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Nrd1  -  nardilysin 1

Rattus norvegicus

Synonyms: N-arginine dibasic convertase, NRD convertase, NRD-C, Nardilysin, Nrdc
 
 
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High impact information on Nrd1

 

Biological context of Nrd1

 

Anatomical context of Nrd1

  • Human and rat testis express two mRNA species encoding variants of NRD convertase, a metalloendopeptidase of the insulinase family [4].
  • 2. Whereas NRD convertase is mostly expressed in testis and in 24 cell lines, low mRNA levels were detected in most of the 27 other tissues tested [4].
 

Associations of Nrd1 with chemical compounds

 

Other interactions of Nrd1

  • Specific inhibitors of other metallopeptidases such as enkephalinase [EC 3.4.24.11], the enkephalin generating neutral endopeptidase [EC 3.4.24.15], or NRD convertase do not inhibit the Dyn A processing enzyme activity [8].
  • The subcellular localization of both enzymes supports the involvement of aminopeptidase B in processing events associated with the secretory pathway but led to new hypothesis on the possible physiological role(s) of NRD convertase [5].
 

Analytical, diagnostic and therapeutic context of Nrd1

References

  1. Post-ischemic administration of heparin-binding epidermal growth factor-like growth factor (HB-EGF) reduces infarct size and modifies neurogenesis after focal cerebral ischemia in the rat. Jin, K., Sun, Y., Xie, L., Childs, J., Mao, X.O., Greenberg, D.A. J. Cereb. Blood Flow Metab. (2004) [Pubmed]
  2. N-arginine dibasic convertase (nardilysin) isoforms are soluble dibasic-specific metalloendopeptidases that localize in the cytoplasm and at the cell surface. Hospital, V., Chesneau, V., Balogh, A., Joulie, C., Seidah, N.G., Cohen, P., Prat, A. Biochem. J. (2000) [Pubmed]
  3. Regulation of N-arginine dibasic convertase activity by amines: putative role of a novel acidic domain as an amine binding site. Csuhai, E., Chen, G., Hersh, L.B. Biochemistry (1998) [Pubmed]
  4. Human and rat testis express two mRNA species encoding variants of NRD convertase, a metalloendopeptidase of the insulinase family. Hospital, V., Prat, A., Joulie, C., Chérif, D., Day, R., Cohen, P. Biochem. J. (1997) [Pubmed]
  5. NRD convertase and aminopeptidase B: two processing metallopeptidases with a selectivity for basic residues. Foulon, T., Cadel, S., Prat, A., Chesneau, V., Hospital, V., Segrétain, D., Cohen, P. Ann. Endocrinol. (Paris) (1997) [Pubmed]
  6. N-arginine dibasic convertase (NRD convertase): a newcomer to the family of processing endopeptidases. An overview. Chesneau, V., Pierotti, A.R., Prat, A., Gaudoux, F., Foulon, T., Cohen, P. Biochimie (1994) [Pubmed]
  7. Kinetic analysis of spermine binding to NRD convertase. Csuhai, E., Juliano, M.A., Juliano, L., Hersh, L.B. Arch. Biochem. Biophys. (1999) [Pubmed]
  8. Dynorphin A processing enzyme: tissue distribution, isolation, and characterization. Berman, Y., Ageyeva, L., Veksler, B., Wood, D., Devi, L.A. J. Biochem. (1999) [Pubmed]
  9. New fluorogenic substrates for N-arginine dibasic convertase. Csuhai, E., Juliano, M.A., Pyrek, J.S., Harms, A.C., Juliano, L., Hersh, L.B. Anal. Biochem. (1999) [Pubmed]
 
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