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Immunoglobulin production

The early immunoglobulin products prepared by cold-ethanol fractionation were found to be free from transmitting hepatitis infection (106,108) this was not the case with products prepared by alternative methods (109). Subsequentiy, some batches of intravenous immunoglobulin transmitted hepatitis infection (110), emphasizing the importance of estabHshing vaHdated procedures for dealing with potential viral contaminants (111). [Pg.530]

The resuspended and formulated Fraction II precipitate normally contains some aggregated IgG and trace substances that can cause hypotensive reactions in patients, such as the enzyme prekail ikrein activator (186). These features restrict this type of product to intramuscular adininistration. Further processing is required if products suitable for intravenous adininistration are required. Processes used for this purpose include treatment at pH 4 with the enzyme pepsin [9001-75-6] being added if necessary (131,184), or further purification by ion-exchange chromatography (44). These and other methods have been fiiUy reviewed (45,185,187,188). Intravenous immunoglobulin products are usually suppHed in the freeze-dried state but a product stable in the solution state is also available (189). [Pg.532]

One component of the age-ielated decline in immune function is decreased production of the lymphokine that promotes the growth of T-ceUs, interleukin 2 (IL-2). Administration of recombinant-derived IL-2, both in vitro and in vivo, appears to restore certain immune functions in aged mice. Recovery of T-regulatory effects on B-ceU differentiation has been reported in human cells from elderly patients treated with IL-1 and/or IL-2 (42). Similar effects have been observed in the presence of the pentapeptide thymopentin [69558-55-0] (Arg Lys Asp Val Tyr), a weU-known IL-2 inducer. Recombinant IL-2 adrninistered to aged mice for three weeks has been shown to correct the T-ceU functional deficiency associated with antigen-specific immunoglobulin production by certain lymphoid tissue (43). [Pg.431]

Peters M, Waiting DM, Kelly K, Davis GL, Waggoner JG, Hoofnagle JH (1986) Immunologic effects of interferon-alpha in man treatment with human recombinant interferon-alpha suppresses in vitro immunoglobulin production in patients with chronic type B hepatitis. J Immunol 137 3147-3152... [Pg.239]

Jyonouchi, H., Sun, S., and Gross, M., Effect of carotenoids on in vitro immunoglobulin production by human peripheral blood mononuclear cells astaxanthin, a carotenoid without vitamin A activity, enhances in vitro immunoglobulin production in response to a T-dependent stimulant and antigen, Nutr. Cancer, 23, 171, 1994. [Pg.423]

Breitfeld D, Ohl L, Kremmer E, et al. Follicular B helper T cells express CXC chemokine receptor 5, localize to B cell follicles, and support immunoglobulin production. J Exp Med 2000 192 1545-1552. [Pg.113]

Tsuji, T., et al. Efficient induction of immunoglobulin production in neonatal naive B cells by memory CD4+ T cell subset expressing homing receptor L-selectin, J. Immunol., 152, 4417, 1994. [Pg.340]

If the product is an antibody, then it is essential to distinguish the immunoglobulin product, e.g., mouse IgG, from any media immunoglobulin components, e.g., bovine IgG. Lucas et al.16 developed an immunoassay to measure nanogram quantities of bovine IgG in the presence of a large excess of a structurally homologous protein, mouse MAb. The bovine IgG was a contaminant that copurified with the product from a protein A column. For the bovine IgG assay, whole IgG and protein A-purified IgG reacted differently in the assay. It is important to evaluate these types of assays for cross-reactivity. For other media components, such as chemicals or antibiotics, ELISA is probably not the most appropriate method due to the low immunogenicity of chemicals. Techniques such as HPLC would be better to detect these chemical components. [Pg.291]

Aukrust, P., Mulle, F., Ueland, T., Svardal, A. M., Berge, R. K., and Froland, S. S. (2000). Decreased vitamin A levels in common variable immunodeficiency Vitamin A supplementation in vivo enhances immunoglobulin production and downregulates inflammatory response. Eur. J. Clin. Invest. 30, 252-259. [Pg.210]

Azathioprine acts through its major metabolite, 6-thioguanine. 6-Thioguanine suppresses inosinic acid synthesis, -cell and T-cell function, immunoglobulin production, and interleukin-2 secretion (see Chapter 55). [Pg.806]

The mTOR is a key component of a complex intracellular signaling pathway involved in cellular processes such as cell growth and proliferation, angiogenesis, and metabolism. Thus, blockade of mTOR ultimately can lead to inhibition of interleukin-driven T-cell proliferation. Both everolimus and sirolimus also may inhibit -cell proliferation and immunoglobulin production. [Pg.1191]

Benzene is such a chemical that damages the bone marrow, and aplastic anemia results. This has several effects, one of which is a reduction in the lymphocyte as well as red cell population and so pancytopenia and therefore immunosuppression results. This leads to an increased susceptibility to infection and inhibited immunoglobulin production. These effects have been detected in both experimental animals and humans occupationally exposed to benzene. Thus, shoe workers in Turkey and China have been found to suffer aplastic anemia. [Pg.248]

Kim HS, Raskova J, Degiannis D, Raska K Jr. Effects of cyclosporine and rapamycin on immunoglobulin production by preactivated human B cells. Clin Exp Immunol 1994 96 508-512. [Pg.322]

Bree MA, Dhurjati P, Geoghegan R, Robnett B (1988), Kinetic modeling of hybridoma cell growth and immunoglobulin production in a large-scale suspensions culture, Biotechnol. Bioeng. 32 1067—1072. [Pg.218]

Hata, I., Higasiyama, S., and Otani, H. 1998. Identification of a phosphopeptide in bovine asl-casein digest as a factor influencing proliferation and immunoglobulin production in lymphocyte cultures. J. Dairy Res. 65, 569—578. [Pg.256]

What consequences of immunoglobulin production against glucocerebrosidase might occur in a patient receiving placental enzyme replacement therapy ... [Pg.179]

In addition to cancer, too little apoptosis can also result in diseases such as autoimmune lymphoproliferative syndrome (ALPS). This occurs when there is insufficient apoptosis of auto-aggressive T cells, resulting in multiple autoimmune diseases. An overproliferation of B cells occurs as well, resulting in excess immunoglobulin production, leading to autoimmunity. Some of the common diseases of ALPS include hemolytic anemia, immune-mediated thrombocytopenia, and autoimmune neutropenia. The different types of this condition are caused by different mutations. Type 1A results from a mutation in the death domain of the Fas receptor, Type IB results from a mutation in Fas ligand, and Type 2 results from a mutation in caspase 10, reducing its activity. [Pg.312]

Supraphysiological doses of 1,25-(OH)2D3 produce immunosuppressive effects by causing depletion of thymocytes and decreased immunoglobulin production in mice [365]. A further study of these effects by 1,25-(OH)2D3 showed that hypercalcaemia, induced by 1,25-(OH)2D3 treatment (20 ng/d for 4 days) markedly decreased thymus weight, thymocyte number, and in particular caused atrophy of immature thymocyte subpopulations which re-... [Pg.39]

Lemire JM, Adams JS, Sakai R, and Jordan SC (1984) 1 alpha,25-Dihydroxyvitamin D3 suppresses proliferation and immunoglobulin production by normal human peripheral blood mononuclear cells. Journal of Clinical Investigation 74,657-61. [Pg.436]

Figure 33.1. Immunoglobulin Production. An electron micrograph of a plasma cell shows the highly developed rough endoplasmic reticulum necessary for antibody secretion. [Courtesy of Lynne Mercer.]... Figure 33.1. Immunoglobulin Production. An electron micrograph of a plasma cell shows the highly developed rough endoplasmic reticulum necessary for antibody secretion. [Courtesy of Lynne Mercer.]...
Teschner, W. et al., A new hquid, intravenous immunoglobulin product (IglV 10%) highly purified by a state-of-the-art process. Vox Sang., 92, 42-45, 2007. [Pg.425]

Hamalainen, E. Suomela, H. Ukkonen, P. Virus inactivation during intravenous immunoglobulin production. Vox Sang. 1992, 63, 6-11. [Pg.4012]

Reid, K.G. Cuthbertson, B. Jones, A.D.L. McIntosh, R.V. Potential contribution of mild pepsin treatment at pH 4 to the viral safety of human immunoglobulin products. Vox Sang. 1988, 55, 75-80. [Pg.4012]


See other pages where Immunoglobulin production is mentioned: [Pg.532]    [Pg.444]    [Pg.49]    [Pg.63]    [Pg.411]    [Pg.196]    [Pg.164]    [Pg.1196]    [Pg.72]    [Pg.158]    [Pg.271]    [Pg.188]    [Pg.433]    [Pg.1340]    [Pg.1346]    [Pg.116]    [Pg.393]    [Pg.443]    [Pg.283]    [Pg.220]    [Pg.39]    [Pg.98]    [Pg.74]    [Pg.136]    [Pg.4012]    [Pg.1722]   
See also in sourсe #XX -- [ Pg.35 , Pg.36 ]




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