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Gene Review

RNPEP  -  arginyl aminopeptidase (aminopeptidase B)

Homo sapiens

Synonyms: AP-B, APB, Aminopeptidase B, Arginine aminopeptidase, Arginyl aminopeptidase
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Disease relevance of RNPEP


High impact information on RNPEP

  • Less is known about the regulation of responses mediated by AMPA, kainate, ACPD or APB receptors [5].
  • Functionally, this APB receptor-mediated action found in horizontal cells would provide a means by which spatially restricted changes of glutamate, produced by local illumination of photoreceptors, could regulate IRK+ and consequently the response properties of these neurons [6].
  • We find that glutamate and APB (2-amino-4-phosphonobutyrate) produce a delayed and moderately prolonged suppression of an inward rectifier current (IRK+) [6].
  • We hypothesize that the APB receptor suppresses IRK+ via upregulation of cGMP and subsequent activation of a cGMP-dependent protein kinase [6].
  • The effects of glutamate and APB are blocked by protein kinase inhibitors including Rp-8-pCPT-cGMPS, H-8, and H-7 as well as by ATPgammaS [6].

Chemical compound and disease context of RNPEP


Biological context of RNPEP


Anatomical context of RNPEP

  • It is concluded that aminopeptidase B may participate in processing events occurring either during its intracellular transport along the secretory pathway or at the plasma membrane level, or both [1].
  • Finally, we found that AP-B was up-regulated during activation of normal and leukemic T lymphocytes [15].
  • We studied I wave interaction, ICI and ICF in an intrinsic hand muscle (abductor pollicis brevis, APB), in a proximal arm muscle (biceps brachii, BB) and in a lower limb muscle (tibialis anterior, TA) in 11 normal subjects [16].
  • A ubenimex-sensitive aminopeptidase B-like enzyme was purified from the non-membrane-bound fraction of K562 cells by a series of chromatographic procedures and slab-gel electrophoresis [17].
  • The motor and sensory conduction studies showed only a reduced mean amplitude of the ulnar nerve SAP and of the compound muscle action potential of the APB and EDB muscles [18].

Associations of RNPEP with chemical compounds

  • The identification of the hydrolyzing activity as AP-B was confirmed by its sensitivity to both arphamenine B and bestatin in the nanomolar range [15].
  • Purified AP-B cleaved N-terminal basic amino acid-containing peptides such as thymopentin (H-Arg-Lys-Asp-Val-Tyr-OH), indicating that it might play a role in the regulation of the concentration of important soluble mediators of T cell activation [15].
  • Whereas ProTx-II can be quantitatively depleted from solution upon incubation with phosphatidylcholine/phosphatidylserine liposomes, ApB displays no discernible phospholipid binding activity [19].
  • Synthesis and structure-activity relationships of bestatin analogues, inhibitors of aminopeptidase B [20].
  • The 2-thiolbestatin analogue (6) was found to be a potent inhibitor of all three aminopeptidases (AP-M, Ki = 4.4 microM; LAP, Ki = 0.55 microM; AP-B, Ki = 4.6 nM) but only a slightly better inhibitor of these aminopeptidases than the parent hydroxy-containing compound 1 [21].

Other interactions of RNPEP


Analytical, diagnostic and therapeutic context of RNPEP

  • A rabbit polyclonal antibody was shown to recognize AP-B as assessed by both immunoprecipitation and Western blot experiments [15].
  • Low amplitude muscle vibration (0.5 ms; 80 Hz; duration 1.5 s) was applied in turn to each of three different intrinsic hand muscles (first dorsal interosseus, FDI; abductor pollicis brevis, APB; and abductor digiti minimi, ADM) in order to test its effect on the EMG responses evoked by transcranial magnetic stimulation (TMS) [26].
  • A precise, rapid, automated, rate nephelometric immunoassay for apolipoprotein AI (APA) and apolipoprotein B (APB) is described [27].
  • A complex containing APB could be isolated from a "trimeric" allophycocyanin fraction of the density gradient by agarose gel electrophoresis in the presence of ampholytes [28].
  • The polypeptide composition analyzed by SDS-PAGE showed the "anchor" polypeptide LCM, alpha AP, alpha APB, beta AP subunits, a low molecular weight linker with M(r) 13,500 and a blue-colored polypeptide of M(r) 19,800 [28].


  1. Aminopeptidase B: a processing enzyme secreted and associated with the plasma membrane of rat pheochromocytoma (PC12) cells. Balogh, A., Cadel, S., Foulon, T., Picart, R., Der Garabedian, A., Rousselet, A., Tougard, C., Cohen, P. J. Cell. Sci. (1998) [Pubmed]
  2. A robust assay for alternative lengthening of telomeres in tumors shows the significance of alternative lengthening of telomeres in sarcomas and astrocytomas. Henson, J.D., Hannay, J.A., McCarthy, S.W., Royds, J.A., Yeager, T.R., Robinson, R.A., Wharton, S.B., Jellinek, D.A., Arbuckle, S.M., Yoo, J., Robinson, B.G., Learoyd, D.L., Stalley, P.D., Bonar, S.F., Yu, D., Pollock, R.E., Reddel, R.R. Clin. Cancer Res. (2005) [Pubmed]
  3. Long-term survival of patients with intermediate and high grade lymphoma treated with COMLA/ABP. Olopade, O.I., Larson, R.A., Mick, R., Watson, S.M., Hoffman, P.C., Ultmann, J.E., Golomb, H.M. Leukemia (1990) [Pubmed]
  4. Effect of ubenimex on the proliferation and differentiation of U937 human histiocytic lymphoma cells. Murata, M., Kubota, Y., Tanaka, T., Iida-Tanaka, K., Takahara, J., Irino, S. Leukemia (1994) [Pubmed]
  5. Properties of vertebrate glutamate receptors: calcium mobilization and desensitization. Zorumski, C.F., Thio, L.L. Prog. Neurobiol. (1992) [Pubmed]
  6. Metabotropic glutamate receptor-mediated suppression of an inward rectifier current is linked via a cGMP cascade. Dixon, D.B., Copenhagen, D.R. J. Neurosci. (1997) [Pubmed]
  7. APB (2-amino-4-phosphonobutyric acid) activates a chloride conductance in ganglion cells isolated from newt retina. Chiba, C., Saito, T. Neuroreport (1994) [Pubmed]
  8. Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes. Umezawa, H., Aoyagi, T., Suda, H., Hamada, M., Takeuchi, T. J. Antibiot. (1976) [Pubmed]
  9. Expression and retinoid modulation of N-arginine dibasic convertase and an aminopeptidase-B in human neuroblastoma cell lines. Draoui, M., Bellincampi, L., Hospital, V., Cadel, S., Foulon, T., Prat, A., Barré, N., Reichert, U., Melino, G., Cohen, P. J. Neurooncol. (1997) [Pubmed]
  10. Assignment of the aminopeptidase B gene (RNPEP) to human chromosome 1 band q32 by in situ hybridization. Aurich-Costa, J., Cadel, S., Gouzy, C., Foulon, T., Chérif, D., Cohen, P. Cytogenet. Cell Genet. (1997) [Pubmed]
  11. Human aminopeptidase B (rnpep) on chromosome 1q32.2: complementary DNA, genomic structure and expression. Piesse, C., Tymms, M., Garrafa, E., Gouzy, C., Lacasa, M., Cadel, S., Cohen, P., Foulon, T. Gene (2002) [Pubmed]
  12. Cloning and characterization of a bifunctional leukotriene A(4) hydrolase from Saccharomyces cerevisiae. Kull, F., Ohlson, E., Haeggström, J.Z. J. Biol. Chem. (1999) [Pubmed]
  13. Two nuclear factor binding domains activate expression from the human amyloid beta-protein precursor promoter. Quitschke, W.W. J. Biol. Chem. (1994) [Pubmed]
  14. Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases. Tanioka, T., Hattori, A., Masuda, S., Nomura, Y., Nakayama, H., Mizutani, S., Tsujimoto, M. J. Biol. Chem. (2003) [Pubmed]
  15. Characterization and purification of T lymphocyte aminopeptidase B: a putative marker of T cell activation. Belhacene, N., Mari, B., Rossi, B., Auberger, P. Eur. J. Immunol. (1993) [Pubmed]
  16. Facilitatory I wave interaction in proximal arm and lower limb muscle representations of the human motor cortex. Chen, R., Garg, R. J. Neurophysiol. (2000) [Pubmed]
  17. Purification and characterization of a ubenimex (Bestatin)-sensitive aminopeptidase B-like enzyme from K562 human chronic myeloid leukemia cells. Yamada, M., Sukenaga, Y., Fujii, H., Abe, F., Takeuchi, T. FEBS Lett. (1994) [Pubmed]
  18. Evidence of motor neuron involvement in chronic respiratory insufficiency. Valli, G., Barbieri, S., Sergi, P., Fayoumi, Z., Berardinelli, P. J. Neurol. Neurosurg. Psychiatr. (1984) [Pubmed]
  19. Differential phospholipid binding by site 3 and site 4 toxins. Implications for structural variability between voltage-sensitive sodium channel domains. Smith, J.J., Alphy, S., Seibert, A.L., Blumenthal, K.M. J. Biol. Chem. (2005) [Pubmed]
  20. Synthesis and structure-activity relationships of bestatin analogues, inhibitors of aminopeptidase B. Nishizawa, R., Saino, T., Takita, T., Suda, H., Aoyagi, T. J. Med. Chem. (1977) [Pubmed]
  21. Synthesis of sulfur-containing analogues of bestatin. Inhibition of aminopeptidases by alpha-thiolbestatin analogues. Ocain, T.D., Rich, D.H. J. Med. Chem. (1988) [Pubmed]
  22. Altered levels of acid, basic, and neutral peptidase activity and expression in human clear cell renal cell carcinoma. Varona, A., Blanco, L., López, J.I., Gil, J., Agirregoitia, E., Irazusta, J., Larrinaga, G. Am. J. Physiol. Renal Physiol. (2007) [Pubmed]
  23. Brain aminopeptidases and hypertension. Banegas, I., Prieto, I., Vives, F., Alba, F., Gasparo, M., Segarra, A.B., Hermoso, F., Dur??n, R., Ram??rez, M. Journal of the renin-angiotensin-aldosterone system : JRAAS (2006) [Pubmed]
  24. Types and localization of aminopeptidases in different human blood cells. Grdisa, M., Vitale, L. Int. J. Biochem. (1991) [Pubmed]
  25. Identification of human aminopeptidase O, a novel metalloprotease with structural similarity to aminopeptidase B and leukotriene A4 hydrolase. Díaz-Perales, A., Quesada, V., Sánchez, L.M., Ugalde, A.P., Suárez, M.F., Fueyo, A., López-Otín, C. J. Biol. Chem. (2005) [Pubmed]
  26. Differential effect of muscle vibration on intracortical inhibitory circuits in humans. Rosenkranz, K., Rothwell, J.C. J. Physiol. (Lond.) (2003) [Pubmed]
  27. Automated rate nephelometric determination of apolipoproteins AI and B in human serum by consecutive addition of antibodies. Fotiou, F.K. Anal. Chem. (1992) [Pubmed]
  28. Core substructure of the hemiellipsoidal phycobilisome from the red alga Porphyridium cruentum. Redecker, D., Wehrmeyer, W., Reuter, W. Eur. J. Cell Biol. (1993) [Pubmed]
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