Arachidonic acid depletion extends survival of cold-stored platelets by interfering with the [glycoprotein Ib  - 14-3-3 ] association

Wal, Dianne E. van der; Gitz, Eelo; Du, Vivian X.; Lo, Kimberly; Koekman, Cornelis A.; Versteeg, Sabine; Akkerman, Jan Willem N.

doi:10.3324/haematol.2011.059956

Cited by 37 publications

(31 citation statements)

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“…Interestingly, both responses had normalized following 24 h in the circulation. These data suggest that the recovery of AA stores after prior depletion observed in vitro 9 also occurs in vivo. Thus, inhibition of GPIbα clustering prevents the cold-induced fall in platelet survival without compromising hemostatic functions.…”

Section: © F E R R a T A S T O R T I F O U N D A T I O Nmentioning

confidence: 48%

“…Cold incubation induced a 2.5-fold increase in [14-3-3ζ-GPIbα] complex, confirming earlier observations. 9 Lowering of endogenous AA completely abolished this increase. The same effect was seen in platelets treated with DANA ( Figure 5B).…”

Section: Binding Of 14-3-3ζ To the Cytoplasmic Tail Of Glycoprotein Imentioning

confidence: 99%

“…To investigate the contribution of 14-3-3ζ transfer to the GPIbα raft-and selfassociation, platelet AA content was lowered by incubation with fatty acid-free albumin (AA depletion, in short), as described in detail in an earlier report. 9 This treatment left [GPIbα-GM1] complex formation undisturbed but completely blocked formation of [GPIbα-GPIbα] complexes ( Figure 5A). Conversely, when normal platelets were incubated with exogenous AA, the [GPIbα-GM1] association remained unchanged but formation of a [GPIbα-GPIbα] complex increased significantly.…”

Section: Binding Of 14-3-3ζ To the Cytoplasmic Tail Of Glycoprotein Imentioning

confidence: 99%

“…9 The liberated AA then acts as a carrier for 14-3-3ζ transfer from multiple 14-3-3ζ-associated proteins to GPIbα. To investigate the contribution of 14-3-3ζ transfer to the GPIbα raft-and selfassociation, platelet AA content was lowered by incubation with fatty acid-free albumin (AA depletion, in short), as described in detail in an earlier report.…”

Section: Binding Of 14-3-3ζ To the Cytoplasmic Tail Of Glycoprotein Imentioning

confidence: 99%

“…Formation of a [14-3-3ζ-GPIbα] complex requires release of arachidonic acid (AA) from membrane phospholipids, which transfers 14-3-3ζ to the cytoplasmic tail of GPIbα. 9 AA is released by cytosolic phospholipase A 2 (cPLA 2 ) upon cold-activation of the stress kinase P38-mitogen-activated protein kinase (P38MAPK). 10 Cooling of platelet suspensions reveals the first signs of P38MAPK activation and [14-3-3ζ-GPIbα] association at 10ºC.…”

Section: Introductionmentioning

confidence: 99%

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Improved platelet survival after cold storage by prevention of glycoprotein Ib clustering in lipid rafts

et al. 2012

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The online version of this article has a Supplementary Appendix. BackgroundStoring platelets for transfusion at room temperature increases the risk of microbial infection and decreases platelet functionality, leading to out-date discard rates of up to 20%. Cold storage may be a better alternative, but this treatment leads to rapid platelet clearance after transfusion, initiated by changes in glycoprotein Ibα, the receptor for von Willebrand factor. Design and MethodsWe examined the change in glycoprotein Ibα distribution using Förster resonance energy transfer by time-gated fluorescence lifetime imaging microscopy. ResultsCold storage induced deglycosylation of glycoprotein Ibα ectodomain, exposing N-acetyl-Dglucosamine residues, which sequestered with GM1 gangliosides in lipid rafts. Raft-associated glycoprotein Ibα formed clusters upon binding of 14-3-3ζ adaptor proteins to its cytoplasmic tail, a process accompanied by mitochondrial injury and phosphatidyl serine exposure. Cold storage left glycoprotein Ibα surface expression unchanged and although glycoprotein V decreased, the fall did not affect glycoprotein Ibα clustering. Prevention of glycoprotein Ibα clustering by blockade of deglycosylation and 14-3-3ζ translocation increased the survival of cold-stored platelets to above the levels of platelets stored at room temperature without compromising hemostatic functions. ConclusionsWe conclude that glycoprotein Ibα translocates to lipid rafts upon cold-induced deglycosylation and forms clusters by associating with 14-3-3ζ. Interference with these steps provides a means to enable cold storage of platelet concentrates in the near future.Key words: platelets, cold storage, glycoprotein Ibα, 14-3-3ζ, lipid raft, clustering. Ibα clustering in lipid rafts. Haematologica 2012;97(12):1873-1881. doi:10.3324/haematol.2012 This is an open-access paper. Citation: Gitz E, Koekman CA, van den Heuvel DJ, Deckmyn H, Akkerman JW, Gerritsen HC and Urbanus RT. Improved platelet survival after cold storage by prevention of glycoprotein Improved platelet survival after cold storage by prevention of glycoprotein Ibα clustering in lipid rafts ABSTRACT© F e r r a t a S t o r t i F o u n d a t i o n

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Section: © F E R R a T A S T O R T I F O U N D A T I O Nmentioning

confidence: 48%

Section: Binding Of 14-3-3ζ To the Cytoplasmic Tail Of Glycoprotein Imentioning

confidence: 99%

Section: Binding Of 14-3-3ζ To the Cytoplasmic Tail Of Glycoprotein Imentioning

confidence: 99%

Section: Binding Of 14-3-3ζ To the Cytoplasmic Tail Of Glycoprotein Imentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Improved platelet survival after cold storage by prevention of glycoprotein Ib clustering in lipid rafts

et al. 2012

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Not all (N)SAID and done: Effects of nonsteroidal anti‐inflammatory drugs and paracetamol intake on platelets

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Wal

2020

Research and Practice in Thrombosis and Haemostasis

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This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made. AbstractPlatelets are key mediators of hemostasis and thrombosis and can be inhibited by nonsteroidal anti-inflammatory drugs (NSAIDs). As a result, platelet donors are temporarily deferred from donating if they have recently taken NSAIDs such as aspirin or ibuprofen. Despite these measures, a proportion of platelet donations show exposure to these drugs; however, little is known about the effect of NSAIDs and their metabolites on platelet quality in vivo and during storage. In this review, the effect of NSAIDs on platelet function is summarized, with a focus on the widely consumed over-the-counter (OTC) medications aspirin, ibuprofen, and the non-NSAID paracetamol. Aspirin and ibuprofen have well-defined antiplatelet effects. In comparison, studies regarding the effect of paracetamol on platelets report variable findings. The timing and order of NSAID intake is important, as concurrent NSAID use can inhibit or potentiate platelet activation depending on the drug taken. NSAID deferral periods and maximum platelet shelf-life is set by each country and are revised regularly. Reduced donor deferral periods and longer platelet storage times may affect the quality of platelet products, and it is therefore important to identify the possible impact of NSAID intake on platelet quality before and after storage. K E Y W O R D Sacetaminophen, anti-inflammatory agents, aspirin, blood platelets, ibuprofen, nonsteroidal Essentials• Nonsteroidal anti-inflammatory drugs (NSAIDs) can inhibit platelet aggregation and secretion by inhibiting cyclo-oxygenase 1.• The effect of paracetamol (acetaminophen) on platelets is poorly studied.• Little is known about the effect of NSAIDs and their metabolites on stored platelets.• Postponing platelet donation after NSAID intake may affect platelet quality following storage.

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Reversible thrombocytopenia during hibernation originates from storage and release of platelets in liver sinusoids

et al. 2021

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Immobility is a risk factor for thrombosis due to low blood flow, which may result in activation of the coagulation system, recruitment of platelets and clot formation. Nevertheless, hibernating animals—who endure lengthy periods of immobility—do not show signs of thrombosis throughout or after hibernation. One of the adaptations of hemostasis in hibernators consists of a rapidly reversible reduction of the number of circulating platelets during torpor, i.e., the hibernation phase with reduction of metabolic rate, low blood flow and immobility. It is unknown whether these platelet dynamics in hibernating hamsters originate from storage and release, as suggested for ground squirrel, or from breakdown and de novo synthesis. A reduction in detaching forces due to low blood flow can induce reversible adhesion of platelets to the vessel wall, which is called margination. Here, we hypothesized that storage-and-release by margination to the vessel wall induces reversible thrombocytopenia in torpor. Therefore, we transfused labeled platelets in hibernating Syrian hamster (Mesocricetus auratus) and platelets were analyzed using flow cytometry and electron microscopy. The half-life of labeled platelets was extended from 20 to 30 h in hibernating animals compared to non-hibernating control hamsters. More than 90% of labeled platelets were cleared from the circulation during torpor, followed by emergence during arousal which supports storage-and-release to govern thrombocytopenia in torpor. Furthermore, the low number of immature platelets, plasma level of interleukin-1α and normal numbers of megakaryocytes in bone marrow make platelet synthesis or megakaryocyte rupture via interleukin-1α unlikely to account for the recovery of platelet counts upon arousal. Finally, using large-scale electron microscopy we revealed platelets to accumulate in liver sinusoids, but not in spleen or lung, during torpor. These results thus demonstrate that platelet dynamics in hibernation are caused by storage and release of platelets, most likely by margination to the vessel wall in liver sinusoids. Translating the molecular mechanisms that govern platelet retention in the liver, may be of major relevance for hemostatic management in (accidental) hypothermia and for the development of novel anti-thrombotic strategies.

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Arachidonic acid depletion extends survival of cold-stored platelets by interfering with the [glycoprotein Ib - 14-3-3 ] association

Cited by 37 publications

References 62 publications

Improved platelet survival after cold storage by prevention of glycoprotein Ib clustering in lipid rafts

Improved platelet survival after cold storage by prevention of glycoprotein Ib clustering in lipid rafts

Not all (N)SAID and done: Effects of nonsteroidal anti‐inflammatory drugs and paracetamol intake on platelets

Reversible thrombocytopenia during hibernation originates from storage and release of platelets in liver sinusoids

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