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Gene Review

Pcsk5  -  proprotein convertase subtilisin/kexin type 5

Mus musculus

Synonyms: PC5, PC5/6A, PC5A, PC6, Proprotein convertase 5, ...
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Disease relevance of Pcsk5

  • We therefore propose the novel concept that PC6 could be a potential nonhormonal target in the female reproductive tract for dual protection for women, both in preventing pregnancy and reducing HIV infection [1].
  • Since mice and humans harbor both the furin and the PC6 proteases, we suggest that the virulence mechanism responsible for the lethality of influenza viruses in birds also operates in mammalian hosts [2].
  • Experiments in rodent systems have demonstrated a marked anti-tumour effect of the drug aniline mustard (AM) on tumours with high levels of this enzyme (e.g. the plasmacytomas PC5 and PC6) [3].
  • The activities of the enzyme were also investigated in tissues of non-tumour bearing DBA/2 mice and BALB/c mice bearing the PC6 ascites tumour [4].

High impact information on Pcsk5


Biological context of Pcsk5


Anatomical context of Pcsk5

  • This fragment was present in the hippocampus, which expresses PC5A, but was not detectable in the cerebellum, which does not express PC5A [12].
  • Whole mount in situ hybridization to E8.5 embryos demonstrated strong SPC6 expression in the most posterior somite [13].
  • In situ hybridization analysis of sectioned E6.5 embryos in utero demonstrated strong SPC6 expression in differentiated decidua, overlapping and extending beyond the region previously described for the metalloproteinase inhibitor TIMP-2 [13].
  • Lower levels of SPC6 expression were observed in trophoblasts and in the ectoplacental cone, suggesting multiple roles for this enzyme in implantation [13].
  • SPC6 was expressed at low levels throughout the embryo, except in the developing nervous system, and strong expression was observed in the first branchial arch and in skeletal regions of the developing vertebrae, limbs, and craniofacium, suggesting additional roles for SPC6 in skeletogenesis [13].

Associations of Pcsk5 with chemical compounds

  • The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases [14].
  • In COS-1 cells, plasma membrane-associated PC5A can be displaced by heparin, suramin, or heparinases I and III and by competition with excess exogenous TIMP-2 [14].
  • Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease [15].
  • As members of this serine proteinase family are known to activate latent TGFbeta family members which regulate decidual TIMP-3 levels, we sought to characterize the expression of SPC-6 during pregnancy and artificial decidualization [11].
  • Phospholipid composition of small unilamellar liposomes containing melphalan influences drug action in mice bearing PC6 tumours [16].
  • Following stimulation of Y1 cells with adrenocorticotropic hormone or 8-bromo-cyclic AMP, the cell surface labeling of the prosegment of PC5A is greatly diminished, whereas the signal for mature PC5A is increased [17].

Other interactions of Pcsk5

  • In conclusion, the CRD of PC5A and PACE4 functions as a cell surface anchor favoring the processing of their cognate surface-anchored substrates, including endothelial lipase [14].
  • Furin produced larger fragments, whereas PC5-A and PC5-B had negligible effects [18].
  • 5. Like TIMP-3, we demonstrate that SPC-6 expression is induced during the decidual cell response using an in vivo model of artificial decidualization [11].


  1. Inhibiting uterine PC6 blocks embryo implantation: an obligatory role for a proprotein convertase in fertility. Nie, G., Li, Y., Wang, M., Liu, Y.X., Findlay, J.K., Salamonsen, L.A. Biol. Reprod. (2005) [Pubmed]
  2. Biological heterogeneity, including systemic replication in mice, of H5N1 influenza A virus isolates from humans in Hong Kong. Gao, P., Watanabe, S., Ito, T., Goto, H., Wells, K., McGregor, M., Cooley, A.J., Kawaoka, Y. J. Virol. (1999) [Pubmed]
  3. Response of a high-glucuronidase human tumour xenograft to aniline mustard. Warenius, H.M., Workman, P., Bleehen, N.M. Br. J. Cancer (1982) [Pubmed]
  4. Activities of serine hydroxymethyltransferase in murine tissues and tumours. Tendler, S.J., Threadgill, M.D., Tisdale, M.J. Cancer Lett. (1987) [Pubmed]
  5. SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone morphogenetic proteins at distinct sites during embryogenesis. Constam, D.B., Calfon, M., Robertson, E.J. J. Cell Biol. (1996) [Pubmed]
  6. The isoforms of proprotein convertase PC5 are sorted to different subcellular compartments. De Bie, I., Marcinkiewicz, M., Malide, D., Lazure, C., Nakayama, K., Bendayan, M., Seidah, N.G. J. Cell Biol. (1996) [Pubmed]
  7. Deletion of the gene encoding proprotein convertase 5/6 causes early embryonic lethality in the mouse. Essalmani, R., Hamelin, J., Marcinkiewicz, J., Chamberland, A., Mbikay, M., Chrétien, M., Seidah, N.G., Prat, A. Mol. Cell. Biol. (2006) [Pubmed]
  8. Decidual differentiation of stromal cells promotes Proprotein Convertase 5/6 expression and lefty processing. Tang, M., Mikhailik, A., Pauli, I., Giudice, L.C., Fazelabas, A.T., Tulac, S., Carson, D.D., Kaufman, D.G., Barbier, C., Creemers, J.W., Tabibzadeh, S. Endocrinology (2005) [Pubmed]
  9. Identification and functional expression of a new member of the mammalian Kex2-like processing endoprotease family: its striking structural similarity to PACE4. Nakagawa, T., Hosaka, M., Torii, S., Watanabe, T., Murakami, K., Nakayama, K. J. Biochem. (1993) [Pubmed]
  10. Specific and transient up-regulation of proprotein convertase 6 at the site of embryo implantation and identification of a unique transcript in mouse uterus during early pregnancy. Nie, G.Y., Li, Y., Minoura, H., Findlay, J.K., Salamonsen, L.A. Biol. Reprod. (2003) [Pubmed]
  11. Subtilisin proprotein convertase-6 expression in the mouse uterus during implantation and artificially induced decidualization. Wong, B.S., Liu, S., Schultz, G.A., Rancourt, D.E. Mol. Reprod. Dev. (2002) [Pubmed]
  12. The proprotein convertase PC5A and a metalloprotease are involved in the proteolytic processing of the neural adhesion molecule L1. Kalus, I., Schnegelsberg, B., Seidah, N.G., Kleene, R., Schachner, M. J. Biol. Chem. (2003) [Pubmed]
  13. Murine subtilisin-like proteinase SPC6 is expressed during embryonic implantation, somitogenesis, and skeletal formation. Rancourt, S.L., Rancourt, D.E. Dev. Genet. (1997) [Pubmed]
  14. The cysteine-rich domain of the secreted proprotein convertases PC5A and PACE4 functions as a cell surface anchor and interacts with tissue inhibitors of metalloproteinases. Nour, N., Mayer, G., Mort, J.S., Salvas, A., Mbikay, M., Morrison, C.J., Overall, C.M., Seidah, N.G. Mol. Biol. Cell (2005) [Pubmed]
  15. Identification of an isoform with an extremely large Cys-rich region of PC6, a Kex2-like processing endoprotease. Nakagawa, T., Murakami, K., Nakayama, K. FEBS Lett. (1993) [Pubmed]
  16. Phospholipid composition of small unilamellar liposomes containing melphalan influences drug action in mice bearing PC6 tumours. Large, P., Gregoriadis, G. Biochem. Pharmacol. (1983) [Pubmed]
  17. The regulated cell surface zymogen activation of the proprotein convertase PC5A directs the processing of its secretory substrates. Mayer, G., Hamelin, J., Asselin, M.C., Pasquato, A., Marcinkiewicz, E., Tang, M., Tabibzadeh, S., Seidah, N.G. J. Biol. Chem. (2008) [Pubmed]
  18. Proteolytic processing of chromogranin B and secretogranin II by prohormone convertases. Laslop, A., Weiss, C., Savaria, D., Eiter, C., Tooze, S.A., Seidah, N.G., Winkler, H. J. Neurochem. (1998) [Pubmed]
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