Search PubMedSearch

PubMed · 1775266

Dialysis membranes decrease immunoglobulin and interleukin-6 production by peripheral blood mononuclear cells in vitro.

Abstract

In order to determine the influence of dialysis membranes on immunoglobulin (Ig) and interleukin-6 (IL-6) production, peripheral blood mononuclear cells (PBMC) from 11 haemodialysis patients were cultured for 7 days on Cuprophan, Hemophan, and polyacrylonitrile flat-sheet dialysis membranes. IL-6, IgG, IgA, and IgM were assayed in the supernatants using ELISA. Pokeweed-mitogen-stimulated IgG production declined significantly from 319 +/- 40 ng/ml on polystyrole to 162 +/- 26 ng/ml on Cuprophan, 135 +/- 25 ng/ml on Hemophan, and 109 +/- 20 ng/ml on polyacrylonitrile. A similar pattern was observed for IgA production by PBMC. In comparison to polystyrole (724 +/- 34 pg/ml), IL-6 production by PBMC was significantly reduced in the presence of Cuprophan (151 +/- 45 pg/ml), Hemophan (167 +/- 6 pg/ml) and polyacrylonitrile (108 +/- 33 pg/ml). The fact that the level of monocyte-derived IL-6, a stimulator of B cells, was decreased suggests that reduced B cell activity may be due to diminished stimulation by monocytes.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

L Paczek, R M Schaefer, A Heidland. 1991. Dialysis membranes decrease immunoglobulin and interleukin-6 production by peripheral blood mononuclear cells in vitro.. https://pubmed.ncbi.nlm.nih.gov/1775266/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Pathophysiology of the MELAS 3243 transition mutation.

Single base substitutions of the mitochondrial genome are associated with a variety of metabolic disorders. The myopathy, encephalopathy, lactic acidosis, stroke-like episodes syndrome, most frequently associated with an A to G transition mutation at position 3243 of the mitochondrial tRNALeu(UUR) gene, is characterized by biochemical and structural alterations of mitochondria. To investigate the pathophysiology of the mutation, we established distinct Epstein-Barr virus-transformed B-cell lines for analyses that harbored 30-70% of the mutated genome. Interestingly, neither an alteration of the processing of primary transcripts nor a general impairment of individual mitochondrial protein subunit synthesis rates could be observed. Nevertheless a marked decrease of cytochrome-c oxidase activity and reduced content of mitochondrial encoded subunits in the assembled respiratory complex IV was recorded on the cell line harboring 70% mutated mtDNA. Quantitative analysis of incorporation rates of the amino acid leucine into newly synthesized mitochondrial proteins, representing the functionality of the tRNALeu(UUR) in protein biosynthesis, revealed a specific decrease of this amino acid in distinct mitochondrial translation products. This observation was supported by a variation in the proteolytic fingerprint pattern. Our results suggest that the malfunctioning mitochondrial tRNALeu(UUR) leads to an alteration of amino acid incorporation into the mitochondrially synthesized subunits of the oxidative phosphorylation system, thus altering it's structure and function.

B-Lymphocytes

Longitudinal study of HIV-specific cytotoxic lymphocytes in HIV type 1-infected patients: relative balance between host immune response and the spread of HIV type 1 infection.

To evaluate the contribution of a specific cytotoxic response in the control of HIV infection in relation to clinical status, we performed serial analysis of anti-Env and anti-Gag cytotoxic activity in 13 infected individuals over a 6- to 10-year period, using cryopreserved peripheral blood mononuclear cells (PBMCs). Autologous EBV-transformed B cell lines infected in vitro with recombinant vaccinia viruses expressing HIV-1 env and gag genes were used as targets. Without any stimulation of the effector cells, we were able to show an anti-HIV cytotoxic activity in the PBMCs of 12 of 13 HIV-1-infected patients, consistent with chronic immune activation in HIV infection. Different patterns of HIV-specific cytotoxic activity were observed, and the extent of this cytotoxic response varied between the clinically defined groups of individuals. No direct relationship was observed with the number of CD4 and CD8 lymphocytes during the observation period. However, patients who remained asymptomatic had a more vigorous cytotoxic response than patients with clinical deterioration during the observation period, and a significant difference was observed for HIV Gag-specific CTL activity. From these data, we suggest that the HIV-specific cytotoxic response has a protective role in the course of HIV infection.

B-Lymphocytes

The DNA binding domain of the A-MYB transcription factor is responsible for its B cell-specific activity and binds to a B cell 110-kDa nuclear protein.

Expression studies as well as the use of transgenic animals have demonstrated that the A-MYB transcription factor plays central and specific role in the regulation of mature B cell proliferation and/or differentiation. Furthermore, it is highly expressed in Burkitt's lymphoma cells and may participate in the pathogenesis of this disease. We have therefore investigated the transcriptional activity of A-MYB and its regulation in several human lymphoid cell lines using co-transfection assays and show that A-MYB is transcriptionally active in all the B cell lines studied, but not in T cells. In particular the best responder cell line was the Burkitt's cell line Namalwa. The activity of A-MYB in B and not T cells was observed when either an artificial construct or the c-MYC promoter was used as a reporter. Furthermore, the functional domains responsible for DNA binding, transactivation, and negative regulation, previously characterized in a fibroblast context, were found to have similar activity in B cells. The region of A-MYB responsible for the B cell specific activity was defined to be the N-terminal 218 amino acids containing the DNA binding domain. Finally, a 110-kDa protein has been identified in the nuclei of all the B, but not T, cell lines that specifically binds to this A-MYB N-terminal domain. We hypothesize that this 110-kDa protein may be a functionally important B cell-specific co-activator of A-MYB.

B-Lymphocytes