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BIOSYNTHESIS OF THE 3RD component OF complement IN RAT-LIVER EPITHELIAL-CELL LINES AND ITS STIMULATION BY EFFECTOR MOLECULES FROM CULTURED HUMAN MONONUCLEAR-CELLS

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IN VITRO CELLULAR & DEVELOPMENTAL BIOLOGY 1987年第12期23卷 821-829页

作者： GUIGUET, M FRIGERE, MFE DETHIEUX, MC BIDAN, Y MACK, G 1. Laboratoire de Biochimie Médicale Unité de Recherche INSERM U208 Faculté de Médecine 7 boulevard Jeanne d'Arc 21033 Dijon Cedex France

Rat liver epithelial cell lines, growing in a serum-supplemented medium, synthesize and secrete into the culture medium the third component of complement (C3). We studied the regulation of C3 production in this system... 详细信息

Rat liver epithelial cell lines, growing in a serum-supplemented medium, synthesize and secrete into the culture medium the third component of complement (C₃). We studied the regulation of C₃ production in this system. We found that human peripheral blood mononuclear leukocytes in culture released one or more soluble factors which stimulated rat liver epithelial cells to produce increased quantitites of C₃. This stimulting effect was strongly enhanced when the mononuclear cell cultures were treated with phytohemagglutinin, a T-lymphocyte mitogen. The factor(s) failed to enhance C₃ biosynthesis by rat dermal fibroblasts, which are known to produce this protein. This reveals a tissue-specific differential response between the fibroblasts and the liver epithelial cells. The physical and chemical characteristics, such as heat sensitivity, 2.8M ammonium sulphate precipitation, and lower activity after digestion by proteases unambiguously indicate that the effector molecules are proteins. When the crude supernatant of mononuclear leukocytes was fractionated by gel filtration, the stimulating factor(s) eluted as two peaks with apparent molecular weight of 25 to 60 and 15 to 20 kdalton, respectively. As to the cellular origin of the C₃-stimulating factor(s), several observations were made: (a) in separate cultures containing either T-cells or monocyte-enriched populations from the same sample of blood mononuclear cells, no activity was detected in the presence or absence of phytohemagglutinin, (b) conditioned media from each of these cultures could not substitute for the corresponding intact cell populations, and (c) the addition of purified T-cells to the monocyte-enriched population in the presence of phytohemagglutinin restored the production of the stimulating activity by the mixed culture. Finally, experiments were c

关键词： rat liver epithelial cell line third component of complement human cytokines

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HEREDITARY PARTIAL DEFICIENCY OF THE 3RD component OF complement ASSOCIATED WITH MINIMAL CHANGE NEPHROTIC SYNDROME

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PEDIATRIC NEPHROLOGY 1987年第4期1卷 608-610页

作者： SPRINGATE, JE MCLEAN, RH WINKELSTEIN, JA FELD, LG CHILDRENS HOSP DEPT PEDIAT219 BRYANT STBUFFALONY 14222

We describe a 10 year old patient admitted to the Children's Hospital of Buffalo with hypocomplementemia associated with steroid responsive minimal change nephrotic syndrome. The sibling also had a low serum C3 concentration and all family members studied hadC 3 slow phenotypes. Factor I levels were at the lower limit of normal in the patient and his brother. Functional assays for CH50, total hemolyticC 3 and serum concentration of C2, C4−C9 and factors B and H were all within normal limits. This case confirms that a depressed serum complement level can occur in minimal change nephrotic syndrome and indicates that this depression could represent a preexisting inherited rather than an acquired deficiency. The findings are consistent with the pressence of a null or hypomorphicC 3 slow allele in hypocomplementemic family members. Additional studies are needed to resolve the association between the inherited partialC 3 deficiency and minimal change nephrotic syndrome.

关键词： Nephrotic syndrome third component of complement

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complement RECEPTORS - SPECIFIC DETECTION BY MOLECULAR COMPLEXES

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JOURNAL OF IMMUNOLOGICAL METHODS 1978年第2-3期19卷 227-234页

作者： COSSMAN, J GLORIOSO, JC ADLER, R UNIV MICHIGAN SCH MED DEPT PATHOL LAB ANIM MED UNIT ANN ARBOR MI 48104 USA UNIV MICHIGAN SCH MED DEPT HUMAN GENET ANN ARBOR MI 48104 USA

Immune complexes of BSA[bovine serum albumin]-anti BSA (Ig[immunoglobulin]G F(ab'')2) will activate human complement [C] by the alternate pathway. The C3 bound to these complexes binds to human peripheral blood mononuclear cells which bear C receptors. This interaction is visualized by fluoresceinated antigen (BSA-FITC [fluorescein isothiocyanate]) or fluorescein conjugated antisera directed at C3. The assay appears to be more sensitive than the usual IgMEAC [erythrocyte, IgM antibody, C] rosette technique and correlates well with the rosette method.

关键词： BSA bovine serum albumin C complement C-Mo mouse complement C-Hu human complement NHS normal human serum C3 third component of complement C4 fourth component of complement BSA-F(ab′)2-C antigen-antibody-complement complex in which the antibody is rabbit anti-BSA IgG F(ab′)2 fraction AgAbC antigen-antibody-complement complex FITC fluorescein isothiocyanate SRBC sheep erythrocyte IgMEAC SRBC sensitized with IgM antibody and complement.

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DETERMINATION OF OPTIMAL INVITRO CONDITIONS FOR CAPRINE ALTERNATIVE complement PATHWAY ASSAY

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VETERINARY IMMUNOLOGY AND IMMUNOPATHOLOGY 1992年第3-4期32卷 359-364页

作者： VENUGOPAL, G RAM, GC BANSAL, MP INDIAN VET RES INST IMMUNOL SECTIZATNAGAR 243122UTTAR PRADESHINDIA

Optimal in vitro testing conditions for caprine alternative complement pathway assay were determined. Effects of the following variables were tested: heterologous erythrocytes;pH, ionic strength and Mg2+ ion concentration of the complement diluent;incubation time and temperature. Rabbit erythrocytes were the optimal target cells. The optimal buffer conditions were: pH 8.0, ionic strength 0.06 mmol NaCl and 5mmol Mg2+ ion. Optimal incubation time and temperature were 75 min and 30-degrees-C, respectively.

关键词： ACP alternative complement pathway C3 third component of complement GVBS VBS containing 10 mM EDTA plus 0.1% gelatin (pH 7.4) VBS veronal buffered saline VBS-EGTA 2+ VBS containing 10 mM EGTA and 10 mM MgCl 2 (pH 7.4)

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DNA ANTIBODY CLASS, SUBCLASS, AND complement-FIXATION IN SYSTEMIC LUPUS-ERYTHEMATOSUS WITH AND WITHOUT NEPHRITIS

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CLINICAL IMMUNOLOGY AND IMMUNOPATHOLOGY 1978年第4期10卷 459-467页

作者： SONTHEIMER, RD GILLIAM, JN Department of Internal Medicine University of Texas Health Science Center Dallas Texas 75235 USA

A recently described indirect immunofluorescence technique, which employs the kinetoplast of a nonpathogenic hemoflagellate, Crithidia luciliae, as a native DNA substrate, was used to compare the complement-fixing, Ig [immunoglobulin] class and subclass properties of anti-native DNA antibodies in sera from systemic lupus erythematosus patients with and without nephritis. This simple technique showed that complement-fixing native DNA antibodies are more specific for lupus nephritis than are non-complement-fixing native DNA antibodies. Nephritis patients usually have native DNA antibodies in all 3 major Ig classes and more frequently have the IgG native DNA antibody subclasses that fix complement, IgG1 and IgG3. Apparently in systemic lupus erythematosus the biological properties of the antibodies produced and the intensity of the DNA antibody response are important determinants in the nephrotoxicity of immune complexes composed of native DNA and its antibody.

关键词： anti-nDNA antibodies to native DNA C3 third component of complement CF-anti-nDNA complement-fixing antibodies to native DNA FITC fluorescein isothiocyanate fluorescein/protein Ig immunoglobulin IIF indirect immunofluorescence nDNA native double-stranded deoxyribonucleic acid PBS phosphate-buffered saline SLE systemic lupus erythematosus TP total protein

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COUPLING OF C3B TO ERYTHROCYTES BY DISULFIDE BOND FORMATION - PREPARATION OF EC3B FOR HEMOLYTIC AND complement RECEPTOR ASSAYS

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JOURNAL OF IMMUNOLOGICAL METHODS 1983年第3期65卷 277-283页

作者： LAMBRIS, JD SCHEINER, O SCHULZ, TF ALSENZ, J DIERICH, MP UNIV MAINZ INST MED MICROBIOL D-6500 MAINZ FED REP GER

A new method of preparing C3[complement component 3]-coated erythrocytes [E] by coupling C3 to thiol-activated erythrocytes was described. The procedure involves 3 steps. Firstly, sheep erythrocytes were treated with N-succinimidyl 3-(2-pyridyldithio) propionate (SPDP) to introduce 3-(2-pyridyldithio) propionyl residues into membrane proteins. Secondly, C3 was cleaved with trypsin or CoVF [cobra venom factor], Bb [activated factor B] enzyme to obtain C3b exposing the SH group (C3b-SH). Finally, the C3b-SH was coupled to the thiol-activated erythrocytes (TA-E) through thiol/disulfide exchange to form the TA-EC3b conjugate. E coated with C3d was prepared by treating TA-EC3b with C3d with KSCN inactivated serum and plasmin. Studying the rosette formation between TA-EC3b or TA-EC3d and cells expressing C3b (CR1) and C3d (CR2) receptors and the inhibition thereof with anti-CR1 and anti-CR2 antibodies as well as with C3-sheep E membrane protein complexes, TA-EC3b and TA-EC3d bound exclusively to CR1 and CR2, respectively. TA-EC3b like EAC1423b [antibody sensitized erythrocyte coated with C1, C4, C2, C3b] bound factors B and H as tested by hemolytic and direct binding assays. The advantage of TA-EC3 for complement receptor and hemolytic assays are the simplicity of the preparation method and the general applicability of the TA-EC3.

关键词： thiolation of erythrocytes third component of complement complement receptors Bb activated factor B BDVEA 1% bovine serum albumin (BSA) 3.2% dextrose 35 mM veronal buffer pH 7.2 with 20 mM EDTA 2 mM sodium azide C complement C3b major fragment of C3 activation 190,000 daltons C3d 30,000 daltons fragment of C3b that retains to complexes following proteolytis of bound C3b CR1 complement receptor type one receptor specific for the C region of C3b and C4b CR2 complement receptor type two receptor specific for the d region of C3b E erythrocyte EA IgM-antibody sensitized E EAC EA coated with complement components EC3 sheep E-C3 complexes prepared by C3 activation and fixation onto sheep E GVB-Ni gelatin veronal buffer containing 0.15 mM nickelous chloride PDP 3-(2-pyridyldithio) propionyl groups TA-E, thiol-activated erythrocytes TA-EC3 TA-E coated with C3 SPDP N-succinimidyl 3-(2-pyridyldithio) propionate

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LACK OF BINDING OF C-3 TO IGG ANTIBODIES DURING THE ACTIVATION OF THE CLASSICAL complement PATHWAY ON THE RED-CELL

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MOLECULAR IMMUNOLOGY 1984年第3期21卷 191-195页

作者： CIRCOLO, A BORSOS, T Laboratory of Immunobiology National Cancer Institute National Institutes of Health FCRF Frederick MD 21701 U.S.A.Received 30 May 1983 Revised 30 September 1983 Available online 12 November 2002

The interaction between C3 [complement component 3] and natural human and rabbit anti-MTX [methotrexate] IgM and hyperimmune IgG antibody [Ab] bound to red cells to which MTX was covalently coupled. IgM Ab molecules bound to the cell surface were measured by their interaction with rabbit anti-human .mu.-chain IgG Ab;the bound anti-.mu.-chain or anti-MTX IgG was quantitated with 125I-labeled PA [protein A]. C3 uptake by .**GRAPHIC**. complexes from purified preparation of C3 was detected by the interaction of bound C3 with rabbit anti-C3 IgG Ab;the bound IgG was then measured with rabbiolabeled PA. In some experiments the uptake of C3 by the .**GRAPHIC**. complexes was measured by using 125I-labeled C3. To find out if C3 was bound to Ab molecules, anti-MTX Ab were eluted from the cells by excess fluid-phase MTX. After dialysis the eluted anti-MTX IgM or IgG Ab was than reattached to fresh EMTX. All cells were then analyzed for Ab and C3 content by a radioimmunoassay. When anti-MTX IgM or IgG was eluted from EMTX AC423 complexes no C3 was removed from the cells, and eluted IgM or IgG did not carry with them either C3 antigen or 125I-labeled C3. Thus, during activation of the classical C-pathway at the red cell surface, no C3 was bound to IgM (rabbit or human) or IgG (rabbit) antibody molecules.

关键词： C complement C1 first component of complement C4 fourth component of complement C2 second component of complement C3 third component of complement C1 … active form of C-components EDTA in VBS 0.01 M tri- N -ethylenediaminetetraacetate in veronal-buffered saline containing 0.1% gelatin, pH 7.4 IgM immunoglobulin of class M IgG immunoglobulin of class G E sheep red blood cell(s) MTX methotrexate E MTX sheep red blood cell(s) to which MTX was covalently coupled PA protein A of Staphylococcus aureus gp guinea-pig Ab antibody

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Cloning and characterization of anti-cathepsin L single chain variable fragment whose expression inhibits procathepsin L secretion in human melanoma cells

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BIOCHEMICAL JOURNAL 2002年第1期367卷 219-227页

作者： Guillaume-Rousselet, N Jean, D Frade, R Hop St Antoine INSERM U354 Ctr INSERM F-75012 Paris France

We previously demonstrated that increase of procathepsin L secretion by human melanoma cells strongly increased their tumourigenicity and switched their phenotype from low to highly metastatic. Thus, we herein analysed whether it was possible to inhibit procathepsin L secretion using anti-cathepsin L ScFv. For this purpose, we produced different forms of fusion cathepsin L in prokaryotic or eukaryotic expression systems. An anticathepsin L monoclonal antibody (mAb), named 3138, was isolated from mice immunized with purified procathepsin L-His. This 3138 mAb interacted with an epitope localized on the 156-197 amino acid sequence of cathepsin L and recognized recombinant or native forms of cathepsin L synthesized by human melanoma cells. An active anti-cathepsin L ScFv was generated and characterized from 3138 mAb heavy and light variable chains. Then, human melanoma cells were transiently co-transfected with 3138 ScFv and cathepsin L cDNAs. Data demonstrated that increase of 3138 ScFv expression in human melanoma cells totally inhibited procathepsin L secretion and induced accumulation of intracellular procathepsin L. Our results constitute the first demonstration that anti-cathepsin L ScFv could be used in human melanoma cells to inhibit procathepsin L secretion. This ScFv represents a new molecular tool to explore cell therapy of human melanomas.

关键词： cell therapy cysteine protease third component of complement

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CONTRIBUTION OF ACTIVATED C-3 TO LYMPHOCYTE-MEDIATED CYTOLYSIS

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MOLECULAR IMMUNOLOGY 1986年第11期23卷 1257-1262页

作者： KLEIN, E SARMAY, G RAMOS, O YEFENOF, E GERGELY, J HEBREW UNIV JERUSALEM HADASSAH MED SCHLAUTENBERG CTR IMMUNOLIL-91010 JERUSALEMISRAEL LOARND EOTVOS UNIV DEPT IMMUNOLGODHUNGARY

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ROLE OF C3B RECEPTORS IN THE ENHANCEMENT OF INTERLEUKIN-2-DEPENDENT T-CELL PROLIFERATION

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MOLECULAR IMMUNOLOGY 1984年第12期21卷 1215-1221页

作者： ERDEI, A SPAETH, E ALSENZ, J RUDE, E SCHULZ, T GERGELY, J DIERICH, MP UNIV INNSBRUCK INST HYG A-6020 INNSBRUCK AUSTRIA UNIV MAINZ INST MED MIKROBIOL D-6500 MAINZ FED REP GER UNIV MAINZ INST IMMUNOL D-6500 MAINZ FED REP GER

The effect of the 3rd complement component (C3) on different T cell-dependent processes was studied using well-defined mouse T cell lines. While C3 did not influence the interleukin-2 (IL-2) production of the ST52/K-9 helper T cells, the IL-2-dependent proliferation of the ST1 line was dose-dependently enhanced by C3. Neither the hemolytic activity of C3 nor the C3a fragment had any role in the process. The effect of C3 on the IL-2-dependent T cell growth was even more enhanced (up to 5-fold) when using polymerized C3. When the ST1 cell line was cultured in the presence of the cross-linked ligand, T cells formed 80% fewer rosettes with red blood cells coated with antibody and mouse or human C3b. C3, particularly when aggregated, apparently exerts its enhancing effect on the growth of the IL-2-dependent cell lines by binding to C3b receptors present on such T cells.

关键词： C3 third component of complement C3a and C3b fragments of C3 C3bR C3b receptor EAC3b hu red blood cells coated with antibody and human C3b EAC3b mo red blood cells coated with antibody and mouse C3b H factor of alternative complement activation pathway HSA human serum albumin IL-2 interleukin-2 PMA phorbol myristate acetate T H helper T-lymphocyte

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