A brief historical perspective
Pierre Chambon, J.D. Weill and Paul Mandel discovered almost 40 years ago, in Strasbourg, the synthesis of a yet uncharacterized polyadenylic acid upon addition of nicotinamide mononucleotide (NMN) in rat liver nuclear extracts.They published in 1963 a paper entitled “Nicotinamide mononucleotide activation of a new DNA-dependent polyadenylic acid synthesizing enzyme” that launched the research on poly (ADP-ribose) metabolism (to download this paper as a pdf file, click here).
The structure of the new unknown compound synthesized by this enzyme in rat liver nuclei was later solved by three laboratories that published the structure of poly( ADP-ribose) at almost the same time (Chambon P. et al., (1966) BBRC 25, 638-643 ; Doly and Petek, 1966 CR Acad. Sc. 263, 1341-1344 ; Sugimura et al. 1967 ; Nishizuka et al., 1967).
Interest for poly (ADP-ribose) polymerase (PARP) activity in eukaryotes started with the characterization by Sidney Shall and coworkers of such a polymerizing activity in the slime mold Physarum polycephalum nuclei (Brightwell and Shall 1971).
The poly (ADP-ribose) glycohydrolase, the enzyme that cleaves the ribose-ribose bond was discovered in 1971 by Masanao Miwa and Takashi Sugimura, but it took a few more years to describe the branched structure of the poly (ADP-ribose) (Miwa and Sugimura, 1971 ; Miwa et al., 1979).
The first evidence for the involvement of poly (ADP-ribosyl)ation in DNA repair came in the early 80’s by the observation of the sensitization of cells to DNA damaging agents by 3-aminobenzamide, an efficient inhibitor of PARP (Durkacz et al., 1980 ; Purnell and Whish, 1980).
Conventional chromatographic methods led many investigators to purify the PARP to homogeneity, but a single-step affinity chromatography using 3-aminobenzamide as the ligand allowed later the rapid isolation of electrophoretically pure enzyme. Availability of purified PARP led to essential biochemical studies (Benjamin and Gill, 1980 ; Ushiro et al., 1987)
