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  • 1
    Electronic Resource
    Electronic Resource
    The Acute Phase Response in the Rodent (1989)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 557 (1989), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1989.tb24000.x
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  • 2
    Electronic Resource
    Electronic Resource
    EVOLUTION OF THYROID HORMONE DISTRIBUTION (1998)
    Oxford, UK : Blackwell Publishing Ltd
    Clinical and experimental pharmacology and physiology 25 (1998), S. 0 
    Details
    ISSN: 1440-1681
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: 1. Appropriate distribution of thyroxine between the lipid-soluble compartments of cells and tissues and the extracellular aqueous space is established by binding to extracellular proteins. Among these proteins, transthyretin is of particular interest because it is the only one synthesized in the brain.2. The evolutionary onset of transthyretin synthesis in cells of the blood-brain barrier precedes that in the liver, with the exception of a very short period of transthyretin synthesis in the liver of tadpoles, just prior to the climax of metamorphosis. In adult liver, transthyretin is only synthesized in endothermic vertebrates.3. The affinity of transthyretin for thyroxine increases and that for 3,5,3′-triiodothyronine decreases during the evolution of eutherians from reptile/bird-like common ancestors.4. A systematic change of the N-terminal region of transthyretin occurred during evolution, leading to shorter and more hydrophilic transthyretin N termini in eutherians compared with those in reptiles and birds.5. The molecular mechanism of the evolution of the transthyretin N termini is a stepwise shift of the splice site at the intron 1/exon 2 border in the 3’ direction. The most probable cause for this shift is a series of single base mutations.6. As the N termini are located on the surface of transthyretin near the entrance to its central channel leading to the thyroxine binding sites, it is possible that a change in the structure of this region could influence the access of thyroxine to the binding sites. The increase in affinity for thyroxine could then be a driving force in the natural selection during evolution of transthyretins with shorter and more hydrophilic N termini.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1681.1998.tb02285.x
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  • 3
    Electronic Resource
    Electronic Resource
    Letter to the Editor (2005)
    Oxford, UK : Blackwell Science Ltd
    International journal of dermatology 44 (2005), S. 0 
    Details
    ISSN: 1365-4632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-4632.2004.02420.x
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  • 4
    Electronic Resource
    Electronic Resource
    Levels of messenger ribonucleic acids for plasma proteins in rat liver during acute experimental inflammation (1986)
    Springer
    Inflammation 10 (1986), S. 59-66 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The levels of mRNA for plasma proteins and for metallothionein in rat liver during the acute-phase response were studied by hybridization to specific cDNA probes. The mRNA forα 2 -macroglobulin, theβ-chain of fibrinogen, α1,-acid glycoprotein (so-called acute-phase reactants) reached a maximum level between 18 and 36 h after inducing an acute inflammation. The level of mRNA for metallothionein-I peaked earlier, after 12 h. The mRNA for transferrin showed a delayed increase with a broad maximum for its relative level after 36–60 h. The mRNA levels for albumin and α2u-globulin (so-called negative acute-phase reactants) decreased, reaching a minimum of 25 % of the normal level after 36 h (albumin) and after 72 h (α2u-globulin). The ratios of the rates of incorporation of leucine into the proteins over the levels of their mRNA in liver changed only a little, indicating that the rates of synthesis of plasma proteins in the liver are regulated at the mRNA level during the acute-phase response to inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00916041
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  • 5
    Electronic Resource
    Electronic Resource
    Acute-phase response of plasma protein synthesis during experimental inflammation in neonatal rats (1985)
    Springer
    Inflammation 9 (1985), S. 1-7 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The pattern of plasma protein concentrations in neonatal rats differs characteristically from that in adult animals. Immediately after birth, the concentration of α2-macroglobulin is about 200 times higher, that of major acute-phase α1 protein the same, and that of α1-acid glycoprotein, another acute phase protein, is considerably lower, compared with the values observed in healthy adults. The concentration of prealbumin, a negative acute-phase protein, remains low in the immediate postnatal period, but increases at a time when concentrations of both thyroxine and corticosterone increase. At this time, there is also a distinct increase in the concentration of α1-acid glycoprotein. Despite the differences in concentration of plasma proteins in the adult rat and the neonate, the neonatal liver has the capability to respond to an acute inflammation with a coordinated change in the synthesis rates of plasma proteins similar to that observed in adult animals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00915406
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of acute inflammation on rat apolipoprotein mRNA levels (1987)
    Springer
    Inflammation 11 (1987), S. 241-251 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Hybridization studies using specific cDNA have been used to determine the mRNA levels for rat apolipoproteins AI, AII, AIV, and E in extracts of rat liver and intestine. The ratios of intestinal mRNA/liver mRNA for apolipoprotein AI (apo AI), apo AIV, and apo E were 1.3, 1.7, and 0.1, respectively. Apo AII mRNA was detected in the liver but not in the intestine. The mRNA levels for apo AII and apo AIV in rat liver decreased during inflammation to minimums of 40% and 25% of normal, respectively. The mRNA levels for apo AIV in the intestine, apo E in the liver and for apo AI in both the liver and intestine did not change significantly during inflammation. The time course for the decrease in the hepatic mRNA levels for apo AIV was similar to those previously observed for the negative acute-phase proteins albumin and transthyretin. The serum levels for apo AIV were not affected by inflammation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00916024
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  • 7
    Electronic Resource
    Electronic Resource
    Effect of recombinant interleukin-1 on mRNA levels in rat liver (1988)
    Springer
    Inflammation 12 (1988), S. 613-617 
    Details
    ISSN: 1573-2576
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Levels of rat liver mRNA for the plasma proteins albumin, apolipoprotein E, transthyretin, transferrin,α 1-acid glycoprotein, major acute-phaseα 1-protein, and theΒ-chain of fibrinogen were measured after intraperitoneal injection of interleukin-1α (IL-1). A maximum response of mRNA levels for most of the plasma proteins studied was reached between 6 and 10 h after injection of IL-1. The results suggest that at the dosage used, IL-1 alone does not elicit a typical acute-phase response of the plasma protein-synthesizing system of the liver.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00914322
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  • 8
    Electronic Resource
    Electronic Resource
    Distribution of Ion-Implanted Nitrogen in Iron Alloys Investigated by AES (2000)
    Springer
    Microchimica acta 132 (2000), S. 237-242 
    Details
    ISSN: 1436-5073
    Keywords: Key words: Auger electron spectroscopy; depth profiling; iron nitride; implantation; plasma.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract.  The depth distribution and the lateral distribution of nitrogen after implantation by means of plasma immersion ion implantation (PIII) in ferritic alloys with 0.3 wt.-% Al and 3.6 wt.-% Cr has been studied by scanning Auger electron spectrometry (AES). To get information about the chemical state of nitrogen and to improve the detection limit methods of data analysis (factor analysis, LLS) have been applied to depth and line profiles, respectively. Thereby the detection limit for nitrogen was reduced from 6% to 1%. The nitrogen distribution is laterally homogeneous in the near surface region only. Depth profiles obtained at several points within the sputter crater showed that the in-depth distribution of nitrogen varies markedly between different points on the sample and from sample to sample. The nitrogen concentration in the implantation maximum corresponds to Fe2N1−x (x ≈ 0.04 ⃛ 0.18). A remarkable feature are grains having a 10 μm wide seam rich in N and a nearly nitrogen-free grain’s interior. The N/Fe ratio determined from line profiles show that the outer layer of the grains has almost the exact composition Fe4N and the transition to the nearly nitrogen-free grain's interior (cN ≤ 1%) occurs within 1 ⃛ 4 μm. The same shape of the N(KLL) peak was found in depth profiles and line scans, respectively, and it corresponds to gasnitrided samples γ ′–Fe4N and ɛ–Fe2N1−x.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s006040050017
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  • 9
    Electronic Resource
    Electronic Resource
    Dissection of multi-protein complexes using mass spectrometry: Subunit interactions in transthyretin and retinol-binding protein complexes (1998)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 33 (1998), S. 3-11 
    Details
    ISSN: 0887-3585
    Keywords: mass spectrometry ; time-of-flight ; nanoflow electrospray ; transthyretin ; retinol binding protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Complexes formed between transthyretin and retinol-binding protein prevent loss of retinol from the body through glomerular filtration. The interactions between these proteins have been examined by electrospray ionization combined with time-of-flight mass analysis. Conditions were found whereby complexes of these proteins, containing from four to six protein molecules with up to two ligands, are preserved in the gas phase. Analysis of the mass spectra of these multimeric species gives the overall stoichiometry of the protein subunits and provides estimates for solution dissociation constants of 1.9 ± 1.0 × 10-7 M for the first and 3.5 ± 1.0 × 10-5 M for the second retinol-binding protein molecule bound to a transthyretin tetramer. Dissociation of these protein assemblies within the gas phase of the mass spectrometer shows that each retinol-binding protein molecule interacts with three transthyretin molecules. Mass spectral analysis illustrates not only a correlation with solution behavior and crystallographic data of a closely related protein complex but also exemplifies a general method for analysis of multi-protein assemblies. Proteins Suppl. 2:3-11, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Dissection of multi-protein complexes using mass spectrometry: Subunit interactions in transthyretin and retinol-binding protein complexes (1998)
    New York, NY : Wiley-Blackwell
    Proteins: Structure, Function, and Genetics 33 (1998), S. 3-11 
    Details
    ISSN: 0887-3585
    Keywords: mass spectrometry ; time-of-flight ; nanoflow electrospray ; transthyretin ; retinol binding protein ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Complexes formed between transthyretin and retinol-binding protein prevent loss of retinol from the body through glomerular filtration. The interactions between these proteins have been examined by electrospray ionization combined with time-of-flight mass analysis. Conditions were found whereby complexes of these proteins, containing from four to six protein molecules with up to two ligands, are preserved in the gas phase. Analysis of the mass spectra of these multimeric species gives the overall stoichiometry of the protein subunits and provides estimates for solution dissociation constants of 1.9 ± 1.0 × 10-7 M for the first and 3.5 ± 1.0 × 10-5 M for the second retinol-binding protein molecule bound to a transthyretin tetramer. Dissociation of these protein assemblies within the gas phase of the mass spectrometer shows that each retinol-binding protein molecule interacts with three transthyretin molecules. Mass spectral analysis illustrates not only a correlation with solution behavior and crystallographic data of a closely related protein complex but also exemplifies a general method for analysis of multi-protein assemblies. Proteins Suppl. 2:3-11, 1998. © 1998 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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