Mast Cell and Myeloid Marker Expression During Early In Vitro Mast Cell Differentiation from Human Peripheral Blood Mononuclear Cells

Welker, Pia; Grabbe, Jürgen; Zuberbier, Torsten; Guhl, Sven; Henz, Beate M.

doi:10.1046/j.1523-1747.2000.00827.x

Cited by 36 publications

(38 citation statements)

References 63 publications

(65 reference statements)

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“…Furthermore, it supports the observation that in mature mast cells, CD34 is differentially regulated in mice and humans, [4][5][6] and suggests that the hCD34 locus lacks key control elements that are present in the murine gene and are required for maintenance of CD34 expression in mature cells of this lineage.…”

Section: Cd34 Expression By Mast Cells: Of Mice and Mensupporting

confidence: 76%

“…A caveat to these observations is the fact that, in humans, CD34 expression is lost upon mast-cell differentiation. [4][5][6] To gain further insights into this discrepancy between mouse and human CD34 (hCD34) regulation, we examined the expression of the human CD34 gene in murine mast cells derived from transgenic mice harboring a 160-kilobase (kb) genomic DNA fragment spanning the hCD34 coding exons, promoter elements, 110 kb of 5Ј upstream sequence and 30 kb of 3Ј downstream flanking (hCD34tg). 7 These mice have proved extremely useful for studying hCD34 gene regulation, since they faithfully recapitulate the normal pattern of hCD34 mRNA expression by vascular endothelia and bone marrow progenitor cells in the murine tissues.…”

Section: Cd34 Expression By Mast Cells: Of Mice and Menmentioning

confidence: 99%

“…As all of the observed GATA1 mutations result in the same truncated protein, 6,7 it is unlikely that individual mutations could determine the degree of differentiation arrest or the propensity for proliferation. Therefore, the observation that proliferating blasts bearing different GATA1 mutations are detected at different stages of megakaryocytic differentiation may possibly be explained by independent clones that vary in their stage of differentiation at the time of acquisition of their respective mutations, or by further differentiation of the proliferating clone occurring despite these mutations, which occurred at some distance apart during fetal development.…”

Section: To the Editormentioning

confidence: 99%

“…Surprisingly, when the free-thrombin concentrations present in plasma were calculated using the Michaelis-Menten constant (K m ) and substrate concentrations, superimposable thrombin generation curves (free thrombin versus time) were obtained. 5 This indicates that the generation of thrombin hardly depends on the action of thrombin but that another component is rate limiting, namely factor Xa, 6 and that the presence of the substrate has virtually no effect on the mechanism of prothrombin activation. 5 We agree with Dr Mann that there are ample differences between our reaction conditions and the natural environment in which protein S acts.…”

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confidence: 99%

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CD34 expression by mast cells: of mice and men

Drew¹,

Huettner²,

Tenen³

et al. 2005

Blood

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calcium by sodium citrate used as an anticoagulant with blood collection. However, protein-S dimerization occurs at concentrations far above the plasma concentration: "at 17 M, the associated product is principally a dimer." 2 Inspection of Figure 5 of the paper by Pauls et al 2 indicates that, at the free protein-S concentration present in plasma (ϳ 150 nM), protein S is principally a monomer.In spite of this, Dr Mann believes that inhibitory protein-S dimers are present at the start of our experiments, and that slow depolymerization of these dimers after recalcification of plasma invalidated our conclusions. 1 We refuted this possibility by recalcifying the plasma 15 minutes before initiation of thrombin generation with tissue factor/phospholipid. This provided ample time for the Ca 2ϩ -induced conformational changes of vitamin-K-dependent proteins to occur, and for depolymerization of protein-S dimers if present. Figure 1 shows that after "pre"-recalcification of plasma the activated protein C (APC)-independent inhibitory effect of protein S on thrombin generation prevailed.The endogenous thrombin potentials (ETPs) determined in the absence of functional protein S were similar without and with preincubation of plasma with CaCl 2 (Figure 1). In the presence of protein S (Figure 1 open symbols), the ETP determined in plasma preincubated with CaCl 2 (521 nM thrombin min) was even lower than the ETP of plasma that was not preincubated with CaCl 2 (659 nM thrombin min). Protein S decreased the ETP in freshly recalcified citrated plasma by 30%, compared with 40% when plasma was preincubated with CaCl 2 , and thus became an even better inhibitor of thrombin generation. Moreover, if protein-S dimers in citrated plasma had caused the observed phenomena, the inhibitory effect of protein S on thrombin generation would have been abrogated at high phospholipid concentrations. 2 However, increasing phospholipid concentrations did not affect the anticoagulant potential of protein S in plasma. 1 This demonstrates that the inhibition of thrombin formation by protein S in plasma is not due to competition for phospholipid binding sites.Dr Mann raised an important point regarding the effect of the thrombin substrate on thrombin generation. Indeed, it has been shown that the measured ETP increases with increasing substrate concentrations, 5 likely due to the fact that the substrate protects thrombin against inhibition by antithrombins. However, it should be emphasized that only free thrombin (ie, thrombin that is not occupied by substrate) will be available for feedback reactions. Surprisingly, when the free-thrombin concentrations present in plasma were calculated using the Michaelis-Menten constant (K m ) and substrate concentrations, superimposable thrombin generation curves (free thrombin versus time) were obtained. 5 This indicates that the generation of thrombin hardly depends on the action of thrombin but that another component is rate limiting, namely factor Xa, 6 and that the presence of the substrate has virtually no ...

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Section: Cd34 Expression By Mast Cells: Of Mice and Mensupporting

confidence: 76%

Section: Cd34 Expression By Mast Cells: Of Mice and Menmentioning

confidence: 99%

Section: To the Editormentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

CD34 expression by mast cells: of mice and men

Drew¹,

Huettner²,

Tenen³

et al. 2005

Blood

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show abstract

“…SCF is involved in the early phases of hematopoiesis (de Vries et al 1991, Brandt et al 1992) (for review, see Galli et al 1994, Broudy 1997. In particular, this growth factor also acts as an important growth factor for human and murine mast cells (Galli et al 1994, 1995, Broudy 1997, including in vitro proliferation and differentiation of immature CD34 + progenitors into mast cells in the bone marrow (Kirshenbaum et al 1992), and in peripheral blood (Rottem et al 1994, Welker et al 2000.…”

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confidence: 99%