Abstract
HL-60 cells transferred from serum-supplemented to serum-free culture medium initially bound to culture plate tightly and then released from the plate on increasing the culture time and resumed exponential growth after about 8 h lag. At the initial stage of the culture, the cells became extremely sensitive to 3-aminobenzamide, a potent inhibitor of poly (ADP-ribose) polymerase, and, at 1 mM, 80 to 90% of the cells were lysed within 20 h, whereas the inhibitor was totally ineffective on the cell growth in serum-supplemented medium at the concentration. Non-inhibitory analogs of the inhibitor were ineffective. Assay of poly(ADP-ribose) polymerase activity in permeable cells indicated that a transient activation of the enzyme occurred during the culture in serum-free medium (the maximum activation was observed at 8 h of the culture). The cells conditioned in serum-free medium for 24 h acquired significant resistancy to the inhibitor. A low concentration of fibronectin (5 to 10μ/ml) and a relatively high concentration of bovine serum albumin (0.5 to 1 mg/ml) effectively blocked the cell attachment to plate and also the 3-aminobenzamide-induced cell lysis. These results suggest that poly(ADP-ribose) polymerase is involved in a process essential for HL-60 cells to adapt to a serumdeprived growth condition.
Similar content being viewed by others
References
Nishizuka Y,Ueda K, Yoshihara K, Yamamura H, Takeda M, Hayaishi O: Enzymic adenosine diphosphoribosylation of nuclear proteins. Cold Spr Harb Symp Quant Biol 34: 781–786, 1969
Adamietz P: Acceptor proteins of poly(ADP-ribose). In: O Hayaishi, K Ueda (eds) ADP-Ribosylation Reactions. Academic Press, New York, 1982, pp 77–101
Yoshihara K, Tanigawa Y, Burzio L,Koide SS: Evidence for adenosine diphosphoribosylation of Ca2+,Mg2+-dependent endonuclease. Proc Natl Acad Sci USA 72: 289–293, 1975
Ferro AM, Olivera BM: Poly (ADP-ribosylation) of DNA topoisomerase I from calf thymus. J Biol Chem 259: 547–554, 1984
Yoshihara K, Itaya A, Tanaka Y, Ohashi Y, Ito K, Teraoka H, Tsukada K, Matsukage A, Kamiya T: Poly-(ADP-ribosyl)ation of nuclear enzymes. In: FR Althaus, H Hilz, S Shall (eds) ADP-ribosylation of Proteins. Springer-Verlag, Berlin, 1985, pp 82–92
Yoshihara K, Hashida T, Tanaka Y, Matsunami N, Yamaguchi A, Kamiya T: Mode of enzyme-bound poly(ADP-ribose) synthesis and histone-modification by reconstituted poly(ADP-ribose) polymerase DNA-cellulose complex. J Biol Chem 256: 3471–3478, 1981
Miwa M, Sugimura T: Structure and properties of poly(ADP-ribose). In: O Hayaishi, K Ueda (eds) ADP-Ribosylation Reactions. Academic Press, New York, 1982, pp 43–63
Benjamin RC, Gill DM: Poly(ADP-ribose) synthesisin vitro programmed by damaged DNA. J Biol Chem 255: 10,493–10,501, 1980
Ohgushi H, Yoshihara K, Kamiya T: Bovine thymus poly-(ADP-ribose) polymerase; physical properties and binding to DNA. J Biol Chem 255: 6205–6211, 1980
Durkacz BW, Omidiji O, Gray DA, Shall S: (ADP-ribose)n participates in DNA excision repair. Nature 283: 593–596, 1980
Shall S: ADP-ribose in DNA repair. In: O Hayaishi, K Ueda (eds) ADP-Ribosylation Reactions. Academic Press, New York, 1982, pp 477–520
Oikawa A, Tohda H, Kanai M, Miwa M, Sugimura T: Inhibitors of poly(adenosine diphosphate ribose) polymerase induce sister chromatid exchange. Biochem Biophys Res Commun 97: 1311–1316, 1980
Chatterjee S, Hirschler NV, Petzold SJ, Berger SJ, Berger NA: Mutant cells defective in poly(ADP-ribose) synthesis due to stable alterations in enzyme activity or substrate availability. Exp Cell Res 184: 1–15, 1989
Nakayasu M, Shima H, Aonuma S, Nakagama H, Nagao M, Sugimura T: Deletion of transferted oncogenes from NIH 3T3 transformants by inhibitors of poly(ADP-ribose) polymerase. Proc Natl Acad Sci USA 85: 9066–9070, 1988
Farzaneh F, Panayotou GN, Dowler LD, Hardas BD, Broom T, Walther C, Shall S: ADP-ribosylation is involved in the integration of foreign DNA into the mammalian cell genome. Nucleic Acids Res 16: 11,319–11,326, 1988
Gaal JC, Pearson CK: Eukaryotic nuclear ADP-ribosylations. Biochem J 230: 1–18, 1985
Taniguchi T, Tomoda T, Nomura I, Kurashige T, Yamamoto H, Fujimoto S: Inhibition of interferon γ-dependent induction of major histocompatibility complex class II antigen by expressing exogenous poly(ADP-ribose) synthetase gene. In: GG Poirier, P Moreau (eds) ADP-Ribosilation Reactions. Springer-Verlag, New York, 1992, pp 141–144
Carson DA, Seto S, Wasson DB, Carrena CJ: DNA strand breaks, NAD metabolism, and prgrammed cell death. Exp Cell Res 164: 273–281, 1986
Yoshihara K, Itaya A, Hironaka T, Sakuramoto S, Tanaka Y, Tsuyuki M, Inada Y, Kamiya T, Ohnishi K, Honma M, Kataoka E, Mizusawa H, Uchida M, Uchida K, Miwa M: Poly(ADP-ribose) polymerase-defective mutant cell clone of mouse L-1210 cells. Exp Cell Res 200: 126–134, 1992
Breitman TR, Collins SJ, Keene BR: Replacement of serum by insulin and transferrin supports growth and differentiation of the human promyelocytic leukemia cell line, HL-60. Exp Cell Res 126: 494–498, 1980
Brunk CF, Jones KC, James TW: Assay for nanogram quantities of DNA in cellular homogenates. Anal Biochem 92: 497–500, 1979
Berger NA, Petzold SJ, Berger SJ: Association of poly(ADP-rib) synthesis with cessation of DNA synthesis and DNA fragmentation. Biochim Biophys Acta 564: 90–104, 1979
Waring P, Kos FJ, Mullbacher A: Apotosis or programmed cell death. Medical Research Reviews 11: 219–236, 1991
Rankin PW, Jacobson EL, Benjamin RC, Moss J, Jacobson MK: Quantitative studies of inhibitors of ADP-ribosylationin vitro andin vivo. J Biol Chem 264: 4312–4317, 1989
Brown MS, Faust JR, Coldstein JL: Induction of 3-hydroxy-3-methylglutaryl coenzyme A reductase activity in human fibroblasts incubated with compactin (ML-236 B), a competitive inhibitor of the reductase. J Biol Chem 253: 1121–1128, 1978
Volpe JJ, Hennessy SW: Cholesterol biosynthesis and 3-hydroxy-3-methylglutaryl coenzyme A reductase in cultured glial and neuronal cells; regulation by lipo-protein and by certain free sterols. Biochim Biophys Acta 486: 408–420, 1977
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Yoshihara, K., Tsuyuki, M., Itaya, A. et al. 3-Aminobenzamide, a potent inhibitor of poly (ADP-ribose) polymerase, causes a rapid death of HL-60 cells cultured in serum-free medium. Mol Cell Biochem 135, 143–151 (1994). https://doi.org/10.1007/BF00926517
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00926517