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Gene Review

DPEP1  -  dipeptidase 1 (renal)

Sus scrofa

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Disease relevance of DPEP1


High impact information on DPEP1


Biological context of DPEP1


Anatomical context of DPEP1


Associations of DPEP1 with chemical compounds

  • Purified peptidyl dipeptidase (angiotensin I converting enzyme or kininase II) from human lung or hog kidney is inhibited by commercially prepared plasma protein preparations, by human serum albumin and by the additive albumin stabilizer, acetyltryptophan [13].
  • Captopril and amastatin (inhibitors of peptidyl dipeptidase A and aminopeptidases respectively) had no significant effect [16].
  • The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-beta-lactamase enzyme CphA [17].
  • Membrane dipeptidase (EC is a plasma membrane zinc peptidase that is involved in the renal metabolism of glutathione and its conjugates, such as leukotriene D4 [1].
  • However, despite these differences, we show that the unusually marked effect of LacCer to promote the detergent-insolubility of dipeptidase cannot be singularly attributed to the fatty acyl composition of this glycosphingolipid molecule [18].

Other interactions of DPEP1


Analytical, diagnostic and therapeutic context of DPEP1


  1. Identification by site-directed mutagenesis of three essential histidine residues in membrane dipeptidase, a novel mammalian zinc peptidase. Keynan, S., Hooper, N.M., Turner, A.J. Biochem. J. (1997) [Pubmed]
  2. Nitric oxide inhibits the shedding of the glycosylphosphatidylinositol-anchored dipeptidase from porcine renal proximal tubules. Park, S.W., Yoon, H.J., Lee, H.B., Hooper, N.M., Park, H.S. Biochem. J. (2002) [Pubmed]
  3. Behaviour of urinary dipeptidase in patients with chronic renal failure. Fukumura, Y., Kera, Y., Oshitani, S., Ushijima, Y., Kobayashi, I., Liu, Z., Watanabe, T., Yamada, R., Kikuchi, H., Kawazu, S., Yabuuchi, M. Ann. Clin. Biochem. (1999) [Pubmed]
  4. Differential toxicity as a result of apical and basolateral treatment of LLC-PK1 monolayers with S-(1,2,3,4,4-pentachlorobutadienyl)glutathione and N-acetyl-S-(1,2,3,4,4-pentachlorobutadienyl)-L-cysteine. Mertens, J.J., Weijnen, J.G., van Doorn, W.J., Spenkelink, B., Temmink, J.H., van Bladeren, P.J. Chem. Biol. Interact. (1988) [Pubmed]
  5. Histological localization of two dipeptidases in the pig small intestine and liver, using immunofluorescence. Norén, O., Dabelsteen, E., Sjöström, H., Josefsson, L. Gastroenterology (1977) [Pubmed]
  6. Folylpoly-gamma-glutamate carboxypeptidase from pig jejunum. Molecular characterization and relation to glutamate carboxypeptidase II. Halsted, C.H., Ling, E.H., Luthi-Carter, R., Villanueva, J.A., Gardner, J.M., Coyle, J.T. J. Biol. Chem. (1998) [Pubmed]
  7. Rat brain N-acetylated alpha-linked acidic dipeptidase activity. Purification and immunologic characterization. Slusher, B.S., Robinson, M.B., Tsai, G., Simmons, M.L., Richards, S.S., Coyle, J.T. J. Biol. Chem. (1990) [Pubmed]
  8. Membrane dipeptidase and glutathione are major components of pig pancreatic zymogen granules. Höfken, T., Linder, D., Kleene, R., Göke, B., Wagner, A.C. Exp. Cell Res. (1998) [Pubmed]
  9. cDNA cloning and expression in Xenopus laevis oocytes of pig renal dipeptidase, a glycosyl-phosphatidylinositol-anchored ectoenzyme. Rached, E., Hooper, N.M., James, P., Semenza, G., Turner, A.J., Mantei, N. Biochem. J. (1990) [Pubmed]
  10. Ectoenzymes of the kidney microvillar membrane. Isolation and characterization of the amphipathic form of renal dipeptidase and hydrolysis of its glycosyl-phosphatidylinositol anchor by an activity in plasma. Hooper, N.M., Turner, A.J. Biochem. J. (1989) [Pubmed]
  11. Activation of the glycosyl-phosphatidylinositol-anchored membrane dipeptidase upon release from pig kidney membranes by phospholipase C. Brewis, I.A., Turner, A.J., Hooper, N.M. Biochem. J. (1994) [Pubmed]
  12. Site-directed mutagenesis of conserved cysteine residues in porcine membrane dipeptidase. Cys 361 alone is involved in disulfide-linked dimerization. Keynan, S., Habgood, N.T., Hooper, N.M., Turner, A.J. Biochemistry (1996) [Pubmed]
  13. Inhibition of human peptidyl dipeptidase (angiotensin I converting enzyme: kininase II) by human serum albumin and its fragments. Klauser, R.J., Robinson, C.J., Marinkovic, D.V., Erdös, E.G. Hypertension (1979) [Pubmed]
  14. Cloning of cDNAs encoding a rabbit renal brush border membrane protein immunologically related to band 3. Sequence similarity with microsomal dipeptidase. Igarashi, P., Karniski, L.P. Biochem. J. (1991) [Pubmed]
  15. Purification and characterization of a peptidyl dipeptidase resembling angiotensin converting enzyme from the electric organ of Torpedo marmorata. Turner, A.J., Hryszko, J., Hooper, N.M., Dowdall, M.J. J. Neurochem. (1987) [Pubmed]
  16. The hydrolysis of alpha-human atrial natriuretic peptide by pig kidney microvillar membranes is initiated by endopeptidase-24.11. Stephenson, S.L., Kenny, A.J. Biochem. J. (1987) [Pubmed]
  17. The renal membrane dipeptidase (dehydropeptidase I) inhibitor, cilastatin, inhibits the bacterial metallo-beta-lactamase enzyme CphA. Keynan, S., Hooper, N.M., Felici, A., Amicosante, G., Turner, A.J. Antimicrob. Agents Chemother. (1995) [Pubmed]
  18. Differential effects of glycosphingolipids on the detergent-insolubility of the glycosylphosphatidylinositol-anchored membrane dipeptidase. Parkin, E.T., Turner, A.J., Hooper, N.M. Biochem. J. (2001) [Pubmed]
  19. Membrane peptidases in the pig choroid plexus and on other cell surfaces in contact with the cerebrospinal fluid. Bourne, A., Barnes, K., Taylor, B.A., Turner, A.J., Kenny, A.J. Biochem. J. (1989) [Pubmed]
  20. Characterization of antibodies to the glycosyl-phosphatidylinositol membrane anchors of mammalian proteins. Hooper, N.M., Broomfield, S.J., Turner, A.J. Biochem. J. (1991) [Pubmed]
  21. Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P and oxytocin by pig kidney microvillar membranes. Stephenson, S.L., Kenny, A.J. Biochem. J. (1987) [Pubmed]
  22. The hydrolysis of brain and atrial natriuretic peptides by porcine choroid plexus is attributable to endopeptidase-24.11. Bourne, A., Kenny, A.J. Biochem. J. (1990) [Pubmed]
  23. Membrane localization of endopeptidase-24.11 and peptidyl dipeptidase A (angiotensin converting enzyme) in the pig brain: a study using subcellular fractionation and electron microscopic immunocytochemistry. Barnes, K., Turner, A.J., Kenny, A.J. J. Neurochem. (1992) [Pubmed]
  24. Preparative purification of dipeptidyl peptidase IV. Seidl, R., Schaefer, W. Prep. Biochem. (1991) [Pubmed]
  25. Further characterization of porcine kidney aminoacylase I reveals close similarity to 'renal dipeptidase'. Heese, D., Löffler, H.G., Röhm, K.H. Biol. Chem. Hoppe-Seyler (1988) [Pubmed]
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