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1.
Actas dermo-sifiliogr. (Ed. impr.) ; 98(6): 403-414, jul. 2007. ilus, tab
Article in Es | IBECS | ID: ibc-055251

ABSTRACT

Introducción. La dermatomiositis (DM) es una enfermedad de origen autoinmune, incluida en el grupo de las miopatías inflamatorias idiopáticas. En el control clínico de este proceso se precisan marcadores que permitan determinar el grado de actividad de la enfermedad, facilitando así el ajuste a la terapia inmunomoduladora. Se analiza la relación entre los productos de activación del complemento (PAC) y la actividad de la DM y su utilidad en el seguimiento de la enfermedad y en la predicción de las reagudizaciones en relación a los parámetros bioquímicos habituales. Material y métodos. Se estudiaron 16 pacientes con DM, que fueron seguidos periódicamente. En cada revisión se estableció el grado de actividad cutánea y muscular del proceso, y se correlacionó dicha actividad con los niveles plasmáticos de C3a y C5b-9, determinados mediante técnica de ELISA. Resultados. Si bien se obtuvo cierta correlación entre la actividad del proceso y los niveles plasmáticos de C3a y C5b-9, la intensidad de dicha correlación no superó la obtenida por los marcadores bioquímicos tradicionales. En la capacidad de predicción de reagudizaciones, C3a se mostró como el marcador más sensible (100 %), con una especificidad suficiente (83,3 %). Conclusiones. C3a y en menor medida C5b-9 serían de utilidad en la identificación de pacientes con DM especialmente activas, así como en la predicción de reagudizaciones del proceso. Sin embargo, no tienen una utilidad superior al resto de marcadores bioquímicos como marcadores de actividad actual


Introduction. Dermatomyositis (DM) is an autoimmune disease included in the group of idiopathic inflammatory myopathies. Markers of disease activity are needed for clinical control in order to facilitate adjustment of immunomodulatory therapy. We analyzed the relationship between complement activation products (CAP) and the activity of dermatomyositis and its usefulness in the follow-up of the disease and the prediction of recrudescences related to usual biochemical parameters. Material and methods. We studied 16 patients with DM that were followed periodically. In each appointment the degree of cutaneous and muscular activity was assessed and such disease activity was correlated with plasma levels of C3a and C5b-9, measured by ELISA. Results. Though we obtained certain correlation between disease activity and plasma levels of C3a and C5b-9, the strength of such correlation was not superior to that obtained by usual biochemical markers. C3a was shown to be the most sensitive marker (100 %) with a sufficient specificity (83.3 %) in the capability to predict recrudescences. Conclusions. C3a and, to a lesser extent C5b-9, would be useful in the identification of patients with especially active DM as well as in predicting disease recrudescences. Nevertheless they are not superior to the rest of biochemical markers as indicators of current activity


Subject(s)
Humans , Dermatomyositis/diagnosis , Complement Activating Enzymes/analysis , Biomarkers/analysis , Creatine Kinase/analysis , Complement Activation/physiology , Complement C3-C5 Convertases/analysis
2.
Immunity ; 6(2): 119-29, 1997 Feb.
Article in English | MEDLINE | ID: mdl-9047234

ABSTRACT

The complement protein C1q, mannose-binding lectin (MBL), and pulmonary surfactant protein A (SPA) are structurally similar molecules that enhance phagocytic function in vitro. Monoclonal antibodies R3 and R139, which inhibit the enhancement triggered by these three ligands, were used to purify a 126,000 M(r) cell surface protein designated C1qR(P). Amino acid sequence was obtained and the corresponding cDNA was cloned. C1qR(P) is a novel type I membrane protein with the following putative structural elements: a C-type carbohydrate recognition domain, five EGF-like domains, a transmembrane domain, and a short cytoplasmic tail. All peptides identified by amino acid sequencing are encoded by the cDNA. Additionally, an anti-peptide antiserum was generated, which is reactive with C1qR(P). The data indicate that the cloned cDNA encodes the receptor that plays a role in C1q/MBL/SPA-mediated removal or destruction of pathogens and immune complexes by phagocytosis.


Subject(s)
Carrier Proteins/metabolism , DNA, Complementary/analysis , Hyaluronan Receptors , Membrane Glycoproteins , Phagocytosis/physiology , Pulmonary Surfactants/metabolism , Receptors, Complement/analysis , Receptors, Complement/metabolism , Receptors, Immunologic/analysis , Receptors, Immunologic/metabolism , Amino Acid Sequence , Base Sequence , Cloning, Molecular , Collectins , Complement Activating Enzymes/analysis , Complement Activating Enzymes/metabolism , Complement Activating Enzymes/physiology , Humans , Lymphoma, Large B-Cell, Diffuse , Macrophage Activation/physiology , Mitochondrial Proteins , Molecular Sequence Data , Receptors, Complement/physiology , Tumor Cells, Cultured
3.
Article in English | MEDLINE | ID: mdl-7939508

ABSTRACT

The combined effect of heparin coating of cardiopulmonary bypass (CPB) circuits and reduced dose of systemic heparin on activation of the complement system and blood leukocytes was investigated in 19 patients undergoing coronary bypass surgery and randomly allocated to two groups. A heparin-coated CPB circuit together with a 50% reduction of the standard heparin dose were used for ten patients (HC group), and a standard CPB circuit with a standard heparin dose (300 IU/kg) for nine (C group). Significant rise in the levels of neutrophil-derived myeloperoxidase, lactoferrin and calprotectin were observed during CPB in both groups, but the total accumulated levels were significantly lower in the HC than in the C group (p < 0.05). Complement activation, assessed from levels of C3a and terminal complement complexes was similar in both groups. The lower levels of myeloperoxidase, lactoferrin and calprotectin during CPB in the HC group indicate that surface modification with end-point attached heparin enhances the biocompatibility of CPB.


Subject(s)
Cardiopulmonary Bypass/methods , Complement Activation , Heparin/therapeutic use , Neutrophil Activation , Oxygenators , Biocompatible Materials/pharmacology , Complement Activating Enzymes/analysis , Complement Activation/drug effects , Dose-Response Relationship, Drug , Heparin/administration & dosage , Heparin/pharmacology , Humans , Leukocyte Count , Male , Middle Aged , Neutrophil Activation/drug effects , Protamines/administration & dosage , Protamines/pharmacology
4.
Cell Immunol ; 122(1): 48-61, 1989 Aug.
Article in English | MEDLINE | ID: mdl-2787703

ABSTRACT

Mouse resident peritoneal macrophages (PM) were reconstituted in their response to activation for antibody-dependent cellular cytotoxicity (ADCC) for sheep erythrocyte targets (SRBC) by subhemolytic dilutions of homologous or autologous sera. ADCC-responsive inflammatory PM were largely unaffected in their activation by exogenous serum. Augmentation of resident PM for ADCC by homologous serum was correlated with the complement-activating potential of the mouse monoclonal anti-SRBC IgG isotype in that serum augmented IgG gamma 2a greater than IgG gamma 2b much greater than IgG gamma 1. The active component of mouse serum was heat-labile at 56 degrees C for 30 min and was present in both C5-deficient AKR and C5-sufficient homologous C3H mouse sera. Western blot analysis of the cell lysates for Clq confirmed that oil-elicited and thioglycollate-elicited inflammatory PM had greater levels of endogenous Clq than did resident PM which correlated with their innate responsiveness for ADCC activation. Depletion of Clq from serum by immunoprecipitation with IgG antibody to Clq or by ion exchange chromatography removed the active reconstituting activity for ADCC. Purified mouse Clq (0.4 microgram) partially replenished the ADCC augmenting activity of Clq-depleted AKR mouse serum. SRBC targets preopsonized with IgG gamma 2a and purified mouse Clq (0.075-5.0 microgram/ml) fully reconstituted the ADCC response of resident PM similar to homologous serum indicating that the major active component of serum was Clq. Thus resident PM with low endogenous levels of Clq were reconstituted for ADCC by the addition of exogenous Clq, whereas inflammatory PM with sufficiently high endogenous levels of Clq were not further enhanced by exogenous Clq. Our findings indicate that Clq may provide an essential second signal in concert with Fc receptor binding of IgG to initiate ADCC activation of macrophages.


Subject(s)
Antibody-Dependent Cell Cytotoxicity , Complement Activating Enzymes/physiology , Complement C1/physiology , Macrophages/immunology , Animals , Blood Physiological Phenomena , Complement Activating Enzymes/analysis , Complement C1/analysis , Complement C1q , Immunoglobulin G/physiology , Macrophage Activation , Male , Mice , Mice, Inbred C3H , Peritoneal Cavity/cytology
6.
Circ Res ; 64(3): 607-15, 1989 Mar.
Article in English | MEDLINE | ID: mdl-2783892

ABSTRACT

Mitochondria may be a source of molecules that activate complement during ischemic injury to myocardium, providing therewith a stimulus for infiltration of polymorphonuclear leukocytes. To identify specific molecules that activate the classical complement pathway, detergent lysates of canine cardiac mitochondria were fractionated by polyacrylamide gel electrophoresis and transferred electrophoretically to nitrocellulose paper (NCP). The NCP replicas of the gels were incubated with isolated C1q and fresh sera as a source of complement, washed briefly, and overlaid with sensitized sheep erythrocytes (RBC) in agarose. A cluster of four to six molecules between 45 and 53 kDa as well as four others, 34, 30, 26, and 23 kDa, consumed complement thereby preventing complement-mediated lysis of sensitized sheep RBC in the agarose overlay. Additional molecules reactive with C1 were identified by their ability to bind isolated human C1q and to serve as assembly sites for later acting complement components. Sites of localization of complement were demonstrated by incubating NCP replicas of fractionated mitochondria with antisera specific for C1q, C3, C5, and C9, followed by peroxidase-conjugated anti-immunoglobulin and substrate. A total of 12 C1q binding molecules ranging in size from 67 kDa to 23 kDa, which can fix later acting complement components, were identified. At least two of these reacted with antisera prepared against canine cardiac lymph collected in the first 3-4 hours after a 45-minute coronary artery occlusion. These studies present direct evidence that specific molecules, released from subcellular fractions of myocardial cells rich in mitochondria, can activate the complement cascade.


Subject(s)
Complement Activating Enzymes/immunology , Complement Activation , Complement C1/immunology , Complement Pathway, Classical , Coronary Disease/immunology , Mitochondria, Heart/immunology , Animals , Binding Sites , Complement Activating Enzymes/analysis , Complement C1/analysis , Complement C1q , Complement Fixation Tests/methods , Dogs , Electrophoresis, Polyacrylamide Gel/methods , Guinea Pigs , Humans , Lymph/immunology , Mitochondria, Heart/analysis , Molecular Weight , Muscle Proteins/analysis , Muscle Proteins/immunology
7.
Pediatr Med Chir ; 11(1): 33-6, 1989.
Article in Italian | MEDLINE | ID: mdl-2785685

ABSTRACT

Clinical, metabolic, neurophysiologic and immunological data were obtained in a group of 50 patients with type I diabetes mellitus Results were compared with those obtained in 30 healthy subjects of comparable age. M.N.C. (median nerve conduction) velocities and sensitive latency were observed to be significant lower in the diabetic patients rather than in the controls. These abnormalities were correlated with the duration of diabetes rather than with the glucose control. The positivity for circulating immune complexes was found to be associated with a significant reduction of median sensory nerve conduction velocity. There results suggest that in addition to metabolic, genetic, vascular and hormonal abnormalities also immunologic factors may play a role in the pathogenesis of diabetic neuropathy.


Subject(s)
Diabetes Mellitus, Type 1/physiopathology , Median Nerve/physiopathology , Neural Conduction , Adolescent , Child , Complement Activating Enzymes/analysis , Complement Activating Enzymes/immunology , Complement C1/analysis , Complement C1/immunology , Complement C1q , Diabetes Mellitus, Type 1/blood , Diabetes Mellitus, Type 1/immunology , Female , Humans , Male , Median Nerve/immunology , Tibial Nerve/immunology , Tibial Nerve/physiopathology
8.
Ukr Biokhim Zh (1978) ; 61(1): 9-17, 1989.
Article in Russian | MEDLINE | ID: mdl-2787069

ABSTRACT

The distribution of aromatic amino acid residues in the Clq molecule according to their microenvironment was studied by the methods of difference thermal and solvent perturbation spectroscopy, fluorescence and chemical modification. Out of the three tryptophan residues located in the globular part of A- chain one residue is completely exposed on the surface, while other two are only partially exposed to a solvent. Chemical modification of tryptophanyls significantly affects the hemolytic activity of Clq, that may evidence for the formation of immunoglobulin-binding sites with participation of A- chains as well as for the location of, at least, one of the three tryptophan residues in A- chain close to the immunoglobulin-binding site or even participation in the formation of the latter. The average rotation relaxation time of tryptophanyls estimated from the data on fluorescence is 210 +/- 10 ns. It specifies mobility of the globular and collagen parts of the molecule.


Subject(s)
Amino Acids/analysis , Complement Activating Enzymes/analysis , Complement C1/analysis , Complement C1q , Protein Conformation , Spectrophotometry , Tryptophan/analysis
9.
Int J Dermatol ; 28(1): 32-5, 1989.
Article in English | MEDLINE | ID: mdl-2783924

ABSTRACT

Complement components C1q and C4 of classic pathway; C3d, a breakdown product of C3, and factor B of alternate pathway: and C3, a component both of classic and alternate pathways, were studied in 35 patients, comprising 18 type I (Lepra) and 17 type II (ENL) reactions. There was a significant decrease in C3 and factor B with a concomitant rise of C3d during ENL. These changes indicate their preeminent role in immunogenesis of type II (ENL) reaction. The changes in the classic pathway components, on the other hand, were insignificant, apparently suggesting its limited involvement in ENL. Furthermore, reversion of factor B and C3d after subsidence of reaction is intriguing and may indicate that they are not substantially affected even with contemporary treatment. Complement components, of both classic and alternate pathways, showed no significant alterations either during type I (Lepra) reaction or after its amelioration.


Subject(s)
Complement System Proteins/analysis , Leprosy/immunology , Complement Activating Enzymes/analysis , Complement C1/analysis , Complement C1q , Complement C3/analysis , Complement C3d , Complement C4/analysis , Complement Factor B/analysis , Complement Pathway, Alternative , Complement Pathway, Classical , Erythema Nodosum/immunology , Humans , Leprosy, Lepromatous/immunology
11.
J Immunol Methods ; 114(1-2): 101-6, 1988 Nov 10.
Article in English | MEDLINE | ID: mdl-3141513

ABSTRACT

Determination of the C1q content of cerebrospinal fluid (CSF) may be of value in understanding the immunological reactions occurring within the central nervous system (CNS). A double sandwich ELISA method has been developed for the detection of C1q in human serum and CSF. It uses polyclonal antibodies and is sensitive in the nanogram range. The mean concentrations of C1q were determined to be 127 micrograms/ml in serum and 0.4 microgram/ml in CSF. These results suggest that increased levels of C1q in the CSF play a role in some neurodegenerative disorders.


Subject(s)
Complement Activating Enzymes/cerebrospinal fluid , Complement C1/cerebrospinal fluid , Enzyme-Linked Immunosorbent Assay , Adolescent , Adult , Aged , Alzheimer Disease/blood , Alzheimer Disease/cerebrospinal fluid , Amyotrophic Lateral Sclerosis/blood , Amyotrophic Lateral Sclerosis/cerebrospinal fluid , Complement Activating Enzymes/analysis , Complement Activating Enzymes/standards , Complement C1/analysis , Complement C1/standards , Complement C1q , Enzyme-Linked Immunosorbent Assay/standards , Humans , Immunodiffusion , Middle Aged , Reference Standards
12.
Cancer Res ; 48(20): 5868-73, 1988 Oct 15.
Article in English | MEDLINE | ID: mdl-3262415

ABSTRACT

Ninety-five untreated patients with squamous cell carcinoma of the upper aerodigestive tract expressed significantly higher levels of C1q-binding macromolecules as compared to 45 noncancer-bearing controls. No relationship between C1q-binding macromolecules and levels of circulating IgG-immune complexes as determined by the solid-phase C1q-binding assay or the C3d-solid-phase assay could be defined suggesting that C1q-binding macromolecules were distinct from IgG-circulating immune complexes. An elevated level of C1q-binding macromolecules within these patients was predictive of subsequent response to induction chemotherapy; those with elevated levels characteristically showed no response. Using multivariate logistic regression analysis including the covariates of American Joint Committee staging parameters as well as C1q assay results, levels of the isolated macromolecules added significant prognostic information as to the probability of chemotherapeutic response. The quantitation of C1q macromolecules has clinical implication as to choice of therapeutic regimens against head and neck cancer. The nature of these substances remains to be defined.


Subject(s)
Carcinoma, Squamous Cell/blood , Complement Activating Enzymes/analysis , Complement C1/analysis , Head and Neck Neoplasms/blood , Adult , Aged , Aged, 80 and over , Carcinoma, Squamous Cell/drug therapy , Complement C1q , Female , Head and Neck Neoplasms/drug therapy , Humans , Macromolecular Substances , Male , Middle Aged , Protein Binding
13.
Z Gesamte Inn Med ; 43(18): 511-4, 1988 Sep 15.
Article in German | MEDLINE | ID: mdl-2974223

ABSTRACT

In the period of 1975-1983 twenty-three patients with thromboangiitis obliterans were examined at the Surgical Clinic of the Medical Academy of Magdeburg. The diagnosis was established clinically, angiographically histologically and immunologically. In 7 out of 12 patients histology revealed inflammatory vascular alterations including lymphocyte infiltrates throughout the entire vessel wall and also in the perivascular area. Immunohistology showed in 10 out of 15 patients segmental granular fluorescence identifiable as deposits of IgM and IgG. In 6 cases a complement formation was found. The endangiitis group revealed more frequent and increased immune complexes concentrations. Circulating immune complexes were established by phase-locked radio-immunoassay. The therapy is depended on the localization of the obliteration and can be a lumbar sympathectomy or a vascular reconstruction.


Subject(s)
Complement Activating Enzymes/analysis , Complement C1/analysis , Immune Complex Diseases/pathology , Immunoglobulin G/analysis , Immunoglobulin M/analysis , Thromboangiitis Obliterans/pathology , Adult , Arteries/pathology , Complement C1q , Fluorescent Antibody Technique , Humans , Male , Prognosis , Thromboangiitis Obliterans/surgery
14.
Inflammation ; 12(4): 351-60, 1988 Aug.
Article in English | MEDLINE | ID: mdl-3262584

ABSTRACT

RHP is a recently described serum protein which inhibits a number of physiologic functions of C1q unbound to C1r2 x C1s2. In this report we show that sera from patients with rheumatoid arthritis contained elevated levels of RHP and of unbound C1q. Sera from patients with systemic lupus erythematosus contained normal levels of RHP and were characterized by deficits of C1q required to form C1 from existing levels of C1r and C1s.


Subject(s)
Arthritis, Rheumatoid/blood , Blood Proteins/analysis , Complement Activating Enzymes/analysis , Complement C1 Inactivator Proteins/analysis , Complement C1/analysis , Lupus Erythematosus, Systemic/blood , Adult , Aged , Complement C1q , Female , Humans , Male , Middle Aged
16.
J Rheumatol ; 15(7): 1091-6, 1988 Jul.
Article in English | MEDLINE | ID: mdl-2845080

ABSTRACT

Our study was undertaken to determine if native DNA (dsDNA), which is known to bind to collagen, also binds to the collagen-like segment of Clq (CLS). Three methods were employed to demonstrate the binding of dsDNA to CLS: (1) Six human sera and a mouse monoclonal antibody to dsDNA were employed in an enzyme linked immunosorbent assay to detect CLS bound dsDNA. When applied to CLS bound dsDNA, sera with antibodies to dsDNA and monoclonal antibody to DNA yielded mean OD values of greater than or equal to 0.6, significantly higher than those values obtained from control experiments (mean OD less than or equal to 0.2, p less than or equal to 0.003). (2) In a solid phase immunoassay radiolabelled DNA (3H DNA) was exposed to increasing amounts of solid phase adherent CLS. The binding of 3H DNA to the solid phase was substantially greater (more than a 30-fold increase) when the solid phase had been precoated with CLS. (3) dsDNA binding to CLS was demonstrated further by incubating electrophoretically resolved CLS with dsDNA and localizing the bound dsDNA by ethidium bromide staining. Our results indicate the dsDNA binds to CLS. Since CLS is the binding site for Clr and then Clr2Cls2, molecules which bind to CLS, such as dsDNA, could be important factors affecting Cl activation.


Subject(s)
Collagen/genetics , Complement Activating Enzymes/metabolism , Complement C1/metabolism , DNA/metabolism , Complement Activating Enzymes/analysis , Complement Activating Enzymes/genetics , Complement Activation , Complement C1/analysis , Complement C1/genetics , Complement C1q , Diffusion , Electrophoresis, Polyacrylamide Gel , Enzyme-Linked Immunosorbent Assay , Humans , Microbial Collagenase/pharmacology , Molecular Weight
17.
Am J Vet Res ; 49(6): 865-9, 1988 Jun.
Article in English | MEDLINE | ID: mdl-3135770

ABSTRACT

The complement subcomponent, C1q, was isolated from serum obtained from clinically normal dogs, using a rapid 2-step process involving affinity chromatography. Yield of C1q ranged from 8 to 10 mg/L of serum. Hemolytically active C1q had 3 protein bands after sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing conditions and formed a single line of identity with rabbit anti-canine C1q. The amino acid composition of canine C1q was similar to that of human C1q and contained a high percentage of glycine. Isolated canine C1q was iodinated, and the fluid-phase binding assay was used to detect circulating immune complexes in dogs with systemic lupus erythematosus and rheumatoid arthritis.


Subject(s)
Antigen-Antibody Complex/analysis , Complement Activating Enzymes/isolation & purification , Complement C1/isolation & purification , Amino Acids/analysis , Animals , Arthritis, Rheumatoid/diagnosis , Arthritis, Rheumatoid/veterinary , Chromatography, Affinity , Complement Activating Enzymes/analysis , Complement Activating Enzymes/immunology , Complement C1/analysis , Complement C1/immunology , Complement C1q , Dog Diseases/diagnosis , Dogs , Electrophoresis, Polyacrylamide Gel , Hemolytic Plaque Technique , Immunodiffusion , Lupus Erythematosus, Systemic/diagnosis , Lupus Erythematosus, Systemic/veterinary
18.
Curr Eye Res ; 7(3): 277-86, 1988 Mar.
Article in English | MEDLINE | ID: mdl-3258806

ABSTRACT

We studied 8 soft contact lenses from asymptomatic wearers by means of an immunocytochemical method, in transmission electron microscopy. In particular, the presence of IgA, IgG, IgE, Clq complement fraction within the surface deposits was analyzed. All the lenses were found positive for the immunoglobulins and the Clq, being the tarsal side more heavily coated than the corneal one. IgA was the predominant Ig, followed by IgG, IgE, and Clq in this descending order. New, never worn lenses were found completely negative for any of the proteins under investigation. We conclude that the Igs come from the tear fluid and speculate about the Clq as a possible sign of involvement of the host immuno-defense mechanism against the prosthesis.


Subject(s)
Complement Activating Enzymes/analysis , Complement C1/analysis , Contact Lenses, Hydrophilic/adverse effects , Immunoglobulins/analysis , Adult , Complement C1q , Female , Humans , Immunoglobulin A/analysis , Immunoglobulin E/analysis , Immunoglobulin G/analysis , Immunohistochemistry , Male , Microscopy, Electron , Tears/analysis , Tears/immunology
20.
Clin Immunol Immunopathol ; 46(1): 14-23, 1988 Jan.
Article in English | MEDLINE | ID: mdl-3257175

ABSTRACT

The aim of the present study was to isolate and characterize immune complexes measured by the 125I-C1q binding assay in breast cancer sera. The C1q binding assay detects immune complexes by their binding to 125I-C1q and subsequent precipitation with PEG. We purified the C1q binding material from these precipitates by superose 6 gel filtration and cation exchange chromatography. The isolation steps were monitored by the C1q binding assay and the purified material was analyzed by SDS--PAGE and immunodiffusion. The C1q binding material isolated from two breast cancer sera contained complexes of IgM, C4b binding protein (C4-bp), and C1q. The C4-bp fraction showed significant C1q binding activity which increased after the addition of IgM. This C4-bp was not different from C4-bp isolated from normal serum. The IgM fraction, however, differed from normal IgM by its binding to C4-bp and C1q and its stronger affinity to the cation exchange column. These unique properties were not due to rheumatoid factor activity. They might be caused by a different glycosylation pattern or by complex formation with an as yet unknown polysaccharide antigen.


Subject(s)
Antigen-Antibody Complex/analysis , Antigens, Neoplasm/analysis , Breast Neoplasms/immunology , Complement Activating Enzymes/analysis , Complement C1/analysis , Antibodies, Neoplasm/immunology , Carrier Proteins/analysis , Chromatography, Gel , Chromatography, Ion Exchange , Complement C1q , Humans , Immunoglobulin M/analysis , Integrin alphaXbeta2 , Neoplasm Proteins/analysis
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