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  • 1
    Electronic Resource
    Electronic Resource
    The Human Mast Cell Line HMC-1 Expresses C5a Receptors and Responds to C5a but not to C5a(desArg) (1996)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 44 (1996), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The expression of the receptor for the anaphylatoxin C5a (C5aR, CD88) on the human mast cell line HMC-1 was studied with four anti-C5aR monoclonal antibodies directed to the N-terminal domain of the receptor. All antibodies bound to the human mast cell line HMC-1. The binding could be blocked by recombinant C5a and by peptide EX-1 representing amino residues 1–31 on the N-terminal domain of the C5aR. In addition, FITC-labelled C5a bound to HMC-1, and this binding could be blocked by unlabelled C5a or C5aR antibodies. C5aR-specific mRNA was detected in HMC-1 cells by RT-PCR which confirmed the expression of the C5aR gene made by these cells. Lymphocyte-conditioned medium, interferon-γ or phorbol esters which have been shown to induce a down-regulation of C5aR on myeloid cells did not influence the expression of C5aR on HMC-1. C5a let to a transient mobilization of intracellular calcium in HMC-1 which could be inhibited by pre incubation of C5a with a C5a-specific antibody. In contrast to findings with granulocytes, HMC-1 did not respond to C5a(desArg), confirming previous findings with human skin mast cells. The findings show that (i) although HMC-1 differ from granulocytes in their responsiveness to C5a(desArg), they express similar C5aR and (ii) HMC-1 resemble skin mast cells in the expression and function of C5aR and may therefore serve as a model in future studies addressing the biology of this anaphylatoxin receptor on skin mast cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.1996.d01-272.x
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  • 2
    Electronic Resource
    Electronic Resource
    Analysis of the Tissue Distribution of the Rat C5a Receptor and Inhibition of C5a-Mediated Effects Through the Use of Two MoAbs (2000)
    Oxford, U.K. and Cambridge, USA : Blackwell Science Ltd
    Scandinavian journal of immunology 52 (2000), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The C5-anaphylatoxin C5a is a protein of 74 (human) or 77 (rat) amino-acid residues, respectively, the generation of which may be induced by either the classical and/or the alternative pathways. C5a binds specifically to its receptor (C5aR/CD88) which belongs to the superfamily of G-protein-coupled receptors with seven transmembrane segments. In this study we describe the tissue distribution of the rat C5aR (rC5aR) and the blocking of its ligand by the application of two monoclonal antibodies (MoAbs). The first antibody (MoAb R63) which is directed against the amino-terminal domain Ex1 of the rat C5aR was generated in mice immunized with RBL–2H3 cells which had been stably transfected with the rat C5a receptor gene. Checking the rC5aR expression in various tissues bronchial epithelial cells stained positive only in tissue samples from animals with a mycoplasm infection indicating that the receptor may be induced in this cell type as a consequence of an inflammatory process. Using immunohistochemistry there was no evidence for nonmyeloid expression in the large or small intestine, heart, lung, kidney or liver of the normal rat. The MoAb R63 was found to be a reliable tool for the investigation of the expression of the receptor by FACS analyses or immunohistochemistry. Despite numerous attempts neutralizing antibodies could not be generated against the receptor. Therefore a C5a-ligand neutralizing MoAb was generated against the synthesized carboxyterminal 20mer peptide. This antibody (6–9F) recognized the carboxy terminus of C5a/C5a-FLUOS and prevented its binding at a three-fold molar excess as evidenced by FACS-analyses. It also blocked the C5a-mediated signal transduction as demonstrated by the inhibition of intracellular Ca2+-release (at a 16-fold molar excess) and the release of N-Acetyl-β- d-glucosaminidase (at a 25-fold molar excess).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.2000.00795.x
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  • 3
    Electronic Resource
    Electronic Resource
    Nephritic Factor: Its Structure and Function and Its Relationship to Initiating Factor of the Alternative Pathway (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Nephritic factor (NF) has a molecular weight of 170,000 and is composed of two disulfide-linked 85,000-dalton chains. NF assembles the fluid-phase C3 convertase from Factors B and D, C3, and magnesium by physically incorporating itself into the enzyme complex. NF exerts its stabilizing effect on the cell-bound C3/C5 convertase, EC, by physically associating itself with this complex. On decay of the cell-bound enzyme NF is released into the fluid phase and retains its binding and stabilizing potential. Its activity is resistant to diisopropylfluorophosphate treatment. Because NF causes agglutination of EC, it must be endowed with more than one binding site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb03020.x
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  • 4
    Electronic Resource
    Electronic Resource
    Reversible Activation of Proactivator (Factor B) of the Alternative Pathway Without Cleavage of the Molecule (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The serum of a patient (M.C.) with chronic glomerulonephritis and renal deposits of IgA, C3, and properdin converted C3 on overnight exposure to 0°C. The cold reaction was dependent on immunoglobulin, initiating factor, Factors B and D, and magnesium but not on properdin. Factor B, the C3-cleaving enzyme in this reaction, was used in zymogen form. After participation in this reaction, Factor B zymogen in M.C. serum could be fully activated by cobra venom factor (CVF) at 37°C. That activation without fragmentation was not due to an abnormal form of Factor B was shown by its typical cleavage on incubation of M.C. serum with CVF or C3b or after depletion of C3b inactivator. The evidence indicates that in the cold reaction only the initial C3 convertase of the alternative pathway is formed and that this enzyme is responsible for the observed C3 consumption.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb03021.x
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  • 5
    Electronic Resource
    Electronic Resource
    Rat Complement Factor H: Molecular Cloning, Sequencing and Quantification with a Newly Established ELISA (2002)
    Oxford, UK : Blackwell Science Ltd
    Scandinavian journal of immunology 56 (2002), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Factor H (FH) is the predominant soluble regulatory protein of the complement system. With a concentration of 300–600 µg/ml in human plasma it acts as a cofactor for the FI-mediated cleavage of the component C3b to iC3b. Furthermore, it competes with factor B for binding to C3b and C3(H2O) and promotes the dissociation of the C3bBb complex (i.e. it has decay accelerating activity). FH is a monomer of about 155 kDa which comprises 20 short consensus repeats (SCR), each of which is composed of nearly 60 amino acid residues. For the screening of a rat liver cDNA library, we used two hybridization probes which had been produced by polymerase chain reaction (PCR). The probes were generated using degenerated primers which corresponded to conserved parts of the human and the murine factor H nucleotide sequences. The entire rat sequence spanned 4240 nucleotides with an open reading frame of 3708 nucleotides. These were preceded by 23 nucleotides of the 5′ untranslated region, followed by a stop codon and a 3′ untranslated region of 478 nucleotides including the polyadenylation-signal up to the beginning of the poly A tail. Comparison of the rat cDNA-derived coding sequence revealed identities of 74% to the human and 87% to the mouse FH nucleotide sequence. The translation product of rat FH mRNA was 1236 aa in length (leader sequence included) with an identity of 63% to the human and 81.5% to the murine protein. The degree of glycosylation of rat FH-Mr is about 9.5%. To quantitate FH in rat serum and supernatants of primary cultures of rat hepatocytes (HC), a reliable and sensitive sandwich-enzyme-linked immunosorbent assay (ELISA) was established. The concentration of FH in rat serum was calculated to be 238 µg ± 21 µg/ml (mean ± SD). Its concentration in the culture supernatants of HC was upregulated about three-fold by interferon (IFN)-γ (100 U/ml).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3083.2002.01098.x
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  • 6
    Electronic Resource
    Electronic Resource
    The Serine Protease Nature of the C3 and C5 Convertases of the Classical and Alternative Complement Pathways (1976)
    Oxford, UK : Blackwell Publishing Ltd
    Scandinavian journal of immunology 5 (1976), S. 0 
    Details
    ISSN: 1365-3083
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Activated Factor B, incorporated into the cobra venom factor (CVF)-dependent C3/C5 convertase, was inactivated by diisopropylfluorophosphate (DFP). In-activation was time- and dose-dependent and was enhanced by the presence of substrate. Treatment of the zymogen of Factor B with DFP effected significant inactivation. Incorporation of [3H]diisopropylphosphate into the zymogen and into the activated form of Factor B was demonstrated after [3H]DFP treatment and subsequent electrophoresis of the proteins on polyacrylamide gels containing sodium dodecyl sulfate. Inactivation of activated C2 incorporated into the classical c5 convertase was observed on DFP treatment of the enzyme. DFP also reduced the activity of the C2 zymogen. The description of their serine proteinase nature further emphasizes the close structural and functional relationship of C2 and Factor B.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-3083.1976.tb03056.x
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  • 7
    Electronic Resource
    Electronic Resource
    Immune Haemolysis: Reaction of the Terminal Complement Component (1968)
    [s.l.] : Nature Publishing Group
    Nature 217 (1968), S. 1165-1167 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Sensitized sheep erythrocytes (EA) which had been reacted with the first eight components of complement (C'l-C'8, for nomenclature see ref. 5) were prepared and we have investigated the reaction of these E AC '1-8 cells with the last component of complement (C'9). This communication summarizes our ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2171165a0
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  • 8
    Electronic Resource
    Electronic Resource
    Die transhepatische Dauerdrainage bei der hohen Gallengangsstenose (1951)
    Springer
    Langenbeck's archives of surgery 270 (1951), S. 97-101 
    Details
    ISSN: 1435-2451
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01400391
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  • 9
    Electronic Resource
    Electronic Resource
    Kunstafterfragen (1953)
    Springer
    Langenbeck's archives of surgery 276 (1953), S. 544-550 
    Details
    ISSN: 1435-2451
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02443239
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  • 10
    Electronic Resource
    Electronic Resource
    Complement activation in patients with renal failure as detected through the quantitation of fragments of the complement proteins C3, C5, and factor B (1988)
    Springer
    Journal of molecular medicine 66 (1988), S. 857-864 
    Details
    ISSN: 1432-1440
    Keywords: Complement activation ; Hemodialysis ; Immunoassay ; Kidney failure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Using sensitive and highly specific enzyme-linked immunosorbent assays fragments of the complement proteins C3, C5, and factor B were quantitated in patients with renal failure. During hemodialysis on new cuprophan membranes raised levels not only of C3a, but in addition of activated C3, C5a, and Ba were demonstrated. In patients with chronic renal failure and end-stage renal disease plasma concentrations of Ba and activated C3 were markedly elevated independent of hemodialysis. This finding is taken as an indication of a continuous recruitment of the alternative pathway of complement in these patients. As the detected complement protein fragments are known to exert immune regulatory functions these findings may imply that these peptides are involved in the maintenance of the immune suppressed state in renal failure.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01728947
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