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PREP  -  prolyl endopeptidase

Bos taurus

 
 
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Disease relevance of PREP

  • The complete primary structure of the H2B(2) variant has been deduced from sets of overlapping peptides generated by CNBr cleavage, Staphylococcus aureus V8 protease, endoproteinase Arg-C, the post-proline cleaving enzyme, chymotrypsin and cleavage in dilute acid [1].
  • Colonies of Anaplasma were apparent in low numbers at 9 days post exposure (PE) and infection in monolayers reached 100% by 4-5 weeks PE [2].
 

Psychiatry related information on PREP

  • In clinical studies, abnormal plasma PO activity has been associated with bipolar disorder (BD) and schizophrenia [3].
 

High impact information on PREP

 

Biological context of PREP

 

Anatomical context of PREP

  • Following vigorous salt washing and osmotic shock, the prolyl endopeptidase activity was released from the membranes by treatment with the detergent Triton X-100, and was partially purified by gel filtration on a Sephacryl S-200HR column [10].
  • Prolyl endopeptidase from bovine testis: purification, characterization and comparison with the enzymes from other tissues [13].
  • All virus-exposed animals developed fever and showed a significant (P < 0.05, 0.01 or 0.001) drop in the number of circulating leucocytes (neutrophils, lymphocytes and monocytes) by day 3 or 5 post-exposure (PE), which continued to the end of the experiment at day 12 PE [14].
  • BVDV was consistently isolated from the peripheral blood buffy coat cells from day 5 PE, and also from selected tissues (spleen, thymus, mesenteric and submaxillary lymph nodes, small intestine, lungs and thyroid gland) that were collected at the time of euthanasia of the animals at day 12 PE [14].
 

Associations of PREP with chemical compounds

 

Analytical, diagnostic and therapeutic context of PREP

  • The bovine brain prolyl endopeptidase-encoding cDNA was expressed using an expression vector bearing a tac promoter, with an approximate yield of 20 micrograms/ml of cell culture [8].
  • Prolyl oligopeptidase (EC 3.4.21.26) has been purified 26,000-fold from bovine lens tissue by anion-exchange chromatography, gel filtration and isoelectric focussing, with an overall yield of 11% [9].
  • Finally, a significant (P < 0.05 or 0.01) enhanced phagocytic capability of the PBMCs, as analyzed by flow cytometry, was observed in virus-exposed animals at days 3, 5, 7, 10 and 12 PE, when compared to control calves [14].
  • Lyophilization of Dounce and Mourtzikos beef liver catalase (Prep. Biochem. 11 (1981) 501-523) under specified conditions produced conformationally altered but not completely denatured catalase monomer which retained both significant catalatic activity and peroxidatic activity towards ethanol [17].

References

  1. The amino acid sequence of wheat histone H2B(2). A core histone with a novel repetitive N-terminal extension. Brandt, W.F., de Andrade Rodrigues, J., von Holt, C. Eur. J. Biochem. (1988) [Pubmed]
  2. Establishment and characterization of an Oklahoma isolate of Anaplasma marginale in cultured Ixodes scapularis cells. Blouin, E.F., Barbet, A.F., Yi, J., Kocan, K.M., Saliki, J.T. Vet. Parasitol. (2000) [Pubmed]
  3. Two peptidase activities decrease in treated bipolar disorder not schizophrenic patients. Breen, G., Harwood, A.J., Gregory, K., Sinclair, M., Collier, D., St Clair, D., Williams, R.S. Bipolar disorders. (2004) [Pubmed]
  4. Characterization of "thyroliberin-deamidating enzyme" as a post-proline-cleaving enzyme. Partial purification and enzyme-chemical analysis of the enzyme from anterior pituitary tissue. Knisatschek, H., Bauer, K. J. Biol. Chem. (1979) [Pubmed]
  5. Immunological, physical, and chemical evidence for the identity of brain and kidney post-proline cleaving-enzyme. Hersh, L.B. J. Neurochem. (1981) [Pubmed]
  6. A study of prolyl endopeptidase in bovine serum and its relevance to the tissue enzyme. Cunningham, D.F., O'Connor, B. Int. J. Biochem. Cell Biol. (1998) [Pubmed]
  7. Purification and characterization of a novel membrane-bound form of prolyl endopeptidase from bovine brain. O'Leary, R.M., Gallagher, S.P., O'Connor, B. Int. J. Biochem. Cell Biol. (1996) [Pubmed]
  8. Cloning and expression of the cDNA encoding prolyl oligopeptidase (prolyl endopeptidase) from bovine brain. Yoshimoto, T., Miyazaki, K., Haraguchi, N., Kitazono, A., Kabashima, T., Ito, K. Biol. Pharm. Bull. (1997) [Pubmed]
  9. Purification and characterization of prolyl oligopeptidase from bovine lens. Sharma, K.K., Ortwerth, B.J. Exp. Eye Res. (1994) [Pubmed]
  10. Identification and localisation of a synaptosomal membrane prolyl endopeptidase from bovine brain. O'Leary, R.M., O'Connor, B. Eur. J. Biochem. (1995) [Pubmed]
  11. Specific inhibition of post proline cleaving enzyme by benzyloxycarbonyl-Gly-Pro-diazomethyl ketone. Knisatschek, H., Bauer, K. Biochem. Biophys. Res. Commun. (1986) [Pubmed]
  12. Identification and initial characterisation of a N-benzyloxycarbonyl-prolyl-prolinal (Z-Pro-prolinal)-insensitive 7-(N-benzyloxycarbonyl-glycyl-prolyl-amido)-4-methylcoumarin (Z-Gly-Pro-NH-Mec)-hydrolysing peptidase in bovine serum. Cunningham, D.F., O'Connor, B. Eur. J. Biochem. (1997) [Pubmed]
  13. Prolyl endopeptidase from bovine testis: purification, characterization and comparison with the enzymes from other tissues. Yoshimoto, T., Oyama, H., Koriyama, N., Tsuru, D. Chem. Pharm. Bull. (1988) [Pubmed]
  14. Clinical response and immunomodulation following experimental challenge of calves with type 2 noncytopathogenic bovine viral diarrhea virus. Archambault, D., Béliveau, C., Couture, Y., Carman, S. Vet. Res. (2000) [Pubmed]
  15. Cleavage of substance P to an N-terminal tetrapeptide and a C-terminal heptapeptide by a post-proline Cleaving enzyme from bovine brain. Blumberg, S., Teichberg, V.I., Charli, J.L., Hersh, L.B., McKelvy, J.F. Brain Res. (1980) [Pubmed]
  16. Enzymes involved in the degradation of thyrotropin releasing hormone (TRH) and luteinizing hormone releasing hormone (LH-RH) in bovine brain. Hersh, L.B., McKelvy, J.F. Brain Res. (1979) [Pubmed]
  17. A study of the catalase monomer produced by lyophilization. Sichak, S.P., Dounce, A.L. Biochim. Biophys. Acta (1987) [Pubmed]
 
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