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Gene Review

Adprh  -  ADP-ribosylarginine hydrolase

Mus musculus

Synonyms: ADP-ribose-L-arginine cleaving enzyme, Arh1
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High impact information on Adprh

  • ADP-ribosylarginine hydrolase, which preferentially hydrolyzes the alpha-anomer of ADP-ribosylarginine, released [U-14C]arginine from ADP-ribosyl[U-14C]arginine synthesized by mRT6.1, consistent with the conclusion that mRt6.1 catalyzes a stereospecific Sn2-like reaction [1].
  • Since ADP-ribosylarginine hydrolase, the enzyme responsible for cleavage of the ADP-ribosylarginine bond and a component with the transferase of a putative ADP-ribosylation cycle, is cytosolic, the processing of ADP-ribosylated integrin alpha 7 was investigated [2].
  • The ADPRH gene, represented in two overlapping genomic clones, spans approximately 9 kilobases with four exons and three introns [3].
  • Northern analysis using different regions of the ADPRH cDNA as probes identified two mRNAs of 1.7 and 3.0 kb, which resulted from the use of alternative polyadenylation signals, CATAAC and ATTAAA, beginning at positions 1501 and 2885, respectively, of the nucleotide sequence (A of ATG = 1) [3].
  • The ADPRH cDNA had been cloned from human, rat, and mouse tissues and high levels of mRNA were found in brain, spleen, and testis [3].

Biological context of Adprh

  • To begin to understand the molecular mechanisms that regulate ADPRH gene expression, we cloned the full-length cDNA, determined the genomic structure of mouse ADPRH, and investigated promoter function [3].

Anatomical context of Adprh

  • On Western blot analysis of rat cerebrospinal fluid (CSF), the anti-AAH antibodies recognized a protein with a molecular mass of 38 kDa [4].
  • An ADP-ribosylarginine hydrolase, purified extensively from turkey erythrocytes, was a 39-kDa monomeric protein under denaturing and non-denaturing conditions, and was activated by Mg2+ and dithiothreitol [5].

Associations of Adprh with chemical compounds

  • Casein ADP-ribosylated with [32P]NAD and chicken heterophil arginine-specific ADP-ribosyltransferase served as a substrate for the recombinant ADP-ribosylarginine hydrolase and the released ADP-ribose was determined [6].
  • The reverse reaction, catalyzed by ADP-ribosylarginine hydrolase, removes ADP-ribose, regenerating free arginine [5].

Analytical, diagnostic and therapeutic context of Adprh

  • Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase [7].
  • Western blotting showed that the antibodies recognized in mouse brain homogenate a single protein with a molecular mass of 38 kDa, the expected size for mouse AAH [4].


  1. Characterization of mouse Rt6.1 NAD:arginine ADP-ribosyltransferase. Moss, J., Stevens, L.A., Cavanaugh, E., Okazaki, I.J., Bortell, R., Kanaitsuka, T., Mordes, J.P., Greiner, D.L., Rossini, A.A. J. Biol. Chem. (1997) [Pubmed]
  2. Processing of ADP-ribosylated integrin alpha 7 in skeletal muscle myotubes. Zolkiewska, A., Moss, J. J. Biol. Chem. (1995) [Pubmed]
  3. Genomic organization and promoter analysis of the mouse ADP-ribosylarginine hydrolase gene. Aoki, K., Kato, J., Shoemaker, M.T., Moss, J. Gene (2005) [Pubmed]
  4. Immunohistochemical localization of ADP-ribosylarginine hydrolase in rodent CNS. Miyaoka, T., Tsuchiya, M., Yamada, K., Badruzzaman, M., Yamamori, C., Ishino, H., Shimoyama, M. Brain Res. (1997) [Pubmed]
  5. ADP-ribosylarginine hydrolases. Takada, T., Okazaki, I.J., Moss, J. Mol. Cell. Biochem. (1994) [Pubmed]
  6. Detection of arginine-ADP-ribosylated protein using recombinant ADP-ribosylarginine hydrolase. Ohno, T., Tsuchiya, M., Osago, H., Hara, N., Jidoi, J., Shimoyama, M. Anal. Biochem. (1995) [Pubmed]
  7. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. Takada, T., Iida, K., Moss, J. J. Biol. Chem. (1993) [Pubmed]
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