Biosynthesis of complement by human monocytes

Beatty, David M.; Davis, Alvin E.; Cole, F S; Einstein, L P; Colten, Harvey R.

doi:10.1016/0090-1229(81)90126-4

Cited by 46 publications

(15 citation statements)

References 28 publications

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“…For assay of the functional activity of each component, a dilution of culture medium was made in isotonic veronal-buffered saline (VBS) sucrose with gelatin, calcium, and magnesium, pH 7.35 (VBS sucrose) for Cl, Clq, Clr, Cls, C4, C2, and Cl inhibitor (INH) and in VBS with dextrose, magnesium, calcium, and gelatin, pH 7.35 (VBS-dextrose) for C3, C5, C6, C7, C8, C9, and B. Assays for Cl, C2, C4, and Cl INH components were done essentially as outlined by Rapp and Borsos (25) and for C3 as modified by Colten et al (26) and factor B by Beatty et al (27). Clq, Clr, and Cls assays were adapted from the Cl assay (25) using purified Cl subcomponents and EA as indicator cells for Clq and EAC1q4 for Clr and Cls assays.…”

Section: Methodsmentioning

confidence: 99%

Complement biosynthesis by the human hepatoma-derived cell line HepG2.

Morris¹,

Aden²,

Knowles³

et al. 1982

J. Clin. Invest.

236

113

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Section: Methodsmentioning

confidence: 99%

Complement biosynthesis by the human hepatoma-derived cell line HepG2.

Morris¹,

Aden²,

Knowles³

et al. 1982

J. Clin. Invest.

236

113

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“…C3 is synthesized mainly in hepatocytes [11]; however, recent studies have shown that other cells also synthesize complement components, including renal cells, monocytes, macrophages [12, 13, 14], fibroblasts [15], endothelial cells [16, 17, 18]and epithelial cells [19]. C2, C3, C4 and factor B gene expression have been detected by Northern blot analysis in the kidney of a mouse model of systemic lupus erythematosus [20].…”

Section: Introductionmentioning

confidence: 99%

Intraglomerular Synthesis of Complement C3 and Its Activation Products in IgA Nephropathy

Abe

Miyazaki²,

Koji³

et al. 2001

Nephron

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Background: Complement activation is thought to be pathologically important in IgA nephropathy (IgAN). Although C3 deposition in the mesangium is found in IgAN, the origin of C3 is not clear. We recently demonstrated intraglomerular C3 synthesis in the human kidney; however, the activation and pathological role of locally synthesized C3 remains unclear. Here we performed nonradioactive in situ hybridization for C3 mRNA and immunohistochemistry for C3 and its activation products, such as C3d and membrane attack complex (MAC), to determine whether locally produced C3 in glomeruli was activated in IgA nephropathy. Methods: Renal samples from 14 patients with IgAN and 5 with minimal change nephrotic syndrome (MCNS) were examined. Uninvolved portions of surgically removed kidneys with tumors served as normal controls. Results: C3 mRNA was not detected in glomeruli in control tissue and MCNS, but was strongly expressed in resident glomerular cells of IgAN, including mesangial cells, glomerular epithelial cells and the cells of Bowman’s capsule. Examination of serial sections disclosed that more than 70% of cells positive for C3 mRNA were also stained for C3 protein, C3d, and MAC. Double staining for in situ hybridization and immunohistochemistry also revealed that those C3 mRNA signals were present in intraglomerular cells positive for C3. The expression of C3 mRNA and MAC in glomeruli correlated significantly with the degree of mesangial matrix expansion. Conclusions: Our results demonstrated that locally synthesized C3 is activated in the glomeruli of IgAN and that its expression correlated with the severity of mesangial matrix expansion. These findings suggest that activation of C3 may be involved in tissue injury in IgAN through the formation of membrane attack complex.

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“…Factor B is synthesized in many different organs and cell types, including hepatocytes [10,11], monocytes [12][13][14][15], fibroblasts [16,17] and epithelial cells [18]. Multiple transcripts of factor B are generated in different cell types but they give rise to identical polypeptides [19,20].…”

Section: Introductionmentioning

confidence: 99%

Mice Deficient for the Complement Factor B Develop and Reproduce Normally

et al. 1998

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Pekna M, Hietala MA, Landin A, Nilsson AK, Lagerberg C, Betsholtz C, Pekny M. Mice Deficient for the Complement Factor B Develop and Reproduce Normally. Scand J Immunol 1998;47:375-380 Factor B is an essential component of the complement cascade which forms the C3 and C5 convertase of the alternative pathway. Factor B cleavage products also function as cofactors in antibody-independent monocyte-mediated cytotoxicity, macrophage spreading, plasminogen activation and proliferation of B lymphocytes. Several healthy kindreds heterozygous for the factor B null or non-functional allele have been reported but the absence of homozygous factor B deficiency in humans or in animals has been speculated to be caused by the lethality of the phenotype. Here we report the generation of factor B-deficient mice by gene targeting in vivo. These mice were born at the expected Mendelian ratio and they both develop and breed normally in a conventional animal facility. These mice represent a model of complete alternative pathway deficiency. This model enables the dissection of the complement cascade in vivo and the elucidation of the relative contribution of this complement pathway in the various physiological and pathological phenomena ascribed to the complement system.

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Biosynthesis of complement by human monocytes

Cited by 46 publications

References 28 publications

Complement biosynthesis by the human hepatoma-derived cell line HepG2.

Complement biosynthesis by the human hepatoma-derived cell line HepG2.

Intraglomerular Synthesis of Complement C3 and Its Activation Products in IgA Nephropathy

Mice Deficient for the Complement Factor B Develop and Reproduce Normally

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