Studies on the Histogenesis of Blood Platelets

Zajicek, J

doi:10.1159/000204625

Cited by 36 publications

(8 citation statements)

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“…DAMI cells express both AChE‐S and AChE‐R mRNA [25]. This strengthens the hypothesis that in all mammals, the precursor cell common to both megakaryocytic and erythropoietic lineages [100–102] expresses the ACHE gene. It appears that the transition of this bipotential precursor to developing MKs or erythroblasts involves species‐specific differential modulation of ACHE gene expression.…”

Section: Ache Involvement In Normal and Abnormal Hematopoiesissupporting

confidence: 68%

“…In humans, the erythrocyte membrane contains a prominent AChE activity [99], but there is no such activity in mature MKs. In contrast, rodents have a considerable MK and platelet AChE activity [100], but little in erythrocytes. This cell type discordance is even more extreme in cats, which have high platelet AChE but no erythrocyte AChE activity.…”

Section: Ache Involvement In Normal and Abnormal Hematopoiesismentioning

confidence: 99%

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Structural roles of acetylcholinesterase variants in biology and pathology

Grisaru

Sternfeld

Eldor

et al. 1999

European Journal of Biochemistry

323

226

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Apart from its catalytic function in hydrolyzing acetylcholine, acetylcholinesterase (AChE) affects cell proliferation, differentiation and responses to various insults, including stress. These responses are at least in part specific to the three C-terminal variants of AChE which are produced by alternative splicing of the single ACHE gene.`Synaptic' AChE-S constitutes the principal multimeric enzyme in brain and muscle; soluble, monomeric readthrough' AChE-R appears in embryonic and tumor cells and is induced under psychological, chemical and physical stress; and glypiated dimers of erythrocytic AChE-E associate with red blood cell membranes. We postulate that the homology of AChE to the cell adhesion proteins, gliotactin, glutactin and the neurexins, which have more established functions in nervous system development, is the basis of its morphogenic functions. Competition between AChE variants and their homologs on interactions with the corresponding protein partners would inevitably modify cellular signaling. This can explain why AChE-S exerts process extension from cultured amphibian, avian and mammalian glia and neurons in a manner that is C-terminus-dependent, refractory to several active site inhibitors and, in certain cases, redundant to the function of AChE-like proteins. Structural functions of AChE variants can explain their proliferative and developmental roles in blood, bone, retinal and neuronal cells. Moreover, the association of AChE excess with amyloid plaques in the degenerating human brain and with progressive cognitive and neuromotor deficiencies observed in AChE-transgenic animal models most likely reflects the combined contributions of catalytic and structural roles.

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Section: Ache Involvement In Normal and Abnormal Hematopoiesissupporting

confidence: 68%

Section: Ache Involvement In Normal and Abnormal Hematopoiesismentioning

confidence: 99%

Structural roles of acetylcholinesterase variants in biology and pathology

Grisaru

Sternfeld

Eldor

et al. 1999

European Journal of Biochemistry

323

226

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“…In humans, these cells are detected by the presence of platelet peroxidase [54-561 (which is visualized by electron microscopy), or by the expression of plateletlmegakaryocyte-specific antigens which allow detection by immunocytochemistry 157, 581. In the rat, mouse and a few other species, megakaryocytes express a relatively specific cytochemical marker, acetylcholinesterase [5 1,59,60]. Originally described the 1950s by Zajacek [59,60], this marker also identifies immature megakaryocytes [5 11 and allows their morphological classification into three subpopulations of cells ( Fig.…”

Section: Immature Megakaryocytes (Promegakaryoblasts)mentioning

confidence: 99%

“…In the rat, mouse and a few other species, megakaryocytes express a relatively specific cytochemical marker, acetylcholinesterase [5 1,59,60]. Originally described the 1950s by Zajacek [59,60], this marker also identifies immature megakaryocytes [5 11 and allows their morphological classification into three subpopulations of cells ( Fig. 1) [12, 49,501.…”

Section: Immature Megakaryocytes (Promegakaryoblasts)mentioning

confidence: 99%

Population heterogeneity among cells of the megakaryocyte lineage

Long

1993

STEM CELLS

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Understanding the developmental steps in megakaryocyte differentiation requires information regarding the microenvironmental influences which direct or permit the growth and differentiation of these cells. The megakaryocyte microenvironment, like other lineages, is a complex structure comprised of the various megakaryocytic cells, the extracellular matrix (ECM) surrounding them, and the hematopoietic stromal cells which elaborate both growth factors and ECM. As a result, definition of the minimal essential requirements for megakaryocyte development is difficult. The intricacies of megakaryocyte development are further complicated by the cellular heterogeneity of both mature megakaryocytes and their precursors, as well as a differential responsiveness of these cells to hematopoietic growth factors. This review focuses on defining the various subpopulations of megakaryocytic cells and examining their functional distinctions and in vitro responsiveness to various stimuli.

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“…Therefore, detection methods had to be modified cyte AChE activity. 11 Therefore, Zajicek 12 postulated that in and improved. Second, we wished to search for this enzyme mammals this enzyme is distributed in an inverse order bein subcellular compartments where it had not been seen between erythrocytes and platelets.…”

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confidence: 99%

Immature Human Megakaryocytes Produce Nuclear-Associated Acetylcholinesterase

Lev-Lehman

Deutsch

Eldor

et al. 1997

Blood

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Acetylcholinesterase (AChE) is expressed in murine megakaryocytes (MK), where its antisense inhibition suppresses differentiation, yet was never detected in human MK. Here, we report that AChE is produced in normal human bone marrow MK and in cell lines derived thereof. Reverse transcriptase-polymerase chain reaction (RT-PCR) amplification showed two ACHEmRNA forms in human megakaryoblastic DAMI cells. In situ hybridization demonstrated ACHEmRNA surrounding the nucleus of small DAMI cells and the nuclear lobes of large, polyploid cells. Differentiation induction with phorbol ester and exposure to recombinant human thrombopoietin suppressed both ACHEmRNA and AChE activity. The residual AChE in mature differentiated cells acquired higher stability and detergent-sensitivity as compared with AChE in small proliferating cells. AChE activity was primarily associated with nuclei of both DAMI cells and small (10 μm) primary proliferating human bone marrow MK identified with GPIIb/IIIa antibodies. This activity was significantly reduced in medium size MK (10 to 25 μm) and was almost undetectable in large MK (<25 μm), yet was twofold more abundant in some large MK from idiopathic thrombocytopenia purpura (ITP) patients with accelerated MK maturation. The loss of AChE activity at the transition from proliferating to differentiating MK highlights species-specific differences in its expression, suggesting a distinct role for AChE in human MK development.

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Studies on the Histogenesis of Blood Platelets

Cited by 36 publications

References 1 publication

Structural roles of acetylcholinesterase variants in biology and pathology

Structural roles of acetylcholinesterase variants in biology and pathology

Population heterogeneity among cells of the megakaryocyte lineage

Immature Human Megakaryocytes Produce Nuclear-Associated Acetylcholinesterase

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