| 1. |
- Garcia de Frutos, Pablo, et al.
(author)
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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
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In: Blood. - 1528-0020. ; 84:3, s. 815-822
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Journal article (peer-reviewed)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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| 2. |
- Pérez, M. García, et al.
(author)
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Minimum action solutions for SU(2) gauge theory on the torus with non-orthogonal twist
- 1990
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In: Physics Letters, Section B: Nuclear, Elementary Particle and High-Energy Physics. - 0370-2693. ; 235:1-2, s. 117-123
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Journal article (peer-reviewed)abstract
- We use the cooling method and the lattice approximation to study the form and properties of the minimum action configurations for the SU(2) Yang-Mills theory on a space-time torous with twist k=m=(1, 1, 1).
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| 3. |
- Xu, S Y, et al.
(author)
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Purification and characterization of a human neutrophil lipocalin (HNL) from the secondary granules of human neutrophils
- 1994
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In: Scandinavian Journal of Clinical and Laboratory Investigation. - 0036-5513 .- 1502-7686. ; 54:5, s. 365-376
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Journal article (peer-reviewed)abstract
- A 45 kDa-protein was purified from the granules of human neutrophils. The protein consists of two apparently identical subunits. The isoelectric point was pH8.40, and the molecular weight 45kDa (unreduced) or 24kDa (reduced). Treatment of the protein with Endoglucosidase F resulted in a reduction in the molecular weight to 20 kDa, indicating the presence of N-linked carbohydrate. The extinction coefficient was E1%lcm = 13.76 at 280nm. The 60 amino acid sequence revealed up to 65% sequence homology with rat α2-microglobulin-related protein, which belongs to the lipocalin family. The protein co-sedimented with secondary (specific) granule marker proteins and correlated to the neutrophil content of Lactoferrin (r = 0.81,p<0.001) and was estimated to be 0.59 fig 10-6 cells. Release studies showed that the neutrophils released 51.4 ± 9.0% of the total cellular content of the protein when they were exposed to serum-opsonized particles, which was much higher than the release of Myeloperoxidase (12.7 ±3.5%) and Lactoferrin (22.9 ± 4.7%). The N-terminal and four tryptic fragment amino acid sequence of the protein was identical with an N-formyl peptide binding 24 kDa protein and gelatinase associated protein of human neutrophils. In conclusion, we have purified and characterized a protein, human neutrophil lipocalin (HNL), from the secondary granules of human neutrophils and shown that it is readily mobilized from the neutrophils upon stimulation.
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