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  • 1
    Electronic Resource
    Electronic Resource
    Alcohol dehydrogenase-I from horse liver stimulates immunoglobulin production by human hybridoma and human peripheral blood lymphocytes (1997)
    Springer
    Molecular and cellular biochemistry 173 (1997), S. 1-7 
    Details
    ISSN: 1573-4919
    Keywords: alcohol dehydrogenase-I ; human-human hybridoma ; human peripheral blood lymphocyte ; immunoglobulin productionstimulating factor ; serum-free culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Immunoglobulin production stimulating activity of alcohol dehydrogenase[EC 1.1.1.1] was assessed. Alcohol dehydrogenase-I (ADH-I) derived fromhorse liver stimulated IgM production by human-human hybridoma, HB4C5 cellsproducing human lung cancer specific monoclonal IgM. IgM production of HB4C5cells was enhanced more than 6 fold by the addition of ADH-I at 400µg/ml under serum-free condition. However, yeast derived ADHs, such asADH-II and -III were ineffective to accelerate immunoglobulin production ofthe hybridoma line. These results imply that the immunoglobulin productionstimulating effect of ADH-I is irrelevant to its enzymatic function, anddefined as a novel feature of ADH-I. This enzyme also stimulated IgM and IgGproduction by human peripheral blood lymphocytes 2.9 fold and 1.4 fold,respectively . This fact suggests that ADH-I stimulates immunoglobulinproduction not only by specific hybridoma cell line, but also bynon-specific immunoglobulin producers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006883828460
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  • 2
    Electronic Resource
    Electronic Resource
    Lysozyme stimulates immunoglobulin production by human-human hybridoma and human peripheral blood lymphocytes (1997)
    Springer
    Cytotechnology 24 (1997), S. 177-182 
    Details
    ISSN: 1573-0778
    Keywords: human-human hybridoma ; human peripheral blood lymphocytes ; immunoglobulin production stimulating factor (IPSF) ; lysozyme ; serum-free culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Lysozyme [EC 3.2.1.17] derived from hen egg white stimulated immunoglobulin production by human-human hybridoma, HB4C5 cells producing human lung cancer specific monoclonal IgM. IgM production by HB4C5 cells was enhanced more than 13-fold by the addition of lysozyme at 380 μg/ml in a serum-free medium. The immunoglobulin production stimulating effect of lysozyme was observed immediately after inoculation and maintained for 5 days. Lysozyme enhanced immunoglobulin production by the hybridoma line without growth promotion. This enzyme also accelerated IgM and IgG production of human peripheral blood lymphocytes 5.3-fold and 2.3-fold, respectively. These results suggest that lysozyme stimulates immunoglobuling production of not only specific hybridoma line, but also non-specific immunoglobulin producers. However, although the enzymatic activity of lysozyme was almost lost by heat-treatment at 100 °C for 30 min, the IPSF activity was retained. This fact suggests that IPSF activity of lysozyme does not come from its enzymatic activity or reaction products. All these findings clearly indicate that lysozyme has a novel function as an immunoglobulin production stimulating factor. GAPDH - glyceraldehyde-3-phosphate dehydrogenase; Ig - immunoglobulin; IPSF - immunoglobulin production stimulating factor; PBL - peripheral blood lymphocytes; HPLC - high-performance liquid chromatography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007936629501
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  • 3
    Electronic Resource
    Electronic Resource
    Purification and characterization of immunoglobulin production stimulating factor derived from human B lymphoblastoid HO-323 cells (1990)
    Springer
    Cytotechnology 3 (1990), S. 189-197 
    Details
    ISSN: 1573-0778
    Keywords: immunoglobulin production stimulating factor ; human B lymphoblastoid cell line HO-323 ; hybridoma ; serum-free culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An immunoglobulin (Ig) production stimulating factor (IPSF) for hybridomas was found in spent medium of the human B lymphoblastoid cell line, HO-323. The IPSF was purified by serial use of DEAE chromatography, ultrafiltration, gel filtration and HPLC-DEAE chromatography. Purified IPSF was estimated to be a 410 k macro molecule by gel filtration, and contained three types of isomers which were separated from each other by native polyacrylamide gel electrophoresis. All of the isomers were, however, assumed to have the same protein components by SDS polyacrylamide gel electrophoresis. The IPSF was effective for human-human and mouse-mouse hybridomas producing IgM, but not for IgG producers in the experimental condition used here. Human-human hybridoma HF10B4, cultured in IPSF-containing medium, produced 20 times more IgM than in IPSF-free medium under serum-free conditions. The IPSF showed very little proliferation stimulating activity on HF10B4 cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00143681
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  • 4
    Electronic Resource
    Electronic Resource
    Effects of organic pH buffers on a cell growth and an antibody production of human-human hybridoma HB4C5 cells in a serum-free culture (1995)
    Springer
    Cytotechnology 17 (1995), S. 117-125 
    Details
    ISSN: 1573-0778
    Keywords: antibody production ; cell growth ; chemical structure ; human-human hybridoma ; organic conceptual diagram ; organic pH buffer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Human-human hybridoma cells secreting a human monoclonal antibody were cultured in a serum-free medium containing various organic pH buffers in order to clarify their effects on cell growth and antibody production. Organic pH buffers having either one sulfonic acid and several acyclic amine moieties, or several cyclic amine moieties containing two amino nitrogen did not inhibit cell growth; while other organic buffers sulfonic acid moiety plus several cyclic amine moieties containing one amino nitrogen slightly decreased cell growth, but enhanced antibody production. Using Fujita's organic conceptual diagram, a relationship between the organicity and inorganicity of a pH buffer to cell growth and antibody production was found. pH buffers with large inorganicity and small organicity values were favorable for cell growth, and buffers with small inorganicity and large organicity values were preferred to enhance antibody production. Although the pH buffering range affects cell growth, its effect on antibody production is not clear. In conclusion, 2-morpholinoethanesulfonic acid (MES), 3-morpholino-propanesulfonic acid (MOPS) and 1, 2-N, N′-bis[N″, N‴-di(2-sulfonoethyl)piperazinyl]ethane (Bis-PIPES) are shown to be the most optimal of the buffers tested, because they enhanced antibody production without decreasing the cell growth among the pH buffers tested here.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00749399
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  • 5
    Electronic Resource
    Electronic Resource
    Effects of DNA on immunoglobulin production stimulating activity of alcohol dehydrogenase (1999)
    Springer
    Cytotechnology 31 (1999), S. 95-102 
    Details
    ISSN: 1573-0778
    Keywords: alcohol dehydrogenase-I ; deoxyribonucleic acid (DNA) ; human-human hybridoma ; immunoglobulin production stimulating factor (IPSF) ; serum-free culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Alcohol dehydrogenase-I (ADH-I) derived from horse liver stimulated IgM production by human-human hybridoma, HB4C5 cells and lymphocytes. The IPSF activity of ADH-I was suppressed by coexistence of short DNA whose chain length is less than 200 base pairs (bp) and fibrous DNA in a dose-dependent manner. These DNA preparations completely inhibited the IPSF activity at the concentration of 250 μg/ml and 1.0 mg/ml, respectively. DNA sample termed long DNA whose average chain length is 400–7000 bp slightly stimulated IPSF activity at 0.06 μg/ml. However, long DNA suppressed IPSF activity by half at 1.0 mg/ml. The laser confocal microscopic analysis had revealed that ADH-I was incorporated by HB4C5 cells. The uptake of ADH-I was strongly inhibited by short DNA and fibrous DNA. However, long DNA did not suppress the internalization of ADH-I into HB4C5 cells. These findings indicate that short DNA and fibrous DNA depress IPSF activity of ADH-I by inhibiting the internalization of this enzyme. According to the gel-filtration analysis using HPLC, ADH-I did not directly interact with short DNA. It is expected from these findings that short DNA influences HB4C5 cells to suppress the internalization of ADH-I. Moreover, these facts also strongly suggest that ADH-I acts as IPSF after internalization into the cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008024322602
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  • 6
    Electronic Resource
    Electronic Resource
    Stimulation of proliferation and immunoglobulin M production by lactoferrin in human-human and mouse-mouse hybridomas cultures in serum-free conditions (1990)
    Springer
    Cytotechnology 3 (1990), S. 123-131 
    Details
    ISSN: 1573-0778
    Keywords: lactoferrin ; stimulation of IgM production ; human-human hybridomas ; serum-free culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The effects of growth factors, such as insulin, transferrin, lactoferrin, ethanolamine, and selenium, on proliferation and IgM production of human-human hybridomas HB4C5 cells in a serum-free enriched RDF (eRDF) medium were studied. Among them, lactoferrin markedly stimulated proliferation and IgM production of the cells. Another iron-binding protein, transferrin, stimulated proliferation of HB4C5 cells as well as lactoferrin, but its stimulatory effect on IgM production was negligible. The proliferation and IgM production of HB4C5 cells gave some detectable delays in conventional ITES-eRDF medium at low cell densities, but the delays were avoided by the addition of lactoferrin. However, eRDF medium supplemented with lactoferrin could not support proliferation and IgM production of the cells at high cell densities. For proliferation and IgM production of HB4C5 cells, eRDF medium supplemented with 25 μg/ml lactoferrin, 10μM ethanolamine, 35 μ/ml transferrin, and 2.5 nM selenium (LETS-eRDF) gave the best result. Lactoferrin stimulated proliferation of human-human and mouse-mouse hybridomas producing IgG or IgM, but stimulation of Ig production was detected only in IgM producers. These results suggest that cell proliferation, IgM production, and IgG production of hybridomas are regulated by different mechanisms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00143674
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  • 7
    Electronic Resource
    Electronic Resource
    Purification and characterization of immunoglobulin production stimulating factor-IIβ derived from Namalwa cells (1992)
    Springer
    Cytotechnology 10 (1992), S. 137-146 
    Details
    ISSN: 1573-0778
    Keywords: immunoglobulin production stimulating factor human ; enolase α-chain ; Burkitt's lymphoma cell line Namalwa cells ; human-human hybridoma ; serum-free medium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Two immunoglobulin production stimulating factors (IPSF) have been found in human Burkitt's lymphoma Namalwa cells. One IPSF named IPSF-IIα was purified and identified as glyceraldehyde-3-phosphate dehydrogenase as previously reported. We report here purification, identification and characterization of IPSF-IIβ. IPSF-IIβ was purified by the serial use of ammonium sulfate fractionation, hydrophobic interaction column chromatography, anion-exchange column chromatography and gel filtration. The IPSF-IIβ was estimated as a 46 KD monomeric polypeptide by gel filtration and SDS-PAGE. Partial amino acid sequence of the 46 KD protein was analyzed for 26 amino acid residues. The sequence very closely coincided with enolase (EC 4.2.1.11) derived from various origins and, it was completely homologous with that of human enolase α-chain. Rabbit muscle enolase stimulated IgM production of hybridoma lines, and IPSF-IIβ had the enzymic activity. These results suggested that IPSF-IIβ was α-enolase or its isozyme. IPSF activities of IPSF-IIβ was stable in alkaline conditions whereas the enzymic activity was rapidly lost in alkaline conditions. Though IPSF-IIβ stimulated IgM production of both human-human and mouse-mouse hybridoma lines in serum-free condition, it partially suppressed IgE production of mouse-mouse hybridoma lines.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00570890
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  • 8
    Electronic Resource
    Electronic Resource
    Purification of immunoglobulin production stimulation factor II α derived from Namalwa cells (1991)
    Springer
    Cytotechnology 5 (1991), S. 255-263 
    Details
    ISSN: 1573-0778
    Keywords: immunoglobulin production stimulating factor ; human lymphoblastoid Namalwa cells ; human-human hybridomas ; serum-free culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract An immunoglobulin production stimulating factor (IPSF) in human lymphoblastoid Namalwa cells was purified by the serial use of ammonium sulfate fractionation, hydrophobic interaction chromatography and gel filtration, and named IPSF-II α. IPSF-II α was estimated as a 112 KD protein composed of a 40 KD polypeptide and two 36 KD polypeptides. The 36 KD protein extracted from SDS-polyacrylamide gel showed IPSF activity, but not the 40 KD protein. The IPSF activity was reasonably stable in alkaline but unstable in acidic solution and heat-unstable. In a serum-free medium, IPSF-II α stimulated IgM production of human-human and mouse-mouse hybridomas 4–15 and 2-fold, respectively, although its growth stimulatory effect on hybridomas was negligible. The factor did not stimulate IgG production in either human or mouse hybridomas in the same serum-free medium. These results suggested that IPSF-II α was a new cellular factor for stimulating IgM productivity of hybridomas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00556295
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  • 9
    Electronic Resource
    Electronic Resource
    Immunoglobulin production stimulating factor-IIα (IPSF-IIα) is glyceraldehyde-3-phosphate dehydrogenase like protein (1991)
    Springer
    Cytotechnology 6 (1991), S. 115-120 
    Details
    ISSN: 1573-0778
    Keywords: immunoglobulin production stimulating factor ; glyceraldehyde-3-phosphate dehydrogenase ; Burkitt's lymphoma cell line Namalwa cell ; human-human hybridoma ; serum-free medium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Amino acid sequence of the 36 KD protein which is the active subunit of immunoglobulin production stimulating factor-IIα (IPSF-IIα) derived from Burkitt's lymphoma Namalwa cells was analyzed for the 20 amino acids from N-terminus. The N-terminal amino acid sequence of this protein coincided very closely with glyceraldehyde-3-phosphate dehydrogenase (GPD; EC 1.2.1.12) derived from various origins. Especially, it was completely homologous with that of human liver GPD. Several GPD's derived from human erythrocytes, rabbit muscle and Bacillus stearothermophilus also stimulated IgM production of hybridomas, as well as IPSF-IIα. Conversely, IPSF-IIα had GPD enzymic activity as strong as rabbit muscle and B. stearothermophilus, and stronger than human erythrocytes GPD. These results suggested that 36 KD subunit of IPSF-IIα was a GPD, or GPD like protein. The level of mRNA for IgM was not enhanced by IPSF-IIα in hybridoma cells, though the IgM productivity of the cell was remarkably stimulated by the protein, indicating that IPSF-IIα does not stimulate immunoglobulin production by enhancement of transcription.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00373028
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  • 10
    Electronic Resource
    Electronic Resource
    Spermine enhances IgM productivity of human-human hybridoma HB4C5 cells and human peripheral blood lymphocytes (1998)
    Springer
    Cytotechnology 26 (1998), S. 111-118 
    Details
    ISSN: 1573-0778
    Keywords: Human-human hybridoma ; Human peripheral blood lymphocyte ; Immunoglobulin production stimulating factor ; Serum-free culture ; Spermine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The polyamine spermine was assessed for enhancement of IgM production by human-human hybridoma, HB4C5 cells, under serum-free conditions. IgM production of HB4C5 cells was stimulated approximately 6-fold by the addition of 7.3 mM of spermine. The facilitating effect was observed soon after inoculation. In spite of suppression of cell growth, the IgM production rate was accelerated for at least 5 days without medium change. Moreover, laser confocal microscopic analysis revealed that the IgM content inside HB4C5 cells was increased by spermine treatment. These findings suggest that spermine enhances specific IgM productivity of the hybridoma line. Spermine also facilitated IgM production by human peripheral blood lymphocytes under serum-free conditions. This result implies that spermine enhances immunoglobulin production of not only specific hybridoma lines, but also non-specific immunoglobulin producers. Immunoglobulin production stimulating activity of spermine was accelerated 2-fold by the addition of DNA whith a chain length of about 400–7000 base pairs (bp). However, degraded short-chain DNA fragments (less than 200 bp) did not facilitate the immunoglobulin production stimulating activity of spermine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007939213564
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