Thrombocyte

Résumé

thumb|300px|De gauche à droite : érythrocyte (globule rouge), thrombocyte activé (noter les spiculations) (plaquette), leucocyte (globule blanc), en microscopie électronique à balayage en fausse couleur. Un thrombocyte (du grec thrombôsis, dérivé du verbe thromboûn : faire coaguler et de kytos : enveloppe) ou plaquette sanguine est un élément figuré du sang, formé par fragmentation des mégacaryocytes, grandes cellules contenues dans la moelle osseuse. Les thrombocytes ne sont donc en fait pas des cellules complètes mais uniquement de petits fragments. Ceux-ci sont dépourvus de noyau chez les mammifères, mais sont nucléés chez les oiseaux. Leur durée de vie est d'environ 8 à 12 jours dans le compartiment sanguin. Le lieu de dégradation des thrombocytes est la rate. Elles sont un des composants indispensables à l'hémostase primaire. Ultrastructure Ce sont les plus petits éléments figurés du sang. Les thrombocytes ne sont pas des cellules à proprement parler ; il s'agit de f

Source officielle

https://fr.wikipedia.org/wiki/Thrombocyte

À propos de ce résultat

Cette page est générée automatiquement et peut contenir des informations qui ne sont pas correctes, complètes, à jour ou pertinentes par rapport à votre recherche. Il en va de même pour toutes les autres pages de ce site. Veillez à vérifier les informations auprès des sources officielles de l'EPFL.

Publications associées (34)

Publications associées

Chargement

Personnes associées (3)

Personnes associées

Chargement

Unités associées (2)

Unités associées

Chargement

Concepts associés (133)

Concepts associés

Chargement

Cours associés (9)

Cours associés

Chargement

Séances de cours associées (14)

Séances de cours associées

Chargement

Atroxlysin-III (Atr-III) was purified from the venom of Bothrops atrox. This 56-kDa protein bears N-linked glycoconjugates and is a P-III hemorrhagic metalloproteinase. Its cDNA-deduced amino acid sequence reveals a multidomain structure including a proprotein, a metalloproteinase, a disintegrin-like and a cysteine-rich domain. Its identity with bothropasin and jararhagin from Bothrops jararaca is 97% and 95%, respectively. Its enzymatic activity is metal ion-dependent. The divalent cations, Mg2+ and Ca2+, enhance its activity, whereas excess Zn2+ inhibits it. Chemical modification of the Zn2+-complexing histidine residues within the active site by using diethylpyrocarbonate (DEPC) inactivates it. Atr-III degrades plasma fibronectin, type I-collagen, and mainly the alpha-chains of fibrinogen and fibrin. The von Willebrand factor (vWF) A1-domain, which harbors the binding site for GPIb, is not hydrolyzed. Platelets interact with collagen via receptors for collagen, glycoprotein VI (GPVI), and alpha 2 beta 1 integrin. Neither the alpha 2 beta 1 integrin nor its collagen-binding A-domain is fragmented by Atr-III. In contrast, Atr-III cleaves glycoprotein VI (GPVI) into a soluble similar to 55-kDa fragment (sGPVI). Thereby, it inhibits aggregation of platelets which had been stimulated by convulxin, a GPVI agonist. Selectively, Atr-III targets GPVI antagonistically and thus contributes to the antithrombotic effect of envenomation by Bothrops atrox.

2019

Chargement

Standardization and Validation of Fluorescence-Based Quantitative Assay to Study Human Platelet Adhesion to Extracellular-Matrix in a 384-Well Plate

François Cuenot, Cindy Marie Elodie Khawand, Tom Yohan Abraham Lachkar, Augusto Martins Lima, Damian Salim Saint Auguste, Nikolaos Stergiopulos

Platelets play a crucial role in the immunological response and are involved in the pathological settings of vascular diseases, and their adhesion to the extracellular matrix is important to bring leukocytes close to the endothelial cells and to form and stabilize the thrombus. Currently there are several methods to study platelet adhesion; however, the optimal parameters to perform the assay vary among studies, which hinders their comparison and reproducibility. Here, a standardization and validation of a fluorescence-based quantitative adhesion assay to study platelet-ECM interaction in a high-throughput screening format is proposed. Our study confirms that fluorescence-based quantitative assays can be effectively used to detect platelet adhesion, in which BCECF-AM presents the highest sensitivity in comparison to other dyes.

2020

Chargement

The May-Hegglin anomaly gene MYH9 is a negative regulator of platelet biogenesis modulated by the Rho-ROCK pathway

Zhao Chen, Olaia Maria Naveiras Torres-Quiroga

The gene implicated in the May-Hegglin anomaly and related macrothrombocytopenias, MYH9, encodes myosin-IIA, a protein that enables morphogenesis in diverse cell types. Defective myosin-IIA complexes are presumed to perturb megakaryocyte (MK) differentiation or generation of proplatelets. We observed that Myh9(-/-) mouse embryonic stem (ES) cells differentiate into MKs that are fully capable of proplatelet formation (PPF). In contrast, elevation of myosin-IIA activity, by exogenous expression or by mimicking constitutive phosphorylation of its regulatory myosin light chain (MLC), significantly attenuates PPF. This effect occurs only in the presence of myosin-IIA and implies that myosin-IIA influences thrombopoiesis negatively. MLC phosphorylation in MKs is regulated by Rho-associated kinase (ROCK), and consistent with our model, ROCK inhibition enhances PPF. Conversely, expression of AV14, a constitutive form of the ROCK activator Rho, blocks PPF, and this effect is rescued by simultaneous expression of a dominant inhibitory MLC form. Hematopoietic transplantation studies in mice confirm that interference with the putative Rho-ROCK-myosin-IIA pathway selectively decreases the number of circulating platelets. Our studies unveil a key regulatory pathway for platelet biogenesis and hint at Sdf-1/CXCL12 as one possible extracellular mediator. The unexpected mechanism for Myh9-associated thrombocytopenia may lead to new molecular approaches to manipulate thrombopoiesis.

American Society of Hematology2007

Chargement