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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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Volume 396, Issue 6-7


The life and work of Dr. Robert Bittman (1942–2014)

Nigel J. Pyne
  • Strathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, 161 Cathedral Street, Glasgow G4 0RE, UK, e-mail:
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Richard N. Kolesnick
  • Laboratory of Signal Transduction, Sloan Kettering Institute, Memorial Sloan Kettering Cancer Center, 1275 York Ave, New York, NY 10021, USA, e-mail:
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2015-05-01 | DOI: https://doi.org/10.1515/hsz-2014-0275


  • Baek, D.J., MacRitchie, N., Anthony, N.G., MacKay, S.P., Pyne, S., Pyne, N.J., and Bittman, R. (2013). Structure-activity relationships and molecular modeling of sphingosine kinase inhibitors. J. Med. Chem. 56, 9310–9327.Google Scholar

  • Baker, D.L., Fujiwara, Y., Pigg, K.R., Tsukahara, R., Kobayashi, S., Murofushi, H., Uchiyama, A., Murakami-Murofushi, K., Koh, E., Bandle, R.W., et al. (2006). Carba analogs of cyclic phosphatidic acid are selective inhibitors of autotaxin and cancer cell invasion and metastasis. J. Biol. Chem. 281, 22786–22793.Google Scholar

  • Bandhuvula, P., Li, Z., Bittman, R., and Saba, J.D. (2009). Sphingosine 1-phosphate lyase enzyme assay using a BODIPY-labeled substrate. Biochem. Biophys. Res. Commun. 380, 366–370.Web of ScienceGoogle Scholar

  • Berdyshev, E.V., Gorshkova, I., Skobeleva, A., Bittman, R., Lu, X., Dudek, S.M., Mirzapoiazova, T., Garcia, J.G.N., and Natarajan, V. (2009). FTY720 inhibits ceramide synthases and upregulates dihydrosphingosine 1-phosphate formation in human lungt endothelial cells. J. Biol. Chem. 284, 5467–5477.Web of ScienceGoogle Scholar

  • Bittman, R. and Rottem, S. (1976). Distribution of cholesterol between the outer and inner halves of the lipid bilayer of Mycoplasma cell membranes. Biochem. Biophys. Res. Commun. 71, 318–324.Google Scholar

  • Bittman, R., Chen, W.C., and Blau, L. (1974). Stopped-flow kinetic and equilibrium studies of filipin III binding to sterols. Biochemistry 13, 1374–1379.Google Scholar

  • Bittman, R., Clejan, S., Lund-Katz, S., and Phillips, M.C. (1984). Influence of cholesterol on bilayers of ester- and ether-linked phospholipids. Permeability and 13C-Nuclear Magnetic Resonance measurements. Biochim. Biophys. Acta 772, 117–126.Google Scholar

  • Bittman, R., Witzke, N.M., Lee, T.-C., Blank, M.L., and Snyder, F. (1987). Synthesis and biochemical studies of analogs of platelet-activating factor bearing a methyl group at C2 of the glycerol backbone. J. Lipid Res. 28, 733–738.Google Scholar

  • Bittman, R., Swords, B., Liliom, K., and Tigyi, G. (1996). Inhibitors of lipid phosphatide receptors: N-palmitoylserine and N-palmitoyltyrosine phosphoric acids. J. Lipid Res. 37, 391–398.Google Scholar

  • Bode, C., Sensken, S.-C., Peest, U., Beutel, G., Thol, F., Levkau, B., Li, Z., Bittman, R., Huang, T., Tölle, M., et al. (2010). Erythrocytes serve as a reservoir for cellular and extracellular sphingosine 1-phosphate. J. Cell. Biochem. 109, 1232–1243.Web of ScienceGoogle Scholar

  • Byun, H.-S., Erukulla, R.K., and Bittman, R. (1994). Synthesis of sphingomyelin and ceramide 1-phosphate from ceramide without protection of the allylic hydroxyl group. J. Org. Chem. 59, 6495–6498.Google Scholar

  • Chun, J., Li, G., Byun, H.-S., and Bittman, R. (2001). New Trans Double Bond Sphingolipid Analogs: Δ6 Δ4,6 Ceramides. (Chicago: Division of Organic Chemistry, American Chemical Society).Google Scholar

  • Clejan, S. and Bittman, R. (1984). Decreases in rates of lipid exchange between Mycoplasma gallisepticum cells and unilamellar vesicles by incorporation of sphingomyelin. J. Biol. Chem. 259, 10823–10826.Google Scholar

  • Degagné, E., Panduranga, A., Bandhuvula, P., Kumar, A., Eltanawy, A., Zhang, M., Yoshinaga, Y., Nefedov, M., de Jong, P.J., Fong, L.G., et al. (2014). Sphingosine-1-phosphate lyase downregulation promotes colon carcinogenesis through STAT3-activated microRNAs. J. Clin. Invest. 124, 5368–5384.Web of ScienceGoogle Scholar

  • Evangelisti, C., Evangelisti, C., Teti, G., Chiarini, F., Falconi, M., Melchionda, F., Pession, A., Bertaina, A., Locatelli, F., McCubrey, J.A., et al. (2014). Assessment of the effect of sphingosine kinase inhibitors on apoptosis, unfolded protein response, and autophagy of T-Acute Lymphoblastic Leukemia cells; Indications for novel therapeutics. Oncotarget 5, 7886–7901.Google Scholar

  • Fyrst, H., Oskouian, B., Bandhuvula, P., Gong, Y., Byun, H.-S., Bittman, R., Lee, A.R., and Saba, J.D. (2009). Natural sphingadienes inhibit Akt-dependent signaling and prevent intestinal tumorigenesis, Cancer Res. 69, 9457–9464.Google Scholar

  • Gomez-Muñoz, A., Duffy, P.A., Martin, A., O’Brien, L., Byun, H.-S., Bittman, R., and Brindley, D.N. (1995). Ceramide-1-phosphate is a novel stimulator of DNA synthesis: antagonism by cell-permeable ceramides. Mol. Pharmacol. 47, 883–889.Google Scholar

  • He, L., Byun, H.-S., and Bittman, R. (2000). A stereocontrolled, efficient synthetic route to bioactive sphingolipids: synthesis of phytosphingosine and phytoceramides from unsaturated ester precursors via cyclic sulfate intermediates. J. Org. Chem. 65, 7618–7626.Google Scholar

  • Hölttä-Vuori, M., Uronen, R.L., Repakova, J., Salonen, E., Vattulainen, I., Panula, P., Li, Z., Bittman, R., and Ikonen, E. (2008). BODIPY-cholesterol: a new tool to visualize sterol trafficking in living cells and organisms. Traffic 9, 1839–1849.Web of ScienceGoogle Scholar

  • Joseph, C.K., Byun, H.-S., Bittman, R., and Kolesnick, R.N. (1993). Substrate recognition by ceramide-activated protein kinase: evidence that kinase activity is proline-directed. J. Biol. Chem. 268, 20002–20006.Google Scholar

  • Kirschner, K., Eigen, M., Bittman, R., and Voigt, B. (1966). The binding of nicotinamide adenine dinucleotide to yeast D-glyceraldehyde-3-phosphate dehydrogenase: temperature-jump relaxation studies on the mechanism of an allosteric enzyme. Proc. Natl. Acad. Sci. USA 56, 1661–1667.Google Scholar

  • Kumar, A., Pandurangan, A.K., Lu, F., Fyrst, H., Zhang, M., Byun, H- S., Bittman, R., and Saba, J.D. (2012). Chemopreventive sphingadienes downregulate Wnt signaling via a PP2A/Akt/GSK3ß pathway in colon cancer. Carcinogenesis 33, 1726–1735.Web of ScienceGoogle Scholar

  • Lankalapalli, R.S., Ouro, A., Arana, L., Gómez Muñoz, A., and Bittman, R. (2009). Caged ceramide 1-phosphate analogues: synthesis and properties. J. Org. Chem. 74, 8844–8847.Google Scholar

  • Lim, K.G., Sun, C., Bittman, R., Pyne, N.J., and Pyne, S. (2011). (R)-FTY720 methyl ether is a specific sphingosine kinase 2 inhibitor: effect on sphingosine kinase 2 expression in HEK293 cells and actin rearrangement and survival of MCF-7 breast cancer cells. Cell. Signal. 23, 1590–1595.Web of ScienceGoogle Scholar

  • Lu, X., Song, L., Metelitsa, L.S., and Bittman, R. (2006). Synthesis and evaluation of a α-C-galactosylceramide analogue that induces Th1-biased responses in human natural killer T cells. ChemBioChem 7, 1750–1756.Google Scholar

  • Liu, Y. and Bittman, R. (2006). Synthesis of fluorescent lactosylceramide stereoisomers. Chem. Phys. Lipids 142, 58–69.Google Scholar

  • Mattjus, P., Malewicz, B., Valiyaveettil, J.T., Baumann, W.J., Bittman, R., and Brown, R.E. (2002). Sphingomyelin modulates the transbilayer distribution of galactosylceramide in phospholipid membranes. J. Biol. Chem. 277, 19476–19481.Google Scholar

  • Megha, Sawatzki, P., Kolter, T., Bittman, R., and London, E. (2007). Effect of ceramide N-acyl chain and polar headgroup structure on the properties of ordered lipid domains (lipid rafts). Biochim. Biophys. Acta 1768, 2205–2212.Web of ScienceGoogle Scholar

  • Patel, O., Cameron, G., Pellicci, D.G., Liu, Z., Byun, H.-S., Beddoe, T., McCluskey, J., Franck, R.W., Castaño, A.R., Harrak, Y., et al.(2011). Natural killer T-cell receptor recognition of CD1d-C-galactosylceramide. J. Immunol. 187, 4705–4713.Google Scholar

  • Pietiäinen, V., Vassilev, B., Blom, T., Wang, W., Nelson, J., Bittman, R., Bäck, N., Zelcer, N., and Ikonen, E. (2013). NDRG1 functions in LDL receptor trafficking by regulating endosomal recycling and degradation. J. Cell. Sci. 126, 3961–3971.Web of ScienceGoogle Scholar

  • Salari, H., Dryden, P., Howard, S., and Bittman, R. (1992). Two different sites of action for platelet activating factor and 1-O-Alkyl-2-O-methyl-sn-glycero-3-phosphocholine on platelets and leukemia cells. Biochem. Cell Biol. 70, 129–135.Google Scholar

  • Younes, A., Kahn, D.W., Besterman, J.M., Bittman, R., Byun, H.-S., and Kolesnick, R.N. (1992). Ceramide is a competitive inhibitor of diacylglycerol kinase in vitro and in intact human leukemia (HL-60) cells. J. Biol. Chem. 267, 842–847.Google Scholar

  • Zhang, C., Baker, D.L., Yasuda, S., Makarova, N., Johnson, L., Balazs, L., Marathe, G., McIntyre, T.M., Xu, Y., Prestwich, G.D., et al. (2004). Lysophosphatidic acid induces neointima formation through PPARγ activation. J. Exp. Med. 199, 763–774.Google Scholar

  • Zhao, Y., Usatyuk, P.V., Gorkoshova, I., He, D., Watkins, T., Saatian, B., Sun, C, Brindley, D.N., Bittman, R., Garcia, J.G.N., et al. (2007). Intracellular generation of sphingosine 1-phosphate in human lung endothelial cells: role of lipid phosphate phosphatase-1 and sphingosine kinase 1. J. Biol. Chem. 282, 14165–14177.Web of ScienceGoogle Scholar

  • Zhou, X., Li, X., Xiong, W., Lichtfield, D., Bittman, R., and Arthur, G. (1996). 1-O-Octadecyl-2-O-methylglycerophosphocholine inhibits the transduction of growth signals via the MAP kinase cascade in MCF-7 cells by interfering with the membrane association of Raf-1. J. Clin. Invest. 98, 937–944.Google Scholar

About the article

Published Online: 2015-05-01

Published in Print: 2015-06-01

Citation Information: Biological Chemistry, Volume 396, Issue 6-7, Pages 827–830, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2014-0275.

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