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Article ; Online: Low-dose Btk inhibitors: an 'aspirin' of tomorrow?

Payrastre, Bernard / Ribes, Agnès

2021 Volume 106, Issue 1, Page(s) 2–4

MeSH term(s)	Agammaglobulinaemia Tyrosine Kinase ; Aspirin ; Humans ; Lectins, C-Type ; Platelet Activation ; Protein Kinase Inhibitors
Chemical Substances	Lectins, C-Type ; Protein Kinase Inhibitors ; Agammaglobulinaemia Tyrosine Kinase (EC 2.7.10.2) ; Aspirin (R16CO5Y76E)
Language	English
Publishing date	2021-01-01
Publishing country	Italy
Document type	Editorial ; Comment
ZDB-ID	2333-4
ISSN	1592-8721 ; 0017-6567 ; 0390-6078
ISSN (online)	1592-8721
ISSN	0017-6567 ; 0390-6078
DOI	10.3324/haematol.2020.265173
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Article ; Online: SHIP1 Controls Internal Platelet Contraction and α

Severin, Sonia / Consonni, Alessandra / Chicanne, Gaëtan / Allart, Sophie / Payrastre, Bernard / Gratacap, Marie-Pierre

International journal of molecular sciences

2023 Volume 24, Issue 2

Abstract: The Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP1) is known to dephosphorylate PtdIns(3,4,5) ... ...

Abstract	The Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP1) is known to dephosphorylate PtdIns(3,4,5)P
MeSH term(s)	Blood Platelets/metabolism ; Integrin beta3/metabolism ; Phosphatidylinositols/metabolism ; Platelet Activation ; Platelet Glycoprotein GPIIb-IIIa Complex/metabolism ; Thrombin/pharmacology ; Thrombin/metabolism ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases/metabolism ; Integrin alpha2/metabolism
Chemical Substances	Integrin beta3 ; Phosphatidylinositols ; Platelet Glycoprotein GPIIb-IIIa Complex ; Thrombin (EC 3.4.21.5) ; Inpp5d protein, mouse (EC 3.1.3.86) ; Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases (EC 3.1.3.86) ; Integrin alpha2
Language	English
Publishing date	2023-01-04
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24020958
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Article ; Online: SARS-CoV-2 Omicron variant infection affects blood platelets, a comparative analysis with Delta variant.

Garcia, Cédric / Compagnon, Baptiste / Ribes, Agnès / Voisin, Sophie / Vardon-Bounes, Fanny / Payrastre, Bernard

Frontiers in immunology

2023 Volume 14, Page(s) 1231576

Abstract: Introduction: In November 2021, the SARS-CoV-2 Omicron variant of concern has emerged and is currently dominating the COVID-19 pandemic over the world. Omicron displays a number of mutations, particularly in the spike protein, leading to specific ... ...

Abstract	Introduction: In November 2021, the SARS-CoV-2 Omicron variant of concern has emerged and is currently dominating the COVID-19 pandemic over the world. Omicron displays a number of mutations, particularly in the spike protein, leading to specific characteristics including a higher potential for transmission. Although Omicron has caused a significant number of deaths worldwide, it generally induces less severe clinical signs compared to earlier variants. As its impact on blood platelets remains unknown, we investigated platelet behavior in severe patients infected with Omicron in comparison to Delta. Methods: Clinical and biological characteristics of severe COVID-19 patients infected with the Omicron (n=9) or Delta (n=11) variants were analyzed. Using complementary methods such as flow cytometry, confocal imaging and electron microscopy, we examined platelet activation, responsiveness and phenotype, presence of virus in platelets and induction of selective autophagy. We also explored the direct effect of spike proteins from the Omicron or Delta variants on healthy platelet signaling. Results: Severe Omicron variant infection resulted in platelet activation and partial desensitization, presence of the virus in platelets and selective autophagy response. The intraplatelet processing of Omicron viral cargo was different from Delta as evidenced by the distribution of spike protein-positive structures near the plasma membrane and the colocalization of spike and Rab7. Moreover, spike proteins from the Omicron or Delta variants alone activated signaling pathways in healthy platelets including phosphorylation of AKT, p38MAPK, LIMK and SPL76 with different kinetics. Discussion: Although SARS-CoV-2 Omicron has different biological characteristics compared to prior variants, it leads to platelet activation and desensitization as previously observed with the Delta variant. Omicron is also found in platelets from severe patients where it induces selective autophagy, but the mechanisms of intraplatelet processing of Omicron cargo, as part of the innate response, differs from Delta, suggesting that mutations on spike protein modify virus to platelet interactions.
MeSH term(s)	Humans ; Blood Platelets ; SARS-CoV-2 ; Spike Glycoprotein, Coronavirus/genetics ; Pandemics ; COVID-19
Chemical Substances	Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2
Language	English
Publishing date	2023-09-27
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2023.1231576
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Article ; Online: What can we learn from the platelet lipidome?

Chicanne, Gaëtan / Darcourt, Jean / Bertrand-Michel, Justine / Garcia, Cédric / Ribes, Agnès / Payrastre, Bernard

Platelets

2023 Volume 34, Issue 1, Page(s) 2182180

Abstract: Besides their proteome, platelets use, in all responses to the environmental cues, a huge and diverse family of hydrophobic and amphipathic small molecules involved in structural, metabolic and signaling functions; the lipids. Studying how platelet ... ...

Abstract	Besides their proteome, platelets use, in all responses to the environmental cues, a huge and diverse family of hydrophobic and amphipathic small molecules involved in structural, metabolic and signaling functions; the lipids. Studying how platelet lipidome changes modulate platelet function is an old story constantly renewed through the impressive technical advances allowing the discovery of new lipids, functions and metabolic pathways. Technical progress in analytical lipidomic profiling by top-of-the-line approaches such as nuclear magnetic resonance and gas chromatography or liquid chromatography coupled to mass spectrometry enables either large-scale analysis of lipids or targeted lipidomics. With the support of bioinformatics tools and databases, it is now possible to investigate thousands of lipids over a concentration range of several orders of magnitude. The lipidomic landscape of platelets is considered a treasure trove, not only able to expand our knowledge of platelet biology and pathologies but also to bring diagnostic and therapeutic opportunities. The aim of this commentary article is to summarize the advances in the field and to highlight what lipidomics can tell us about platelet biology and pathophysiology.
MeSH term(s)	Humans ; Lipidomics ; Blood Platelets ; Chromatography, Liquid ; Computational Biology ; Lipids
Chemical Substances	Lipids
Language	English
Publishing date	2023-02-22
Publishing country	England
Document type	Journal Article
ZDB-ID	1034283-7
ISSN	1369-1635 ; 0953-7104
ISSN (online)	1369-1635
ISSN	0953-7104
DOI	10.1080/09537104.2023.2182180
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Article: Strengths and Weaknesses of Light Transmission Aggregometry in Diagnosing Hereditary Platelet Function Disorders.

Alessi, Marie-Christine / Sié, Pierre / Payrastre, Bernard

Journal of clinical medicine

2020 Volume 9, Issue 3

Abstract: Hereditary defects in platelet function are responsible for sometimes severe mucocutaneous hemorrhages. They are a heterogeneous group of abnormalities whose first-line diagnosis typically involves interpreting the results of in vitro light transmission ... ...

Abstract	Hereditary defects in platelet function are responsible for sometimes severe mucocutaneous hemorrhages. They are a heterogeneous group of abnormalities whose first-line diagnosis typically involves interpreting the results of in vitro light transmission aggregometry (LTA) traces. Interpretation of LTA is challenging. LTA is usually performed in specialized laboratories with expertise in platelet pathophysiology. This review updates knowledge on LTA, describing the various platelet aggregation profiles typical of hereditary platelet disorders to guide the physician in the diagnosis of functional platelet disorders.
Language	English
Publishing date	2020-03-12
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2662592-1
ISSN	2077-0383
ISSN	2077-0383
DOI	10.3390/jcm9030763
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Article ; Online: Foreword for the special issue advances in COVID-19: Biology and clinic.

McCubrey, James A / Akula, Shaw M / Payrastre, Bernard

Advances in biological regulation

2020 Volume 77, Page(s) 100744

MeSH term(s)	Anticoagulants/therapeutic use ; Antiviral Agents/therapeutic use ; Betacoronavirus/pathogenicity ; COVID-19 ; Comorbidity ; Coronavirus Infections/diagnosis ; Coronavirus Infections/drug therapy ; Coronavirus Infections/epidemiology ; Coronavirus Infections/transmission ; Cytokine Release Syndrome/diagnosis ; Cytokine Release Syndrome/drug therapy ; Cytokine Release Syndrome/epidemiology ; Cytokine Release Syndrome/mortality ; Disseminated Intravascular Coagulation/diagnosis ; Disseminated Intravascular Coagulation/drug therapy ; Disseminated Intravascular Coagulation/epidemiology ; Disseminated Intravascular Coagulation/mortality ; Humans ; Lung/blood supply ; Lung/drug effects ; Lung/pathology ; Lung/virology ; Pandemics ; Pneumonia, Viral/diagnosis ; Pneumonia, Viral/drug therapy ; Pneumonia, Viral/epidemiology ; Pneumonia, Viral/transmission ; Pulmonary Embolism/diagnosis ; Pulmonary Embolism/drug therapy ; Pulmonary Embolism/epidemiology ; Pulmonary Embolism/mortality ; Respiratory Insufficiency/diagnosis ; Respiratory Insufficiency/drug therapy ; Respiratory Insufficiency/epidemiology ; Respiratory Insufficiency/mortality ; SARS-CoV-2 ; Survival Analysis ; Trace Elements/therapeutic use ; Vitamins/therapeutic use
Chemical Substances	Anticoagulants ; Antiviral Agents ; Trace Elements ; Vitamins
Keywords	covid19
Language	English
Publishing date	2020-07-09
Publishing country	England
Document type	Editorial
ZDB-ID	2667413-0
ISSN	2212-4934 ; 2212-4926
ISSN (online)	2212-4934
ISSN	2212-4926
DOI	10.1016/j.jbior.2020.100744
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Article ; Online: Liposome-Based Methods to Study GTPase Activation by Phosphoinositides.

Viaud, Julien / Ceccato, Laurie / Payrastre, Bernard / Gaits-Iacovoni, Frédérique

Methods in molecular biology (Clifton, N.J.)

2021 Volume 2251, Page(s) 185–194

Abstract: Phosphoinositides (PIPs) are lipid messengers with different functions according to their localization. After their local production by the action of lipid kinases or phosphatases, PIPs regulate various biological processes such as cytoskeleton ... ...

Abstract	Phosphoinositides (PIPs) are lipid messengers with different functions according to their localization. After their local production by the action of lipid kinases or phosphatases, PIPs regulate various biological processes such as cytoskeleton rearrangement, membrane remodeling/trafficking, or gene expression through binding of their phosphorylated inositol head group with different protein domains such as PH, PX, and FYVE. It is well known that PIPs regulate the activity of small GTPases by interacting with and activating Guanyl-nucleotide Exchange Factor (GEF) proteins through specific domains such as the ones mentioned above. However, most of the in vitro assays to assess the activation of GTPases focus on the GTPase only and neglect the fact that co-activators, such as membranes and protein activators, have a significant effect in vivo. Herein, we describe not only the classical protein-lipid overlay and liposome sedimentation methods but also an assay we have developed, which contains three partners: a liposome which composition reproduces the membrane of the target of the GTPase, the recombinant specific DH-(PIP affinity) GEF domain, and the recombinant GTPase to be tested by different PIPs. This assay allows us to clearly quantify the GTPase activation.
MeSH term(s)	3T3 Cells ; Animals ; GTP Phosphohydrolase Activators/metabolism ; GTP Phosphohydrolases/metabolism ; Guanine Nucleotide Exchange Factors/metabolism ; Humans ; Liposomes/analysis ; Liposomes/metabolism ; Mice ; Monomeric GTP-Binding Proteins/metabolism ; Phosphatidylinositols/analysis ; Phosphatidylinositols/metabolism ; Phosphorylation ; Protein Binding/physiology ; Protein Domains/physiology ; Protein Interaction Mapping/methods ; Proteins/chemistry ; Signal Transduction/physiology ; rhoA GTP-Binding Protein/metabolism
Chemical Substances	GTP Phosphohydrolase Activators ; Guanine Nucleotide Exchange Factors ; Liposomes ; Phosphatidylinositols ; Proteins ; GTP Phosphohydrolases (EC 3.6.1.-) ; Monomeric GTP-Binding Proteins (EC 3.6.5.2) ; rhoA GTP-Binding Protein (EC 3.6.5.2)
Language	English
Publishing date	2021-01-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-1142-5_13
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Article ; Online: Exploring the Role of PI3P in Platelets: Insights from a Novel External PI3P Pool.

Mujalli, Abdulrahman / Viaud, Julien / Severin, Sonia / Gratacap, Marie-Pierre / Chicanne, Gaëtan / Hnia, Karim / Payrastre, Bernard / Terrisse, Anne-Dominique

Biomolecules

2023 Volume 13, Issue 4

Abstract: Phosphoinositides (PIs) play a crucial role in regulating intracellular signaling, actin cytoskeleton rearrangements, and membrane trafficking by binding to specific domains of effector proteins. They are primarily found in the membrane leaflets facing ... ...

Abstract	Phosphoinositides (PIs) play a crucial role in regulating intracellular signaling, actin cytoskeleton rearrangements, and membrane trafficking by binding to specific domains of effector proteins. They are primarily found in the membrane leaflets facing the cytosol. Our study demonstrates the presence of a pool of phosphatidylinositol 3-monophosphate (PI3P) in the outer leaflet of the plasma membrane of resting human and mouse platelets. This pool of PI3P is accessible to exogenous recombinant myotubularin 3-phosphatase and ABH phospholipase. Mouse platelets with loss of function of class III PI 3-kinase and class II PI 3-kinase α have a decreased level of external PI3P, suggesting a contribution of these kinases to this pool of PI3P. After injection in mouse, or incubation ex vivo in human blood, PI3P-binding proteins decorated the platelet surface as well as α-granules. Upon activation, these platelets were able to secrete the PI3P-binding proteins. These data sheds light on a previously unknown external pool of PI3P in the platelet plasma membrane that recognizes PI3P-binding proteins, leading to their uptake towards α-granules. This study raises questions about the potential function of this external PI3P in the communication of platelets with the extracellular environment, and its possible role in eliminating proteins from the plasma.
MeSH term(s)	Mice ; Humans ; Animals ; Blood Platelets/metabolism ; Cell Membrane/metabolism ; Carrier Proteins/metabolism ; Phosphatidylinositol 3-Kinases/metabolism
Chemical Substances	Carrier Proteins ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-)
Language	English
Publishing date	2023-03-24
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2701262-1
ISSN	2218-273X ; 2218-273X
ISSN (online)	2218-273X
ISSN	2218-273X
DOI	10.3390/biom13040583
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Article ; Online: Inactivating the lipid kinase activity of PI3KC2β is sufficient to rescue myotubular myopathy in mice.

Massana-Muñoz, Xènia / Goret, Marie / Nattarayan, Vasugi / Reiss, David / Kretz, Christine / Chicanne, Gaetan / Payrastre, Bernard / Vanhaesebroeck, Bart / Laporte, Jocelyn

JCI insight

2023 Volume 8, Issue 9

Abstract: Phosphoinositides (PIs) are membrane lipids that regulate signal transduction and vesicular trafficking. X-linked centronuclear myopathy (XLCNM), also called myotubular myopathy, results from loss-of-function mutations in the MTM1 gene, which encodes the ...

Abstract	Phosphoinositides (PIs) are membrane lipids that regulate signal transduction and vesicular trafficking. X-linked centronuclear myopathy (XLCNM), also called myotubular myopathy, results from loss-of-function mutations in the MTM1 gene, which encodes the myotubularin phosphatidylinositol 3-phosphate (PtdIns3P) lipid phosphatase. No therapy for this disease is currently available. Previous studies showed that loss of expression of the class II phosphoinositide 3-kinase (PI3K) PI3KC2β (PI3KC2B) protein improved the phenotypes of an XLCNM mouse model. PI3Ks are well known to have extensive scaffolding functions and the importance of the catalytic activity of this PI3K for rescue remains unclear. Here, using PI3KC2β kinase-dead mice, we show that the selective inactivation of PI3KC2β kinase activity is sufficient to fully prevent muscle atrophy and weakness, histopathology, and sarcomere and triad disorganization in Mtm1-knockout mice. This rescue correlates with normalization of PtdIns3P level and mTORC1 activity, a key regulator of protein synthesis and autophagy. Conversely, lack of PI3KC2β kinase activity did not rescue the histopathology of the BIN1 autosomal CNM mouse model. Overall, these findings support the development of specific PI3KC2β kinase inhibitors to cure myotubular myopathy.
MeSH term(s)	Animals ; Mice ; Phosphatidylinositol 3-Kinases/genetics ; Phosphatidylinositols ; Mutation ; Mice, Knockout ; Myopathies, Structural, Congenital/genetics ; Myopathies, Structural, Congenital/pathology
Chemical Substances	Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Phosphatidylinositols
Language	English
Publishing date	2023-05-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2379-3708
ISSN (online)	2379-3708
DOI	10.1172/jci.insight.151933
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Article ; Online: Platelet P2Y

Ribes, Agnès / Garcia, Cédric / Gratacap, Marie-Pierre / Kostenis, Evi / Martinez, Laurent O / Payrastre, Bernard / Sénard, Jean-Michel / Galés, Céline / Pons, Véronique

BMC biology

2023 Volume 21, Issue 1, Page(s) 14

Abstract: Background: Purinergic P2Y: Results: Here, we investigated the pharmacology of P2Y: Conclusions: This study sheds new light on ... ...

Abstract	Background: Purinergic P2Y Results: Here, we investigated the pharmacology of P2Y Conclusions: This study sheds new light on P2Y
MeSH term(s)	Animals ; Humans ; Mice ; beta-Arrestin 2/metabolism ; Drug Inverse Agonism ; GTP-Binding Proteins/metabolism ; HEK293 Cells ; Signal Transduction ; Receptors, Purinergic P2Y1/metabolism ; Blood Platelets
Chemical Substances	beta-Arrestin 2 ; GTP-Binding Proteins (EC 3.6.1.-) ; Receptors, Purinergic P2Y1
Language	English
Publishing date	2023-02-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2133020-7
ISSN	1741-7007 ; 1741-7007
ISSN (online)	1741-7007
ISSN	1741-7007
DOI	10.1186/s12915-023-01528-y
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