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Immunoglobulin production stimulating factor-IIα (IPSF-IIα) is glyceraldehyde-3-phosphate dehydrogenase like protein

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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.

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References

  • ArcariP, MartinelliR and SalvatoreF (1984) The complete sequence of a full length cDNA for human liver glyceraldehyde 3-phosphate dehydrogenase: evidence for multiple mRNA species. Nucl. Acids Res. 12(23): 9179–9189.

    Google Scholar 

  • DavidsonDE, SajgoM, NollerHF and HarrisJI (1967) Amino acid sequence of glyceraldehyde 3-phosphate dehydrogenase from lobster muscle. Nature 216: 1181–1185.

    Google Scholar 

  • GlisinV, CrkvenjakovR and ByusC (1974) Ribonucleic acid isolated by cesium chloride centrifugation. Biochem. 13(12): 2633–2637.

    Google Scholar 

  • HarrisJI and PerhamRN (1968) Glyceraldehyde 3-phosphate dehydrogenase from pig muscle. Nature 219: 1025–1028.

    Google Scholar 

  • HollandJP, LabieniecL, SwimmerC and HollandMJ (1983) Homologous nucleotide sequences at the 5′ termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehydrogenase gene families. J. Biol. Chem. 258: 5291–5299.

    Google Scholar 

  • LaemmliUK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.

    Google Scholar 

  • MatsudairaP (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262. 21: 10035–10038.

    Google Scholar 

  • MurakamiH, HashizumeS, OhashiH, ShinoharaK, YasumotoK, NomotoK and OmuraH (1985) Human-human hybridomas secreting antibodies specific to human lung carcinoma. In Vitro Cell. Develop. Biol. 21: 593–596.

    Google Scholar 

  • NowakK, WolnyM and BanasT (1981) The complete amino acid sequence pf human muscle glyceraldehyde 3-phosphate dehydrogenase. FEBS Letters 134: 143–146.

    Google Scholar 

  • PanabieresF, PiechaczykM, RainerB, DaniCH, FortPH, RiaadS, MartyL, ImbachJL, JeanteurPH and BlanchardJM (1984) Complete nucleotide sequence of the messenger RNA coding for chicken muscle glyceraldehyde 3-phosphate dehydrogenase. Bioch. Biophys. Res. Com. 118: 767–773.

    Google Scholar 

  • RyazanovAG (1985) Glyceraldehyde-3-phosphate dehydrogenase is one of the three major RNA-binding proteins of rabbit reticulocytes. FEBS letters 192: 131–134.

    Google Scholar 

  • SarkerG and SommerSS (1988) RNA amplification with transcript sequencing. Nucl. Acids Res. 16: 5197.

    Google Scholar 

  • SindeyFV (1955) Glyceraldehyde-3-phosphate dehydrogenase from muscle. Methods in Enzymol. 1: 401–406.

    Google Scholar 

  • SinmotoH, MurakamiH, YamadaK, DosakoS and OmuraH (1988) Immunoglobulin production stimulating and inhibiting factor derived from human lung adenocarcinoma PC-8 cells. Cytotechnology 1: 295–300.

    Google Scholar 

  • SugaharaT, ShirahataS, YamadaK and MurakamiH (1991) Purification of immunoglobulin production stimulating factor IIα derived from Namalwa cells. Cytotechnology 5:255–263.

    Google Scholar 

  • ToyodaK, SugaharaT, InoueK, YamadaK, ShirahataS and MurakamiH (1990) Purification and characterization of the immunoglobulin production stimulating factor derived from human B lymphoblastoid cell HC-323. Cytotechnology 3: 189–197.

    Google Scholar 

  • UllrichA, ShineJ, ChirgwinJ, PictetR, TischerE and RutterW (1977) Rat insulin gene: Construction of plasmids containing the coding sequences. Science 169: 1313–1319.

    Google Scholar 

  • WalkerJE, CarneAF, RunswickMJ, BridgenJ and HarrisJI (1980) D-glyceraldehyde-3-phosphate dehydrogenase Complete amino-acid sequence of the enzyme from Bacillus stearothermophilus. Eur. J. Biochem. 108: 549–565.

    Google Scholar 

  • YamadaK, AkiyoshiK, MurakamiH, SugaharaT, IkedaI, ToyodaK and OmuraH (1989) Partial purification and characterization of immunoglobulin production stimulating factor derived from Namalwa cells. In vitro Cell. Develop. Biol. 25: 243–247.

    Google Scholar 

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Authors and Affiliations

  1. Department of Food Science and Technology, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, 812, Fukuoka, Japan

    Takuya Sugahara

  2. Graduate School of Genetic Resources Technology, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, 812, Fukuoka, Japan

    Sanetaka Shirahata & Hiroki Murakami

  3. Department of Applied Biotechnology, Research Center, Taisho Pharmaceutical Co., Ltd, 403-1 Yoshino-cho, 330, Omiya, Japan

    Kazuhiko Akiyoshi

  4. Department of Chemistry, Faculty of Science, Tokyo Metropolitan University, 2-1-1 Fukasawa, Setagaya-ku, 158, Tokyo, Japan

    Toshiaki Isobe & Tsuneo Okuyama

Authors
  1. Takuya Sugahara
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  2. Sanetaka Shirahata
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  3. Kazuhiko Akiyoshi
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  4. Toshiaki Isobe
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  5. Tsuneo Okuyama
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  6. Hiroki Murakami
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Sugahara, T., Shirahata, S., Akiyoshi, K. et al. Immunoglobulin production stimulating factor-IIα (IPSF-IIα) is glyceraldehyde-3-phosphate dehydrogenase like protein. Cytotechnology 6, 115–120 (1991). https://doi.org/10.1007/BF00373028

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  • DOI: https://doi.org/10.1007/BF00373028

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