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PubMed1991

May the alterations in lipid fluidity-mediated platelet hypersensitivity contribute to accelerated aging of platelets in diabetes mellitus?

Reduced platelet membrane lipid fluidity occurring in diabetes implies that platelet membrane receptors are more exposed to the external environment. This, in turn, may result in an increased sensitivity of platelets from diabetic humans to platelet aggregating agents. Platelet hypersensitivity (PH) may lead to augmented effects of agonists on the release of amine storage granules from the platelets of diabetic individuals. Aggregating and release-inducing agents decrease platelet density, which is assumed to be relevant to the aging processes. Thus it has become commonly accepted that platelet senescence or aging contributes to platelet density heterogeneity (PDH). Alterations of dynamic parameters of platelet membranes in diabetes may thus underlie the increased rate of aging or senescence of platelets in diabetic subjects.

Blood Platelets↗
PubMed2001

Inhibition of platelet aggregation and the release of P-selectin from platelets by cilostazol.

To evaluate the in vitro effects of cilostazol, a phosphodiesterase III inhibitor, on platelet responses, we measured platelet aggregation and the levels of soluble P-selectin, a glycoprotein present on the alpha-granule membrane in resting platelets, and cAMP. Platelet-rich plasma and washed platelets from healthy human volunteers were treated with cilostazol (5, 25 and 50 microM). Platelet-rich plasma was stimulated by ADP (1 and 5 microM) or collagen (5 microg/ml). Washed platelets were stimulated by thrombin (4 U/ml) in the presence or absence of 1 microM forskolin. In vehicle-treated samples, soluble P-selectin levels in response to 1 microM ADP-induced primary aggregation were similar to those of circulating levels of healthy volunteers but the levels in response to 5 microM ADP-induced secondary aggregation and collagen-induced aggregation increased markedly compared to those in response to primary aggregation. This result suggests that P-selectin is released from platelets according to the extent of platelet aggregation. Cilostazol inhibited platelet aggregation as well as P-selectin release in a concentration-dependent manner. Cilostazol inhibited completely thrombin-induced aggregation in the presence of 1 microM forskolin, when cAMP levels were two-fold higher than those in the absence of forskolin. Cilostazol, which increases intracellular cAMP in platelets, may be useful in the treatment of arterial occlusive diseases.

Adenosine Diphosphate↗
PubMed1999

Effects of fish oil supplementation on platelet survival and ex vivo platelet function in hypercholesterolemic patients.

Little is known about the effects of dietary supplementation on platelet survival with low doses of n-3 and n-6 fatty acids in patients with hypercholesterolemia. The effects of a 6-week intervention with fish oil capsules (daily intake: 216 mg eicosapentaenoic acid, 140 mg docosahexaenoic acid, 390 mg gamma-linolenic acid, and 3480 mg linoleic acid) on in vivo platelet survival (111 In-oxine labeled platelets) and on ex vivo markers of platelet activation were investigated in a placebo-controlled, double-blind study with 26 hypercholesterolemic patients. In vivo platelet survival increased in the fish oil group (T) from a mean of 159+/-14 hours to a mean of 164+/-12 hours (p=0.025), whereas it remained unchanged in the placebo (P) group (T vs. P; p=0.055). Ex vivo, thromboxane B2 decreased from a mean of 225+/-16 to 212+/-21 ng/mL (p=0.003) in T but did not change in P (T vs. P: p=0.002). Malondialdehyde formation was lowered significantly by fish oil supplementation from a mean of 5.49+/-1.3 to 5.12+/-1.05 nM/10(9) platelets, p=0.005, as compared with P (T vs. P; p=0.018). The trendwise decrease in 11-DH-thromboxane B2 plasma levels was not significant nor was the increase in platelet sensitivity to prostaglandin I2 by fish oil. Baseline platelet survival in patients with hyperlipoproteinemia type IIa was not different from those with hyperlipoproteinemia IIb and response to treatment in terms of platelet activation markers was not either. The changes in platelet activation parameters in T were associated with significant reductions in cholesterol (-2.9%), low density lipoprotein cholesterol (-3.5%), and triglycerides (-12.4%). Both ex vivo and in vivo platelet activation parameters exhibited signs of decreased activation by a 6-week diet supplemented with n-3 and n-6 fatty acids, which might be beneficial in reducing atherothrombotic risk, in patients with hyperlipoproteinemia type IIa and IIb.

Blood Platelets↗
PubMed1999

Platelet-bound immunogloblins before and after platelet transfusion: measurement of in vivo binding.

In routine tests to investigate immunological mechanisms as a cause for enhanced destruction of transfused platelets; serum from the patient is tested against a panel of donor lymphocytes and platelets to demonstrate the presence of antibodies against HLA or platelet specific antibodies. Here we describe a flow cytometric technique in which in vivo binding of immunoglobulins (Ig) is measured. By comparing the histograms of the platelet suspensions before and after transfusion, four different patterns were obtained: no Ig binding before and after transfusion (pattern 1), pre-existent Ig binding (patterns 2 and 3) or preferential Ig binding to the transfused platelets (pattern 4). This technique was tested in 164 random platelet transfusions and 34 HLA-matched platelet transfusions. A statistically significant association was found between pattern 1 and a negative result of the indirect platelet immunofluorescence test for the detection of antibodies in the serum taken before the transfusion studied or a good platelet recovery and between pattern 4 and a positive indirect platelet immunofluorescence test or a low platelet recovery.

Autoimmunity↗
PubMed1975

Use of platelet aggregometry in selection of compatible platelet donors.

To determine if platelet aggregometry was useful in selecting compatible platelet donors, six patients who had become refractory to random platelets were studied. Serum from the patient was added to citrated platelet-rich plasma from the prospective donor in a standard aggregometry system. Serial aggregometry studies revealed no platelet aggregation unless the refractory state had been reached. At that time positive aggregation occurred only between the poorly matched pairs. A correlation between platelet aggregation and HL-A histocompatibility was noted. Family members with negative aggregation were selected as donors, and their platelets were able to provide consistently satisfactory increments in the platelet count of the recipient who was refractory to random donors. In contrast, platelets from family members who exhibited positive aggregation failed to do so. These findings suggest that platelet aggregometry can be used to select compatible platelet donors.

Blood Donors↗
PubMed1997

Platelet signal transduction defect with Galpha subunit dysfunction and diminished Galphaq in a patient with abnormal platelet responses.

G proteins play a major role in signal transduction upon platelet activation. We have previously reported a patient with impaired agonist-induced aggregation, secretion, arachidonate release, and Ca2+ mobilization. Present studies demonstrated that platelet phospholipase A2 (cytosolic and membrane) activity in the patient was normal. Receptor-mediated activation of glycoprotein (GP) IIb-IIIa complex measured by flow cytometry using antibody PAC-1 was diminished despite normal amounts of GPIIb-IIIa on platelets. Ca2+ release induced by guanosine 5'-[gamma-thio]triphosphate (GTP[gammaS]) was diminished in the patient's platelets, suggesting a defect distal to agonist receptors. GTPase activity (a function of alpha-subunit) in platelet membranes was normal in resting state but was diminished compared with normal subjects on stimulation with thrombin, platelet-activating factor, or the thromboxane A2 analog U46619. Binding of 35S-labeled GTP[gammaS] to platelet membranes was decreased under both basal and thrombin-stimulated states. Iloprost (a stable prostaglandin I2 analog) -induced rise in cAMP (mediated by Galphas) and its inhibition (mediated by Galphai) by thrombin in the patient's platelet membranes were normal. Immunoblot analysis of Galpha subunits in the patient's platelet membranes showed a decrease in Galphaq (<50%) but not Galphai, Galphaz, Galpha12, and Galpha13. These studies provide evidence for a hitherto undescribed defect in human platelet G-protein alpha-subunit function leading to impaired platelet responses, and they provide further evidence for a major role of Galphaq in thrombin-induced responses.

Blood Platelets↗
PubMed1997

Sphingosine 1-phosphate induces platelet activation through an extracellular action and shares a platelet surface receptor with lysophosphatidic acid.

Sphingosine 1-phosphate (Sph-1-P) has been implicated as an intracellular second messenger in many studies. We investigated the metabolism of Sph-1-P and the mechanism by which Sph-1-P induces activation in enucleated and highly differentiated platelets. Platelets lack Sph-1-P lyase activity, possess persistently active sphingosine (Sph) kinase, and abundantly store Sph-1-P. Although exogenous Sph-1-P activated platelets, intracellular Sph-1-P, formed from exogenously added Sph by cytosolic Sph kinase, failed to do so. To support the notion that exogenous Sph-1-P stimulates platelets from outside, contact of platelet surfaces with immobilized Sph-1-P covalently linked to glass particles resulted in platelet activation. Furthermore, we detected the specific binding sites for radiolabeled Sph-1-P on the platelet surface, suggesting extracellular effects of Sph-1-P on plasma membrane receptors. This specific Sph-1-P binding was inhibited not by other sphingolipids but by lysophosphatidic acid (LPA), and platelet aggregation response to LPA was specifically desensitized by prior addition of Sph-1-P. Finally, internally stored Sph-1-P is released extracellularly upon stimulation, and the release correlated well with protein kinase C activation in intact platelets. These results suggest that Sph-1-P acts not intracellularly but intercellularly, following discharge from activated platelets, and shares a platelet surface receptor with LPA.

Blood Platelets↗
PubMed1997

Thrombin receptors on human platelets. Initial localization and subsequent redistribution during platelet activation.

Platelet responses to thrombin are at least partly mediated by a G-protein-coupled receptor whose NH2 terminus is a substrate for thrombin. In the present studies we have examined the location of thrombin receptors in resting platelets and followed their redistribution during platelet activation. The results reveal several new aspects of thrombin receptor biology. 1) On resting platelets, approximately two-thirds of the receptors were located in the plasma membrane. The remainder were present in the membranes of the surface connecting system. 2) When platelets were activated by ADP or a thromboxane analog, thrombin receptors that were initially in the surface connecting system were exposed on the platelet surface, increasing the number of detectable receptors by 40% and presumably making them available for subsequent activation by thrombin. 3) Platelet activation by thrombin rapidly abolished the binding of the antibodies whose epitopes are sensitive to receptor cleavage and left the platelets in a state refractory to both thrombin and the agonist peptide, SFLLRN. This was accompanied by a 60% decrease in the binding of receptor antibodies directed COOH-terminal to the cleavage site irrespective of whether the receptors were activated proteolytically by thrombin or nonproteolytically by SFLLRN. 4) The loss of antibody binding sites caused by thrombin was due in part to receptor internalization and in part to the shedding of thrombin receptors into membrane microparticles, especially under conditions in which aggregation was allowed to occur. However, at least 40% of the cleaved receptors remained on the platelet surface. 5) Lacking the ability to synthesize new receptors and lacking an intracellular reserve of preformed receptors comparable to that found in endothelial cells, platelets were unable to repopulate their surface with intact receptors following exposure to thrombin. This difference underlies the ability of endothelial cells to recover responsiveness to thrombin rapidly while platelets do not, despite the presence on both of the same receptor for thrombin.

Amino Acid Sequence↗
PubMed2001

Inhibition of leukocyte chemiluminescence by platelets: role of platelet-bound fibrinogen.

Tethering of PMNL by platelets via CD62P has been shown to cause PMNL activation. Co-incubation of purified PMNL with platelets that were activated with thrombin and then fixed and washed, resulted in the formation of platelet-PMNL conjugates as well as in a generation of reactive oxygen species that were measured as luminol-enhanced chemiluminescence. When platelets were thrombin activated in the presence of RGDS to prevent binding of fibrinogen to membrane receptors, they had a reduced capacity to adhere to PMNL, but ROS generation was enhanced. In samples of citrated whole blood RGDS as well as the more specific platelet fibrinogen receptor antagonist GR144053F or a dissociation of the platelet glycoprotein IIb/IIIa complex markedly enhanced ROS generation that was induced by stirring the samples for 10 min at 1000 rpm, by 175%, 95% and 138%, respectively. Removal of platelets from the whole blood samples also resulted in an enhancement of stirring-induced ROS generation, which was inversely correlated to the platelet count. These data provide some evidence that platelets are capable of inhibiting ROS generation in PMNL by a mechanism that involves platelet-bound fibrinogen and probably depends on fibrinogen-mediated platelet-PMNL contact.

Blood Platelets↗
PubMed2006

ThromboFix platelet stabilizer: advances in clinical platelet analyses by flow cytometry?

UNLABELLED: Platelet flow cytometry is restricted by spontaneous platelet activation in unfixed samples or by significant alterations of platelet performance caused by the use of fixatives. Aim of this study was to evaluate the new platelet stabilizer ThromboFix for clinical diagnostics. METHODS: Whole blood samples with or without addition of a weak (ADP) or strong (TRAP-6) agonist were fixed with either ThromboFix or paraformaldehyde (PFA) and stored for different periods of time for up to 7 days. Samples were then incubated with either CD41 and CD62P or CD42b and CD45 monoclonal antibodies and analyzed by flow cytometry. RESULTS: The numbers of platelets, microparticles and aggregates remained stable for 7 days after treatment with ThromboFix but not with PFA due to an increasing aggregate formation after 3 days. Platelet activation was restricted to less than 1% of CD62P positive events in resting samples without a significant difference compared to an unfixed reference sample. Fixation, however, significantly reduced CD62P expression after stimulation (P < 0.05). Stabilized by ThromboFix, the level of platelet activation remained unchanged in resting and ADP stimulated samples for 7 days but decreased moderately with time after a strong stimulation with TRAP-6 (P < 0.01). After PFA fixation, intact CD62P antigen disappeared from the platelet surface within hours (P < 0.01). ThromboFix reduced the formation of platelet-leukocyte conjugates significantly (P < 0.05) and, in contrast to PFA, failed to stabilize the already formed conjugates. CONCLUSION: In clinical situations without immediate access to a flow cytometer, ThromboFix is helpful in the flow cytometric analysis of the platelet activation marker CD62P. It should not be used for the investigation of platelet-leukocyte conjugate formation.

Adenosine Diphosphate↗
PubMed2006

Polyphenols enhance platelet nitric oxide by inhibiting protein kinase C-dependent NADPH oxidase activation: effect on platelet recruitment.

Several studies demonstrated an inverse association between polyphenol intake and cardiovascular events. Platelet recruitment is an important phase of platelet activation at the site of vascular injury, but it has never been investigated whether polyphenols influence platelet recruitment. The aim of the study was to analyze in vitro whether two polyphenols, quercetin and catechin, were able to affect platelet recruitment. Platelet recruitment was reduced by NO donors and by NADPH oxidase inhibitors and was enhanced by L-NAME, an inhibitor of NO synthase. Quercetin and catechin, but not single polyphenol, significantly inhibited platelet recruitment in a concentration-dependent fashion. The formation of superoxide anion was significantly inhibited in platelets incubated with quercetin and catechin but was unaffected by a single polyphenol. Incubation of platelets with quercetin and catechin resulted in inhibition of PKC and NADPH oxidase activation. Treatment of platelets with quercetin and catechin resulted in an increase of NO and also down-regulated the expression of GpIIb/IIIa glycoprotein. This study shows that the polyphenols quercetin and catechin synergistically act in reducing platelet recruitment via inhibition of PKC-dependent NADPH oxidase activation. This effect, resulting in NO-mediated platelet glycoprotein GpIIb/IIIa down-regulation, could provide a novel mechanism through which polyphenols reduce cardiovascular disease.

Adult↗
PubMed2000

A synthetic nonapeptide derived from the sequence of a platelet type I collagen receptor inhibits type I collagen-mediated platelet aggregation.

We have cloned the platelet receptor for type I collagen, but the structure-function of the receptor has not been completely established. The purpose of this investigation was to identify a collagen binding site(s) of the platelet receptor. Three peptides were synthesized chemically. Each peptide serves as an inhibitor of type I collagen-induced platelet aggregation, ATP release, platelet protein phosphorylation, and platelet adhesion to artificial matrices and aortic segments. We show that a nonapeptide specifically inhibits type I collagen-induced platelet aggregation and the release of ATP in a dose-dependent fashion. The peptide also inhibits the binding of radiolabeled alpha (I) chain to washed platelets, the adhesion of radiolabeled platelets to type I collagen-coated petri dishes, rabbit aortic segments, and platelet protein phosphorylation. Deletion of this peptide region of the cloned cDNA abolishes the inhibitory effect of the recombinant protein on type I collagen-induced platelet aggregation. These findings support the likelihood that the nonapeptide forms part of the binding site of the platelet receptor for type I collagen.

Amino Acid Sequence↗
PubMed2001

The role of platelet factor 4 in platelet aggregation induced by the antibodies implicated in heparin-induced thrombocytopenia.

Heparin-induced thrombocytopenia (HIT) is a severe side effect of heparin treatment. Recent studies using immunological methods demonstrated that antibodies contained in plasma, or in purified total immunoglobulin (Ig)G from patients suffering HIT, recognize as target antigen the complex heparin/platelet factor (PF4). In the present study, the role of PF4 in in-vitro platelet aggregation induced by purified total IgG or platelet-poor plasma from patients suffering HIT was investigated. In order to demonstrate the functional role of PF4, an anti-PF4 antibody that specifically blocked PF4 was used. In an experimental system composed of washed platelet suspension, incubation of F(ab')2 fragments (0.125 microg/ml) of the polyclonal anti-PF4 antibody resulted in complete inhibition of platelet aggregation triggered by purified total IgG from patients suffering HIT and heparin. In platelet-rich plasma, a significantly higher concentration (4.25 microg/ml) of the anti-PF4 F(ab')2 was required to inhibit platelet aggregation induced by HIT-PPP and heparin. Intermediate concentrations of the anti-PF4 antibody partially inhibited platelet aggregation. In plasma milieu, the concentration of PF4 was about five-fold higher in comparison with that measured in the purified system. The intensity of platelet aggregation depended on the concentration of HIT-IgG. Platelet aggregation was abolished in the presence of high concentrations of heparin (superior or equal to 10 IU/ml). The present study shows that PF4 is essential for platelet aggregation triggered by the antibodies related to HIT in the presence of heparin. The concentration of PF4 that is available to bind with heparin or with the HIT-related antibodies is critical for platelet aggregation induced by HIT antibodies.

Antibodies↗
PubMed1981

Relationship of raised platelet IgG in thrombocytopenia to total platelet protein content.

Platelet-associated IgG (PA IgG) of washed platelets of 20 normal controls and 45 thrombocytopenic patients was measured by radioimmunoassay and related to total platelet protein content. Mean values (+/- 2 SD) for 20 normals were 4.4 +/- 3.5 fg IgG per platelet (fg IgG/pl), 2.1 +/= 1.0 pg protein per platelet (pg protein/pl) and a ratio of IgG per g platelet protein of 2.1 +/- 1.8 mg IgG/g protein. Patients could be divided into two groups: Group I (31) with normal IgG/g protein ratios and either normal (16) or raised (15) fg IgG/pl, and Group II (14) with both fg IgG/pl and IgG/g protein raised. Of the 21 patients with idiopathic thrombocytopenia (ITP), 13 were in Group I (seven with raised and six with normal fg IgG/pl), and eight in Group II. There was significant correlation between PA IgG (fg IgG/pl) and platelet protein for the entire Group I (r = 0.95, P less than 0.001). The ITP patients in this group showed a similar correlation (r = 0.77, P less than 0.001), suggesting that raised PA IgG levels in Group I patients may be a result of protein-rich platelets. 60-90% of PA IgG was found in the soluble fraction of lysates of platelets from both normals and patients. Thus, it is either non-specifically associated with platelets or is antibody directed towards easily solubilized platelet antigens. Nine thrombocytopenic patients without immune disorders had raised PA IgG. These results question the assumption that raised PA IgG always indicates specific antiplatelet antibody.

Blood Platelets↗
PubMed1984

Measurement of platelet life-span in normal subjects and patients with myeloproliferative disease with indium oxine labelled platelets.

The use of 111Indium oxine as a platelet label for the performance of platelet life-span studies has been examined. Platelet life-span in normal subjects varied between 8 X 10 and 10 X 36 d. Patients with primary thrombocythaemia had clearly reduced platelet life-span whether or not they presented with vascular occlusion and this abnormality persisted after reduction of the platelet count to normal by busulphan therapy. Patients with similarly elevate platelet counts due to chronic granulocytic leukaemia or after splenectomy had platelet life-span values in the normal range. Plasma beta-TG levels could not be used to predict platelet life-span in these groups of patients. Measurement of platelet life-span using 111Indium labelled platelets is a useful technique in the examination of platelet function in occlusive vascular disease.

Adult↗
PubMed1990

Transfusion of ABO-mismatched platelets leads to early platelet refractoriness.

Forty-three consecutive patients previously unexposed to platelets and undergoing treatment for acute leukaemia or autografting for relapsed Hodgkin's lymphoma were randomized to receive transfused platelets of either their own ABO group (OG) or of a major mismatched group (MMG). The 26 evaluable patients were equally distributed between the two study groups. Nine of 13 (69%) MMG patients became refractory with a median onset at transfusion 7 (15 d), compared with only one of 13 (8%) OG patients (P = 0.001). Refractoriness was associated with the formation of high titre isoagglutinins, anti-HLA and platelet specific antibodies. In one patient refractoriness appeared to be due to high titre isoagglutinins alone. Six other patients developed an increase in isoagglutinin titre sufficient to adversely affect platelet increments. Patients receiving ABO-mismatched platelets had a higher incidence of anti-HLA antibodies (5 v. 1) and platelet specific antibodies (4 v. 1). ABO-mismatched platelets transfused prior to the onset of refractoriness resulted in increments similar to those achieved by ABO-matched platelets. The study demonstrates that ABO-mismatched platelets are as effective as matched platelets in patients with low titre isoagglutinins requiring only few transfusions. However, the greater incidence of early refractoriness induced in MMG patients indicates that ABO-mismatched platelets should not be given to patients with marrow failure requiring long-term support.

ABO Blood-Group System↗
PubMed1981

Inhibition of prostaglandin E1-responsive platelet adenylate cyclase by heparin: a study of the mechanism of inhibition and its relevance to platelet aggregation.

1 Heparin can produce platelet aggregation in vitro and in vivo; it has been proposed that this may be due to the reported inhibition of the prostaglandin E(1) (PGE(1))-stimulated adenylate cyclase of the platelet by heparin.2 The effect of heparin on the cyclic adenosine 3',5'-monophosphate (cyclic AMP) response to PGE(1) was measured in intact and broken platelets both in vitro and in platelets obtained from normal subjects during intravenous infusion with herapin.3 In platelet lysates, heparin produced a dose-related inhibition of PGE(1)-stimulated adenylate cyclase. The maximum response to PGE(1) was reduced, with half-maximal inhibition occurring at 3 mug/ml heparin. This inhibition could be prevented by protamine sulphate.4 Heparin did not affect PGE(1)-stimulated cyclic AMP production in intact platelets either in vitro or in platelets taken during the infusion of 5,000iu heparin over 2h to 2 normal volunteers. Similarly, preincubation of platelets with heparin for up to 3h at 37 degrees C did not affect platelet adenylate cyclase.5 The effects of heparin were very similar to those of fluoride on the platelet adenylate cyclase: heparin and fluoride increased basal enzyme activity slightly (3-4 fold) but their effects were not additive; both inhibited the response to PGE(1) by approximately 50% when added directly to the assay and the inhibitory effects of the two were not additive; preincubation of membranes with either heparin or fluoride produced an irreversible state of inhibition.6 As heparin inhibits PGE(1)-stimulated adenylate cyclase activity only in broken platelets, we suggest that the aggregatory effects of heparin are probably independent of any action on cyclic AMP production.

Adenylyl Cyclase Inhibitors↗
PubMed2005

The phospholipid composition and cholesterol content of platelet-derived microparticles: a comparison with platelet membrane fractions.

BACKGROUND: The processes that govern the distribution of molecules between platelets and the microparticles (MP) they release are unknown. Certain proteins are sorted selectively into MP, but lipid sorting has not been studied. OBJECTIVES: To compare the phospholipid composition and cholesterol content of platelet-derived MP obtained with various stimuli with that of isolated platelet membrane fractions. METHODS: Washed platelets from venous blood of healthy individuals (n = 6) were stimulated with collagen, thrombin, collagen plus thrombin, or A23187. Platelet activation, MP release and antigen exposure were assessed by flow cytometry. MPs were isolated by differential centrifugation. Platelet plasma-, granule- and intracellular membranes were isolated from platelet concentrates (n = 3; 10 donors each) by pressure homogenization and Percoll density gradient fractionation. The phospholipid composition and cholesterol content of MPs and membrane fractions were analyzed by high performance thin layer chromatography. RESULTS: The phospholipid composition of MPs was intermediate compared with that of platelet plasma- and granule membranes, and differed significantly from that of intracellular membranes. There were small but significant differences in phospholipid composition between the MPs produced by the various agonists, which paralleled differences in P-selectin exposure in case of the physiological agonists collagen, thrombin, or collagen plus thrombin. The cholesterol content of MPs tended to be higher than that of the three-platelet membrane fractions. CONCLUSIONS: Regarding its phospholipid content, the MP membrane is a composite of the platelet plasma- and granule membranes, showing subtle differences depending on the platelet agonist. The higher cholesterol content of MPs suggests their enrichment in lipid rafts.

Blood Platelets↗