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Wheat germ agglutinin inhibits thrombin‐induced rises in cytosolic free calcium and prostacyclin synthesis by human umbilical vein endothelial cells

Cited by 7 publications

References 23 publications

The effects of lectins on the release of EDRF from rabbit aorta

The effects of lectins on the release of EDRF from rabbit aorta

Red marine alga Bryothamnion triquetrum lectin induces endothelium-dependent relaxation of the rat aorta via release of nitric oxide

EDRF release from canine coronary artery by lectins

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