Thrombopoietin: a pan-hematopoietic cytokine

TL;DR: These studies have shown that it is possible to identify thrombocytes,Thrombocyte precursors, and, possibly, early hematopoietic stem cells in zebrafish embryos and track their proliferation and maturation.

TL;DR: In this article, the authors have cloned zebrafish CD41 cDNA (α IIb, glycoprotein IIb [GPllb]) and its promoter and generated transgeniczebrafish lines with green fluorescent protein (GFP)-tagged thrombocytes.

TL;DR: Data suggest that Akt signaling modulates the SP cell phenotype by regulating the expression of Bcrp1, which encodes the Hoechst dye transporter, which was translocated from the membrane to the intracellular compartment under conditions that promote the SP-depleted state.

TL;DR: The proposed concept is that platelets in thrombocythemia (ET and PV) are hypersensitive and spontaneously activate, secrete their products, form aggregates mediated by von Willebrand factor (vWF) that transiently plug the microcirculation, deaggregate, and then recirculate as exhausted defective platelets with secondary storage pool disease on ex vivo analysis.

TL;DR: Although the use of PP inhibitors shows that there is significant basal PP activity in cells, it has become apparent that the activities of PPs are regulated in a sophisticated manner by a combination of targeting and regulatory subunits and by specific inhibitors.

TL;DR: The prospective identification, purification and characterization, using cell-surface markers and flow cytometry, of a complementary clonogenic common myeloid progenitor that gives rise to all myeloids lineages is reported.

TL;DR: The Lin(-)IL-7R(+)Thy-1(-)Sca-1loc-Kit(lo) population from adult mouse bone marrow possessed a rapid lymphoid-restricted (T, B, and NK) reconstitution capacity in vivo but completely lacked myeloid differentiation potential either in vivo or in vitro.

TL;DR: The proapoptotic function of BAD is regulated by the PI 3-kinase-Akt pathway, and active, but not inactive, forms of Akt were found to phosphorylate BAD in vivo and in vitro at the same residues that are phosphorylated in response to IL-3.