The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

RNASE3  -  ribonuclease, RNase A family, 3

Homo sapiens

Synonyms: ECP, Eosinophil cationic protein, RNS3, RNase 3, Ribonuclease 3
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of RNASE3

  • Eosinophil cationic protein (ECP) is located in the matrix of the eosinophil's large specific granule and has marked toxicity for a variety of helminth parasites, hemoflagellates, bacteria, single-stranded RNA virus, and mammalian cells and tissues [1].
  • By utilizing the colloidal gold particle technique, we localized eosinophil granule major basic protein, eosinophil cationic protein (ECP), and eosinophil-derived neurotoxin (EDN) in human nasal polyp sections by immunoelectron microscopy [2].
  • CONCLUSIONS: ECP contributes to surfactant dysfunction in asthma, which in turn could lead to airway obstruction [3].
  • ECP concentration in milk was under the detection limit (2 microg/L) in all the mothers with a healthy infant, whereas detectable levels were found in 27% of mothers with a CMA infant and in 42% of those with a baby with atopic dermatitis [4].
  • This is the first demonstration that some eosinophil cationic proteins, namely ECP and MBP, found at the site of heart damage in patients with eosinophilia, act as complete secretagogues on HHMC [5].

High impact information on RNASE3


Chemical compound and disease context of RNASE3


Biological context of RNASE3

  • ECP is a small, basic protein found in the matrix of the eosinophil's large specific granule that has cytotoxic, helminthotoxic, and ribonuclease activity, and is a member of the ribonuclease multigene family [8].
  • Amino acid sequence analyses showed that ECP-1 and ECP-2 are identical from residue 1 through residue 59 and that the sequences of EDN and ECP are highly homologous (37 of 55 residues identical) [14].
  • PD98 059 and SB202 190 both caused inhibition of eotaxin-induced ECP release and chemotaxis [15].
  • The ECP nucleotide sequence shows similarity to EDN, rat pancreatic ribonuclease, and human angiogenin; all are members of the ribonuclease gene superfamily [16].
  • Here we present evidence demonstrating that the gene encoding ECP is regulated in an analogous fashion and that an intronic enhancer element functioning in both genes is a consensus binding sequence for the transcription factor NFAT-1 [17].

Anatomical context of RNASE3

  • We have isolated a 725-bp full-length cDNA clone for the human eosinophil cationic protein (ECP) [8].
  • The eosinophil-derived neurotoxin (EDN) and eosinophil cationic protein (ECP) are both small, cationic ribonuclease toxins that are stored in and secreted by activated human eosinophilic leukocytes [17].
  • The high concentration of positive charges and the particular orientation of the side-chains of these residues may also be related to the low activity of ECP as a ribonuclease and provides an explanation for its unique cytotoxic role through cell membrane disruption [18].
  • We tested whether EDN and ECP are present in mature neutrophils [19].
  • ECP concentration in human milk was measured by commercial UniCAP method [4].

Associations of RNASE3 with chemical compounds

  • Both ECP and EDN possess neurotoxic and ribonuclease activities [16].
  • In addition, degranulation of ECP in response to Ca(2+) ionophore, immobilized IgG and serum from allergic patients was inhibited by SP-D [20].
  • Restimulation with the same agonist (PAF or C5a) was unsuccessful as assessed by monitoring intracellular calcium concentration and ECP release [21].
  • ECP levels after allergen challenge correlate well to surfactant dysfunction [3].
  • Suplatast tosilate (IPD-1151T), a new anti-allergic agent, has shown beneficial effect in the treatment of asthma, associated with reduced bronchoalveolar lavage eosinophil infiltration and eosinophilic cationic protein (ECP) release in serum and sputum [22].
  • Analysis of ECP mt1 (R34A/W35A/R36A/K38A) showed that these charged and aromatic residues were involved in ECP binding to heparin and the cell surface [23].

Other interactions of RNASE3


Analytical, diagnostic and therapeutic context of RNASE3


  1. Crystal structure of eosinophil cationic protein at 2.4 A resolution. Boix, E., Leonidas, D.D., Nikolovski, Z., Nogués, M.V., Cuchillo, C.M., Acharya, K.R. Biochemistry (1999) [Pubmed]
  2. Localization of human eosinophil granule major basic protein, eosinophil cationic protein, and eosinophil-derived neurotoxin by immunoelectron microscopy. Peters, M.S., Rodriguez, M., Gleich, G.J. Lab. Invest. (1986) [Pubmed]
  3. Eosinophil cationic protein alters pulmonary surfactant structure and function in asthma. Hohlfeld, J.M., Schmiedl, A., Erpenbeck, V.J., Venge, P., Krug, N. J. Allergy Clin. Immunol. (2004) [Pubmed]
  4. Eosinophil cationic protein in human milk is associated with development of cow's milk allergy and atopic eczema in breast-fed infants. Osterlund, P., Smedberg, T., Hakulinen, A., Heikkilä, H., Järvinen, K.M. Pediatr. Res. (2004) [Pubmed]
  5. Eosinophil granule proteins activate human heart mast cells. Patella, V., de Crescenzo, G., Marinò, I., Genovese, A., Adt, M., Gleich, G.J., Marone, G. J. Immunol. (1996) [Pubmed]
  6. Rapid evolution of a unique family of primate ribonuclease genes. Rosenberg, H.F., Dyer, K.D., Tiffany, H.L., Gonzalez, M. Nat. Genet. (1995) [Pubmed]
  7. Mechanism of membrane damage mediated by human eosinophil cationic protein. Young, J.D., Peterson, C.G., Venge, P., Cohn, Z.A. Nature (1986) [Pubmed]
  8. Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity. Rosenberg, H.F., Ackerman, S.J., Tenen, D.G. J. Exp. Med. (1989) [Pubmed]
  9. Total and specific IgE in nasal polyps is related to local eosinophilic inflammation. Bachert, C., Gevaert, P., Holtappels, G., Johansson, S.G., van Cauwenberge, P. J. Allergy Clin. Immunol. (2001) [Pubmed]
  10. The eosinophil and the eye. Bonini, S., Magrini, L., Rotiroti, G., Lambiase, A., Tomassini, M., Rumi, C., Bonini, S. Allergy (1997) [Pubmed]
  11. Monitoring of disease activity by measurement of inflammatory markers in atopic dermatitis in childhood. Halmerbauer, G., Frischer, T., Koller, D.Y. Allergy (1997) [Pubmed]
  12. Antibacterial properties of eosinophil major basic protein and eosinophil cationic protein. Lehrer, R.I., Szklarek, D., Barton, A., Ganz, T., Hamann, K.J., Gleich, G.J. J. Immunol. (1989) [Pubmed]
  13. Challenge with gliadin induces eosinophil and mast cell activation in the jejunum of patients with celiac disease. Lavö, B., Knutson, L., Lööf, L., Odlind, B., Venge, P., Hällgren, R. Am. J. Med. (1989) [Pubmed]
  14. Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. Gleich, G.J., Loegering, D.A., Bell, M.P., Checkel, J.L., Ackerman, S.J., McKean, D.J. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  15. Eotaxin induces degranulation and chemotaxis of eosinophils through the activation of ERK2 and p38 mitogen-activated protein kinases. Kampen, G.T., Stafford, S., Adachi, T., Jinquan, T., Quan, S., Grant, J.A., Skov, P.S., Poulsen, L.K., Alam, R. Blood (2000) [Pubmed]
  16. Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases. Barker, R.L., Loegering, D.A., Ten, R.M., Hamann, K.J., Pease, L.R., Gleich, G.J. J. Immunol. (1989) [Pubmed]
  17. Intronic enhancer activity of the eosinophil-derived neurotoxin (RNS2) and eosinophil cationic protein (RNS3) genes is mediated by an NFAT-1 consensus binding sequence. Handen, J.S., Rosenberg, H.F. J. Biol. Chem. (1997) [Pubmed]
  18. Three-dimensional crystal structure of human eosinophil cationic protein (RNase 3) at 1.75 A resolution. Mallorquí-Fernández, G., Pous, J., Peracaula, R., Aymamí, J., Maeda, T., Tada, H., Yamada, H., Seno, M., de Llorens, R., Gomis-Rüth, F.X., Coll, M. J. Mol. Biol. (2000) [Pubmed]
  19. Localization of eosinophil-derived neurotoxin and eosinophil cationic protein in neutrophilic leukocytes. Sur, S., Glitz, D.G., Kita, H., Kujawa, S.M., Peterson, E.A., Weiler, D.A., Kephart, G.M., Wagner, J.M., George, T.J., Gleich, G.J., Leiferman, K.M. J. Leukoc. Biol. (1998) [Pubmed]
  20. Surfactant protein D regulates chemotaxis and degranulation of human eosinophils. von Bredow, C., Hartl, D., Schmid, K., Schabaz, F., Brack, E., Reinhardt, D., Griese, M. Clin. Exp. Allergy (2006) [Pubmed]
  21. Eosinophils maintain their capacity to signal and release eosinophil cationic protein upon repetitive stimulation with the same agonist. Simon, H.U., Weber, M., Becker, E., Zilberman, Y., Blaser, K., Levi-Schaffer, F. J. Immunol. (2000) [Pubmed]
  22. CD28 and secretory immunoglobulin A-dependent activation of eosinophils: inhibition of mediator release by the anti-allergic drug, suplatast tosilate. Woerly, G., Decot, V., Loiseau, S., Loyens, M., Chihara, J., Ono, N., Capron, M. Clin. Exp. Allergy (2004) [Pubmed]
  23. Characterization of molecular interactions between eosinophil cationic protein and heparin. Fan, T.C., Fang, S.L., Hwang, C.S., Hsu, C.Y., Lu, X.A., Hung, S.C., Lin, S.C., Chang, M.D. J. Biol. Chem. (2008) [Pubmed]
  24. Eosinophil cationic protein/RNase 3 is another RNase A-family ribonuclease with direct antiviral activity. Domachowske, J.B., Dyer, K.D., Adams, A.G., Leto, T.L., Rosenberg, H.F. Nucleic Acids Res. (1998) [Pubmed]
  25. Polymorphism of the eosinophil cationic protein-gene is related to the expression of allergic symptoms. Jönsson, U.B., Byström, J., Stålenheim, G., Venge, P. Clin. Exp. Allergy (2002) [Pubmed]
WikiGenes - Universities