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Gene Review

QSOX1  -  quiescin Q6 sulfhydryl oxidase 1

Homo sapiens

Synonyms: Q6, QSCN6, Quiescin Q6, Sulfhydryl oxidase 1, UNQ2520/PRO6013, ...
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Disease relevance of QSOX1


High impact information on QSOX1

  • Q6 is strongly expressed when fibroblasts enter reversible quiescence (Coppock, D. L., Cina-Poppe, D., Gilleran, S. (1998) Genomics 54, 460-468) [3].
  • Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases [3].
  • A peptide antibody against Q6 cross-reacts with both the egg white enzyme and a flavin-linked sulfhydryl oxidase isolated from bovine semen [3].
  • These domains apparently underwent a gene fusion event during metazoan evolution to create QSCN6 [1].
  • The expression of decorin and Q6 was very low in SV40-transformed cells (VA13) either in logarithmic growth or at high density, whereas the gene Q10 was expressed more highly in VA13 than in WI38 cells [4].

Biological context of QSOX1


Anatomical context of QSOX1

  • We have identified a gene, Quiescin Q6 (QSCN6), whose expression is induced just as fibroblasts begin to leave the proliferative cycle and enter quiescence [1].
  • Expression of Q6 and S29 mRNAs in endothelial cells was low in growth phase and high in quiescent cells [9].
  • Consistent with this role in the formation of disulfide bonds, QSOX is typically found in the cell in the endoplasmic reticulum and Golgi and outside the cell [5].
  • Expression of the secreted FAD-dependent sulfydryl oxidase (QSOX) in the guinea pig central nervous system [10].
  • According to the nucleotide and protein sequence similarities, SOx-3 belonged to the FAD-linked sulfhydryl oxidase family containing the egg white sulfhydryl oxidase, the rat seminal vesicle sulfhydryl oxidase-2 SOx-2, the quiescence-inducible protein hQ6 [11].

Associations of QSOX1 with chemical compounds

  • The avian QSOX is the best understood enzymatically: its preferred substrates are peptides and proteins, not monothiols such as glutathione [5].

Other interactions of QSOX1


Analytical, diagnostic and therapeutic context of QSOX1

  • Sequence analyses show that the egg white oxidase joins human Q6, bone-derived growth factor, GEC-3 from guinea pig, and homologs found in a range of multicellular organisms as a member of a new protein family [3].


  1. The quiescin Q6 gene (QSCN6) is a fusion of two ancient gene families: thioredoxin and ERV1. Coppock, D.L., Cina-Poppe, D., Gilleran, S. Genomics (1998) [Pubmed]
  2. Cell-specific localization of the sulphydryl oxidase QSOX in rat peripheral tissues. Tury, A., Mairet-Coello, G., Esnard-Fève, A., Benayoun, B., Risold, P.Y., Griffond, B., Fellmann, D. Cell Tissue Res. (2006) [Pubmed]
  3. Homology between egg white sulfhydryl oxidase and quiescin Q6 defines a new class of flavin-linked sulfhydryl oxidases. Hoober, K.L., Glynn, N.M., Burnside, J., Coppock, D.L., Thorpe, C. J. Biol. Chem. (1999) [Pubmed]
  4. Preferential gene expression in quiescent human lung fibroblasts. Coppock, D.L., Kopman, C., Scandalis, S., Gilleran, S. Cell Growth Differ. (1993) [Pubmed]
  5. Sulfhydryl oxidases: emerging catalysts of protein disulfide bond formation in eukaryotes. Thorpe, C., Hoober, K.L., Raje, S., Glynn, N.M., Burnside, J., Turi, G.K., Coppock, D.L. Arch. Biochem. Biophys. (2002) [Pubmed]
  6. Identification of genes linked to gefitinib treatment in prostate cancer cell lines with or without resistance to androgen: A clue to application of gefitinib to hormone-resistant prostate cancer. Yano, S., Matsuyama, H., Hirata, H., Inoue, R., Matsumoto, H., Ohmi, C., Miura, K., Shirai, M., Iizuka, N., Naito, K. Oncol. Rep. (2006) [Pubmed]
  7. Multidomain flavin-dependent sulfhydryl oxidases. Coppock, D.L., Thorpe, C. Antioxid. Redox Signal. (2006) [Pubmed]
  8. High levels of active quiescin Q6 sulfhydryl oxidase (QSOX) are selectively present in fetal serum. Zanata, S.M., Luvizon, A.C., Batista, D.F., Ikegami, C.M., Pedrosa, F.O., Souza, E.M., Chaves, D.F., Caron, L.F., Pelizzari, J.V., Laurindo, F.R., Nakao, L.S. Redox Rep. (2005) [Pubmed]
  9. Regulation of the quiescence-induced genes: quiescin Q6, decorin, and ribosomal protein S29. Coppock, D., Kopman, C., Gudas, J., Cina-Poppe, D.A. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  10. Expression of the secreted FAD-dependent sulfydryl oxidase (QSOX) in the guinea pig central nervous system. Amiot, C., Musard, J.F., Hadjiyiassemis, M., Jouvenot, M., Fellmann, D., Risold, P.Y., Adami, P. Brain Res. Mol. Brain Res. (2004) [Pubmed]
  11. Identification and expression of a new sulfhydryl oxidase SOx-3 during the cell cycle and the estrus cycle in uterine cells. Musard, J.F., Sallot, M., Dulieu, P., Fraîchard, A., Ordener, C., Remy-Martin, J.P., Jouvenot, M., Adami, P. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
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