New Clues To The Mechanism Of Cardioprotection By Estrogen

Blood ◽  
2013 ◽  
Vol 122 (21) ◽  
pp. 4736-4736
Author(s):  
Nishi H Patel ◽  
R. Alan Mitteer ◽  
Jamunabai M Prakash ◽  
Oresta V Borodevyc ◽  
Gerald Soslau

Platelets are circulating anucleated cell fragments that play a major role in thrombosis and hemostasis in response to a number of stimuli. Platelet activation is a multi-step processes that can be modulated via several known mechanisms. It has long been suspected that sex hormones, like estrogen, have an effect on platelet aggregation and thrombosis; the exact role which estrogen plays in these processes remains unclear. Pre-menopausal women have a lower risk for coronary thrombosis than men– presumably due to higher estrogen levels. However, in postmenopausal women, hormone replacement paradoxically increases the risk for thrombotic events such as coronary and venous thrombosis. Current literature on the subject of estrogen effect on platelets varies considerably. Previous and current research indicates potential estrogen mechanisms for thrombosis; yet the complete biochemical pathway has not been elucidated. Current literature describes the aggregatory effects of estrogen, but little is said about the fact that premenopausal women still have a lower risk for coronary thrombosis in relation to their male counterparts despite having comparatively higher estrogen levels. The goal of our study was to better delineate estrogen mediated biochemical pathways involved in platelet aggregation. Blood was collected from healthy male donors and fractionated into platelet rich plasma (PRP). PRP was centrifuged to prepare platelet poor plasma (PPP) to be used as a control during platelet aggregation assays. PRP samples were incubated with varying physiologic concentrations of 17-b-estradiol for 1-10 minutes and then activated with agonist, and compared to activated control samples in the absence of estrogen. Agonists tested include TRAP-1 (activates PAR-1), gamma thrombin (activates PAR-4), collagen, and ADP. Our results show that estrogen at physiologic levels (60-80 nM) has a synergistic effect on platelet aggregation when combined with sub-threshold doses of agonist. We also showed that this synergy is at least in part mediated by lipid rafts, a fact demonstrated in other studies. A role for lipid rafts in the estrogen effect was demonstrated by incubating PRP with the lipid raft disruptor, methyl β cyclodextrin (MβCD), which resulted in the inhibition of estrogen-induced synergy. Incubation with MβCD alone had no effect on platelet aggregation. We demonstrated that estrogen-induced synergy was absent when platelets, derived from male donors, were washed free of plasma components. Upon the addition of PPP (10-25 uL), synergy was restored. We postulated the necessity of some plasma protein in presenting estrogen to its receptor (ERα and ERβ) for there to be any synergistic effect. Using immunoflourescent microscopy we were able to identify that platelets contain both ERα and ERβ and that the expression of each is altered upon binding of estrogen and TRAP-1. Using filtration techniques we were able to determine that the molecular weight of the necessary protein to restore synergy is greater than 90-100,000 kDa. The most likely candidate was the dimerized plasma sex hormone binding globulin (SHBG), due to its high affinity for estrogens. Support for this comes from the ability of anti-SHBG antibodies to block the estrogen-induced synergy of agonist-induced platelet aggregations. Platelets derived from premenopausal females showed no estrogen-induced synergy of platelet aggregations under the identical conditions used with platelets derived from males. However, platelets derived from postmenopausal women did show synergistic effects of estrogen mirroring effects observed with male platelets samples. In all cases where estrogen-induced synergy of aggregation was observed, incubation of the same platelet samples with estrogen for 2-24hrs totally reversed the synergistic effect. This would be comparable to the premenopausal woman whose platelets in vivo are constantly exposed to high levels of estrogen. Our studies demonstrate that the SHBG must present estrogen to the platelet membrane estrogen receptors and that these receptors are down-regulated upon prolonged exposure to estrogen resulting in reduced levels of platelet aggregation in the presence of sub-optimal concentrations of agonists. Results of our studies would account for the varied effects of estrogen on platelet activation reported in the literature. Studies are in progress with testosterone and second messengers. Disclosures: No relevant conflicts of interest to declare.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 1648-1648
Author(s):  
Ilaria Canobbio ◽  
Lucia Stefanini ◽  
Gianni F. Guidetti ◽  
Cesare Balduini ◽  
Mauro Torti

Abstract The low affinity receptor for immunoglobulin G, FcγRIIA, is expressed in human platelets, mediates heparin-associated thrombocytopenia, and participates in platelet activation induced by von Willebrand factor. Activation of FcγRIIA occurs upon clustering of the receptor induced by immunocomplexes, and consists in the phosphorylation of two tyrosine residues within the ITAM, typically promoted by an associated Src kinase. The phosphorylated receptor acts as a docking site for SH2 domain-containing signaling proteins, including the tyrosine kinase Syk. This event initiates an intracellular tyrosine kinase-based signaling cascade that eventually leads to phosphorylation and activation of phospholipase C (PLC) γ2, and elicits cellular responses. To date, very little is known on the possible involvement of FcγRIIA in platelet activation induced by soluble agonists. We have found that stimulation of platelets with agonists acting on G-protein-coupled receptors resulted in Src-kinase-mediated tyrosine phosphorylation of FcγRIIA. Treatment of platelets with the blocking monoclonal antibody IV.3 against FcγRIIA, but not with control IgG, inhibited platelet aggregation induced by TRAP1, TRAP4, the thromboxane A2 analogue U46619, and low concentrations of thrombin. By contrast, platelet aggregation induced by high doses of thrombin was unaffected by blockade of FcγRIIA. We also found that the anti-FcγRIIA monoclonal antibody IV.3 inhibited pleckstrin phosphorylation and calcium mobilization induced by low, but not high, concentrations of thrombin. Thrombin- and U46619-induced tyrosine phosphorylation of Syk and PLCγ2, which represent substrates typically involved in FcγRIIA-mediated signaling, was clearly reduced by incubation with anti-FcγRIIA antibody IV.3. Morever, we were able to demonstrated that platelet stimulation by thrombin induced the association of FcγRIIA with Syk. Signaling through immunoreceptor typically takes places in characteristic membrane microdomains called lipid rafts. Upon stimulation with thrombin, FcγRIIA relocated in lipid rafts, and thrombin-induced tyrosine phosphorylation of FcγRIIA occurred within these membrane domains. Controlled disruption of lipid rafts by depleting membrane cholesterol prevented tyrosine phosphorylation of FcγRIIA, and impaired platelet aggregation induced by U46619 or by low, but not high, concentrations of thrombin. These results indicate that FcγRIIA can be activated in human platelets downstream G-protein-coupled receptors, and initiates a tyrosine kinase-based signaling pathway that significantly contributes to platelet activation and aggregation in response to weak stimulation.


2001 ◽  
Vol 100 (2) ◽  
pp. 207 ◽  
Author(s):  
Helena J. TEEDE ◽  
Barry P. MCGRATH ◽  
Alan TURNER ◽  
Harry MAJEWSKI

2011 ◽  
Vol 10 (3) ◽  
pp. 123-130
Author(s):  
N. A. Voychenko ◽  
I. V. Kuznetsova ◽  
V. B. Mychka ◽  
M. Yu. Kirillova ◽  
S. N. Tolstov

The adverse consequences of estrogen deficiency in postmenopause include cardiovascular disease (CVD), which affects not only women’s quality of life, but also their life expectancy. Before premenopause, women have significantly lower risk of arterial hypertension than men of the same age. However, in people aged over 50, AH is more prevalent among women. Currently, most experts regard hormone replacement therapy (HRT) in peri- and postmenopausal women as pathogenetic, since it facilitates the adaptation of the female organism to the new metabolic state, with reduced ovarian function. Drospirenone, as a part of HRT, reduces CVD risk in postmenopausal women with climacteric disturbances.


2002 ◽  
Vol 196 (8) ◽  
pp. 1057-1066 ◽  
Author(s):  
Corie N. Shrimpton ◽  
Gautam Borthakur ◽  
Susana Larrucea ◽  
Miguel A. Cruz ◽  
Jing-Fei Dong ◽  
...  

The platelet glycoprotein (GP) Ib-IX-V complex mediates the attachment of platelets to the blood vessel wall by binding von Willebrand factor (VWF), an interaction that also transmits signals for platelet activation and aggregation. Because the complex is extensively palmitoylated, a modification known to target proteins to lipid rafts, we investigated the role of raft localization in GP Ib-IX-V functions. In unstimulated platelets, a minor portion of the complex localized to Triton-insoluble raft fractions; this portion increased three to sixfold with platelet activation by VWF. Raft-associated GP Ib-IX-V was selectively palmitoylated, with GP Ib-IX-V–associated palmitate increasing in the raft fraction on VWF-mediated activation. The raft fraction was also the site of association between GP Ib-IX-V and the Fc receptor FcγRIIA. The importance of this association was demonstrated by the ability of the FcγRIIA antibody IV.3 to inhibit shear-induced platelet aggregation. Disruption of rafts by depleting membrane cholesterol impaired several GP Ib-IX-V–dependent platelet fractions: aggregation to VWF under static conditions and under shear stress, tyrosine phosphorylation, and adhesion to a VWF surface. Partial restoration of membrane cholesterol content partially restored shear-induced platelet aggregation and tyrosine phosphorylation. Thus, localization of the GP Ib-IX-V complex within rafts is crucial for both platelet adhesion and postadhesion signaling.


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