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Gene Review

DEFA3  -  defensin, alpha 3, neutrophil-specific

Homo sapiens

Synonyms: DEF3, Defensin, alpha 3, HNP-3, HNP3, HP-3, ...
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Disease relevance of DEFA3


High impact information on DEFA3

  • Using the most stringent statistical analysis (Bonferroni correction), 15 genes were found highly up-regulated in SLE patients, 14 of which are targets of IFN and one, defensin DEFA-3, a major product of immature granulocytes [6].
  • Purified preparations of each of the three human defensins (HNP-1, HNP-2, HNP-3) were then tested [7].
  • Three defensins (human neutrophil peptide defensin [HNP]-1, HNP-2, and HNP-3) constitute between 30 and 50% of the total protein in azurophil granules of human PMN [8].
  • We investigated the regulation of HNP-1 and HNP-3 expression at the transcriptional level using a promyelocytic HL-60 cell line [9].
  • We conclude that individuals can inherit versions of chromosome 8 harboring either two or three copies of the genes that encode the HP-1, HP-2, and/or HP-3 peptides [10].

Chemical compound and disease context of DEFA3


Biological context of DEFA3

  • Inter-population variability of DEFA3 gene absence: correlation with haplotype structure and population variability [11].
  • Association analysis of DEFA3 absence with 136 SNPs from a 100-kb region identified a conserved haplotype in the Caucasian population, extending for the whole region [11].
  • The alpha-defensin cluster on human chromosome 8p23.1 is one of the better-characterized CNVs, in which high copy number variability affecting the DEFA1 and DEFA3 genes has been reported [11].
  • Although the primary amino acid sequences of HNP-1, 2, and 3 are identical except for a single amino-terminal amino acid alteration, HNP-1 and HNP-2 killed C. albicans but HNP-3 did not [12].
  • The results of the study suggest that human alpha-defensins HNP-1, HNP-2, and HNP-3 are up-regulated after surgery, and may in addition to their antimicrobial properties have an important role in wound healing [13].

Anatomical context of DEFA3

  • Inheritance of unequal numbers of the genes encoding the human neutrophil defensins HP-1 and HP-3 [10].
  • Purified defensins HNP-1 and HNP-2 (kindly provided by Dr. R. I. Lehrer, UCLA) were also potent chemoattractants for human T-cells, while HNP-3 was inactive [14].
  • Human defensin HNP-1 and the closely related HNP-3 are amphiphilic dimers that act in part by permeabilizing cell membranes [15].
  • Four monoclonal antibodies (HP-1, HP-2, HP-3 and HP-4) with differing reactivities were raised against human synovial fluid phospholipase A2 [16].

Associations of DEFA3 with chemical compounds

  • The peptides, HNP-1, HNP-2, and HNP-3, which we have termed defensins, were rich in cystine, arginine, and aromatic residues, but were devoid of free sulfhydryl groups and carbohydrate moieties [17].
  • The first peak was resolved further by C4 reversed phase HPLC and yielded an active fraction shown by NH2-terminal amino acid sequence analysis to contain defensins HNP-1, HNP-2, and HNP-3 [14].
  • Bilirubin UGTs (HP2 and HP3) were not detectable in the kidney and HP3 was the major isoform in the liver [18].

Analytical, diagnostic and therapeutic context of DEFA3

  • MEASUREMENTS AND RESULTS: Concentrations of alpha-defensins (human neutrophil peptide [HNP]-1, HNP-2, and HNP-3) were measured by radioimmunoassay in plasma and BAL fluid (BALF) [19].
  • Using ultrafiltration to remove the high molecular weight toxin and enzymes followed by reverse-phase HPLC, three bioactive tridecapeptides, designated "HP-1, HP-2 and HP-3" were isolated from the venom [20].


  1. Theta defensins protect cells from infection by herpes simplex virus by inhibiting viral adhesion and entry. Yasin, B., Wang, W., Pang, M., Cheshenko, N., Hong, T., Waring, A.J., Herold, B.C., Wagar, E.A., Lehrer, R.I. J. Virol. (2004) [Pubmed]
  2. In vitro sensitivity of oral, gram-negative, facultative bacteria to the bactericidal activity of human neutrophil defensins. Miyasaki, K.T., Bodeau, A.L., Ganz, T., Selsted, M.E., Lehrer, R.I. Infect. Immun. (1990) [Pubmed]
  3. Antibacterial activity and specificity of the six human {alpha}-defensins. Ericksen, B., Wu, Z., Lu, W., Lehrer, R.I. Antimicrob. Agents Chemother. (2005) [Pubmed]
  4. Identification of HNP3 as a tumour marker in CD4+ and CD4- lymphocytes of patients with cutaneous T-cell lymphoma. Escher, N., Spies-Weisshart, B., Kaatz, M., Melle, C., Bleul, A., Driesch, D., Wollina, U., von Eggeling, F. Eur. J. Cancer (2006) [Pubmed]
  5. Neutrophil lysosomal nonoxidative microbicidal proteins in early-onset periodontitis. Flemmig, T.F., Miyasaki, K.T. Oral Microbiol. Immunol. (1994) [Pubmed]
  6. Interferon and granulopoiesis signatures in systemic lupus erythematosus blood. Bennett, L., Palucka, A.K., Arce, E., Cantrell, V., Borvak, J., Banchereau, J., Pascual, V. J. Exp. Med. (2003) [Pubmed]
  7. Monocyte-chemotactic activity of defensins from human neutrophils. Territo, M.C., Ganz, T., Selsted, M.E., Lehrer, R. J. Clin. Invest. (1989) [Pubmed]
  8. Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity. Lehrer, R.I., Barton, A., Daher, K.A., Harwig, S.S., Ganz, T., Selsted, M.E. J. Clin. Invest. (1989) [Pubmed]
  9. Role of CCAAT/enhancer-binding protein site in transcription of human neutrophil peptide-1 and -3 defensin genes. Tsutsumi-Ishii, Y., Hasebe, T., Nagaoka, I. J. Immunol. (2000) [Pubmed]
  10. Inheritance of unequal numbers of the genes encoding the human neutrophil defensins HP-1 and HP-3. Mars, W.M., Patmasiriwat, P., Maity, T., Huff, V., Weil, M.M., Saunders, G.F. J. Biol. Chem. (1995) [Pubmed]
  11. Inter-population variability of DEFA3 gene absence: correlation with haplotype structure and population variability. Ballana, E., González, J.R., Bosch, N., Estivill, X. BMC Genomics (2007) [Pubmed]
  12. Modulation of the in vitro candidacidal activity of human neutrophil defensins by target cell metabolism and divalent cations. Lehrer, R.I., Ganz, T., Szklarek, D., Selsted, M.E. J. Clin. Invest. (1988) [Pubmed]
  13. Proteomic analysis of human tears: defensin expression after ocular surface surgery. Zhou, L., Huang, L.Q., Beuerman, R.W., Grigg, M.E., Li, S.F., Chew, F.T., Ang, L., Stern, M.E., Tan, D. J. Proteome Res. (2004) [Pubmed]
  14. Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils. Chertov, O., Michiel, D.F., Xu, L., Wang, J.M., Tani, K., Murphy, W.J., Longo, D.L., Taub, D.D., Oppenheim, J.J. J. Biol. Chem. (1996) [Pubmed]
  15. Biosynthesis of defensins and other antimicrobial peptides. Ganz, T. Ciba Found. Symp. (1994) [Pubmed]
  16. Monoclonal antibodies against human synovial phospholipase A2. Takayama, K., Kudo, I., Hara, S., Murakami, M., Matsuta, K., Miyamoto, T., Inoue, K. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  17. Primary structures of three human neutrophil defensins. Selsted, M.E., Harwig, S.S., Ganz, T., Schilling, J.W., Lehrer, R.I. J. Clin. Invest. (1985) [Pubmed]
  18. The expression of UDP-glucuronosyltransferases of the UGT1 family in human liver and kidney and in response to drugs. Sutherland, L., Ebner, T., Burchell, B. Biochem. Pharmacol. (1993) [Pubmed]
  19. Elevated levels of alpha-defensins in plasma and BAL fluid of patients with active pulmonary tuberculosis. Ashitani, J., Mukae, H., Hiratsuka, T., Nakazato, M., Kumamoto, K., Matsukura, S. Chest (2002) [Pubmed]
  20. Structures and biological activities of new wasp venom peptides isolated from the black-bellied hornet (Vespa basalis) venom. Ho, C.L., Chen, W.C., Lin, Y.L. Toxicon (1998) [Pubmed]
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