| 1. |
- Egesten, Arne, et al.
(författare)
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The heterogeneity of azurophil granules in neutrophil promyelocytes: immunogold localization of myeloperoxidase, cathepsin G, elastase, proteinase 3, and bactericidal/permeability increasing protein
- 1994
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Ingår i: Blood. - 1528-0020. ; 83:10, s. 94-2985
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Tidskriftsartikel (refereegranskat)abstract
- Azurophil granules of myeloid cells form in promyelocytes. They store cytotoxic and digestive agents which when released are involved in the defense against infection. In order to characterize the intragranular distribution of these agents, ultrastructural methods using immunogold were used on promyelocytes. Azurophil granules were divided into nucleated, large spherical (large azurophil) and small electron-dense (small azurophil) granules. Myeloperoxidase showed a peripheral distribution of large azurophils and a uniform distribution of small and nucleated azurophils, consistent with previous findings. Likewise, the major neutral proteases of azurophils, cathepsin G, granulocyte elastase, and proteinase 3, displayed a similar distribution, with a peripheral localization in large azurophils and a uniform distribution in small and nucleated azurophils, except for proteinase 3, which was associated with the crystalloid structure in nucleated azurophils. In contrast, the bactericidal/permeability increasing protein, which is bacteristatic and bactericidal for Gram-negative bacteria, was localized to the membrane area in all types of azurophil granules, consistent with a suggested association of this protein with the granule membrane. The observed differences in intragranular distribution of the proteins investigated may reflect variations in binding to matrix structures and granule membranes.
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| 2. |
- Fioretos, Thoas, et al.
(författare)
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No evidence for genomic imprinting of the human BCR gene
- 1994
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Ingår i: Blood. - 1528-0020. ; 83:12, s. 3441-3444
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Tidskriftsartikel (refereegranskat)abstract
- Chronic myeloid leukemias and 5% to 20% of acute lymphoid leukemias are characterized by the Philadelphia chromosome, a reciprocal chromosomal translocation, t(9;22)(q34;q11), generating BCR-ABL and ABL-BCR fusion genes. Cytogenetic studies have recently shown a preferential involvement of the paternally derived chromosome 9 and the maternally derived chromosome 22 in this translocation, indicating that imprinting might be involved in the formation or selection of the translocation. In this study, we have identified a BamHI polymorphism in the coding region of BCR exon 1, allowing us to investigate whether both BCR alleles are transcribed. By using a reverse transcriptase-polymerase chain reaction assay, we show that both BCR alleles are expressed in the peripheral blood cells of normal individuals.
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| 3. |
- Garcia de Frutos, Pablo, et al.
(författare)
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Differential regulation of alpha and beta chains of C4b-binding protein during acute-phase response resulting in stable plasma levels of free anticoagulant protein S
- 1994
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Ingår i: Blood. - 1528-0020. ; 84:3, s. 815-822
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Tidskriftsartikel (refereegranskat)abstract
- Regulation of C4b-binding protein (C4BP) isoforms during acute phase and its relationship to the plasma concentration of free protein S was elucidated. An assay for beta chain containing C4BP (C4BP beta+) was developed and the concentrations of total C4BP, C4BP beta+, total, free, and bound protein S were measured in patients with acute-phase response. Even though total C4BP was increased to 162% (mean value) of controls, the corresponding value of C4BP beta+ was only 122%. In the acute-phase group, total protein S was increased to the same extent as C4BP beta+ (mean value of 124%), whereas free protein S was not decreased. In controls, total and bound protein S correlated with total C4BP and C4BP beta+. However, in the acute-phase group, the correlation between bound protein S and total C4BP was lost, although the correlation between C4BP beta+ and protein S remained. The present results suggest stable levels of free protein S during acute phase to be the result of differential regulation of C4BP alpha- and beta-chain expression, and the concentration of free protein S to be the resulting molar excess of protein S over C4BP beta+. This mechanism ensures functional levels of free anticoagulant protein S despite high levels of C4BP.
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| 4. |
- Garcia de Frutos, Pablo, et al.
(författare)
-
Differential regulation of α and β chains of C4b-binding protein during acute-phase response resulting in stable plasma levels of free anticoagulant protein S
- 1994
-
Ingår i: Blood. - 1528-0020. ; 84:3, s. 815-822
-
Tidskriftsartikel (refereegranskat)abstract
- Regulation of C4b-binding protein (C4BP) isoforms during acute phase and its relationship to the plasma concentration of free protein S was elucidated. An assay for β chain containing C4BP (C4BPβ+) was developed and the concentrations of total C4BP, C4BPβ+, total, free, and bound protein S were measured in patients with acute-phase response. Even though total C4BP was increased to 162% (mean value) of controls, the corresponding value of C4BPβ+ was only 122%. In the acute-phase group, total protein S was increased to the same extent as C4BPβ+ (mean value of 124%), whereas free protein S was not decreased. In controls, total and bound protein S correlated with total C4BP and C4BPβ+. However, in the acute-phase group, the correlation between bound protein S and total C4BP was lost, although the correlation between C4BPβ+ and protein S remained. The present results suggest stable levels of free protein S during acute phase to be the result of differential regulation of C4BP α- and β-chain expression, and the concentration of free protein S to be the resulting molar excess of protein S over C4BPβ+. This mechanism ensures functional levels of free anticoagulant protein S despite high levels of C4BP.
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