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Gene Review

Furin  -  furin (paired basic amino acid cleaving...

Rattus norvegicus

Synonyms: Dibasic-processing enzyme, Fur, PACE, Pace, Paired basic amino acid residue-cleaving enzyme, ...
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Disease relevance of Pcsk3

  • We have identified two rat insulinoma cDNAs that code for proteins homologous to the Kex2 dibasic protease of yeast and the mammalian furin gene product [1].
  • To further define the role of each convertase, and particularly PC1 and PC2, in pro-TRH processing, recombinant vaccinia viruses were used to coexpress the prohormone convertases PC1, PC2, PACE4, PC5-B, furin, or control dynorphin together with rat prepro-TRH in constitutively secreting LoVo cells or in the regulated endocrine GH4C1 cell line [2].
  • Hence, we propose that BDV GP-84 is involved in attachment to the cell surface receptor whereas its furin-cleaved product, GP-43, is involved in pH-dependent fusion after internalization of the virion by endocytosis [3].
  • We therefore compared the specificity of furin with those of proteases in a variety of cultured cells and in a rat Golgi fraction, using the HA cleavage mutants of a virulent avian influenza virus, A/Turkey/Ireland/1378/85 (H5N8) [4].
  • Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-like endoprotease furin [5].

High impact information on Pcsk3

  • Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation [6].
  • Interaction between AP-1 and furin is dependent on phosphorylation of the enzyme's cytoplasmic domain by casein kinase II [6].
  • The cytoplasmic domain mediates localization of furin to the trans-Golgi network en route to the endosomal/lysosomal system [7].
  • To investigate the mechanisms of membrane protein localization to the Golgi complex, we have examined the intracellular trafficking of epitope-tagged forms of the mammalian endopeptidase, furin, in stably transformed rat basophilic leukemia cells [7].
  • Interestingly, deletion of most of the cytoplasmic domain of furin results in a molecule that is predominantly localized to intracellular vesicles, some of which display characteristics of lysosomes [7].

Biological context of Pcsk3


Anatomical context of Pcsk3


Associations of Pcsk3 with chemical compounds

  • Inhibition of furin inhibited angiotensin II-induced TGF-beta1 activation, indicating that TGF-beta1 amplifies its activating convertase in CFBs [13].
  • The PCs furin and PC7, which display a comparable subcellular localization and cleavage activity, were found in VSMCs, but their levels did not increase following PDGF-BB, Ang II, or FCS stimulation [16].
  • Furin expression continued, however, even after the BrdU incorporation decreased [10].
  • After overloading Golgi-derived vesicles with very-low-density lipoproteins (VLDL) by feeding rats with ethanol, the distribution of PC7/LPC was shifted markedly towards lower densities, in contrast with those of furin and the TGN marker [17].
  • To test whether known processing enzymes can perform this cleavage, purified proCPE was incubated with furin, prohormone convertase 1, or a dynorphin converting enzyme, and the products were analyzed on denaturing polyacrylamide gels [18].

Co-localisations of Pcsk3


Regulatory relationships of Pcsk3


Other interactions of Pcsk3

  • The IGF-1 receptor (IGF-1R) and MT1-MMP are synthesized as larger precursor proproteins, which require endoproteolytic activation by the proprotein convertases (PCs) furin/PC5 to gain full biological activity [21].
  • Stepwise posttranslational processing of progrowth hormone-releasing hormone (proGHRH) polypeptide by furin and PC1 [14].
  • Colocalization studies demonstrated that furin is expressed in the parathyroid, whereas proprotein convertase (PC)1 and PC2 are not [22].
  • Furin and PC6 were weakly and evenly expressed in the entire islet [23].
  • These results suggest the involvement of furin in the ConA-induced activations of MT1-MMP and MMP-2 [24].

Analytical, diagnostic and therapeutic context of Pcsk3


  1. Isolation of two complementary deoxyribonucleic acid clones from a rat insulinoma cell line based on similarities to Kex2 and furin sequences and the specific localization of each transcript to endocrine and neuroendocrine tissues in rats. Hakes, D.J., Birch, N.P., Mezey, A., Dixon, J.E. Endocrinology (1991) [Pubmed]
  2. Processing of prothyrotropin-releasing hormone by the family of prohormone convertases. Schaner, P., Todd, R.B., Seidah, N.G., Nillni, E.A. J. Biol. Chem. (1997) [Pubmed]
  3. Mechanism of Borna disease virus entry into cells. Gonzalez-Dunia, D., Cubitt, B., de la Torre, J.C. J. Virol. (1998) [Pubmed]
  4. Sequence specificity of furin, a proprotein-processing endoprotease, for the hemagglutinin of a virulent avian influenza virus. Walker, J.A., Molloy, S.S., Thomas, G., Sakaguchi, T., Yoshida, T., Chambers, T.M., Kawaoka, Y. J. Virol. (1994) [Pubmed]
  5. Processing of the Borna disease virus glycoprotein gp94 by the subtilisin-like endoprotease furin. Richt, J.A., Fürbringer, T., Koch, A., Pfeuffer, I., Herden, C., Bause-Niedrig, I., Garten, W. J. Virol. (1998) [Pubmed]
  6. Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation. Dittié, A.S., Thomas, L., Thomas, G., Tooze, S.A. EMBO J. (1997) [Pubmed]
  7. The cytoplasmic domain mediates localization of furin to the trans-Golgi network en route to the endosomal/lysosomal system. Bosshart, H., Humphrey, J., Deignan, E., Davidson, J., Drazba, J., Yuan, L., Oorschot, V., Peters, P.J., Bonifacino, J.S. J. Cell Biol. (1994) [Pubmed]
  8. The developmental expression in rat of proteases furin, PC1, PC2, and carboxypeptidase E: implications for early maturation of proteolytic processing capacity. Zheng, M., Streck, R.D., Scott, R.E., Seidah, N.G., Pintar, J.E. J. Neurosci. (1994) [Pubmed]
  9. Prohormone-converting enzymes: regulation and evaluation of function using antisense RNA. Bloomquist, B.T., Eipper, B.A., Mains, R.E. Mol. Endocrinol. (1991) [Pubmed]
  10. Developmental expression of proprotein-processing endoprotease furin in rat pancreatic islets. Kayo, T., Konda, Y., Tanaka, S., Takata, K., Koizumi, A., Takeuchi, T. Endocrinology (1996) [Pubmed]
  11. Inhibition of processing of parathyroid hormone-related peptide by anti-sense furin: effect in vitro and in vivo on rat Leydig (H-500) tumor cells. Liu, B., Amizuka, N., Goltzman, D., Rabbani, S.A. Int. J. Cancer (1995) [Pubmed]
  12. Selective expression of the proprotein convertases furin, pc5, and pc7 in proliferating vascular smooth muscle cells of the rat aorta in vitro. Stawowy, P., Marcinkiewicz, J., Graf, K., Seidah, N., Chrétien, M., Fleck, E., Marcinkiewicz, M. J. Histochem. Cytochem. (2001) [Pubmed]
  13. Regulation of matrix metalloproteinase MT1-MMP/MMP-2 in cardiac fibroblasts by TGF-beta1 involves furin-convertase. Stawowy, P., Margeta, C., Kallisch, H., Seidah, N.G., Chrétien, M., Fleck, E., Graf, K. Cardiovasc. Res. (2004) [Pubmed]
  14. Stepwise posttranslational processing of progrowth hormone-releasing hormone (proGHRH) polypeptide by furin and PC1. Posner, S.F., Vaslet, C.A., Jurofcik, M., Lee, A., Seidah, N.G., Nillni, E.A. Endocrine (2004) [Pubmed]
  15. Furin interacts with proMT1-MMP and integrin alphaV at specialized domains of renal cell plasma membrane. Mayer, G., Boileau, G., Bendayan, M. J. Cell. Sci. (2003) [Pubmed]
  16. Proprotein convertase PC5 regulation by PDGF-BB involves PI3-kinase/p70(s6)-kinase activation in vascular smooth muscle cells. Stawowy, P., Blaschke, F., Kilimnik, A., Goetze, S., Kallisch, H., Chrétien, M., Marcinkiewicz, M., Fleck, E., Graf, K. Hypertension (2002) [Pubmed]
  17. Furin and proprotein convertase 7 (PC7)/lymphoma PC endogenously expressed in rat liver can be resolved into distinct post-Golgi compartments. Wouters, S., Leruth, M., Decroly, E., Vandenbranden, M., Creemers, J.W., van de Loo, J.W., Ruysschaert, J.M., Courtoy, P.J. Biochem. J. (1998) [Pubmed]
  18. Processing of procarboxypeptidase E into carboxypeptidase E occurs in secretory vesicles. Song, L., Fricker, L. J. Neurochem. (1995) [Pubmed]
  19. The proprotein convertase furin colocalizes with caveolin-1 in the Golgi apparatus and endosomes of hepatocytes. Mayer, G., Boileau, G., Bendayan, M. Cell Tissue Res. (2004) [Pubmed]
  20. Secretion of soluble leptin receptors by exocrine and endocrine cells of the gastric mucosa. Cammisotto, P.G., Gingras, D., Renaud, C., Levy, E., Bendayan, M. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  21. Proprotein convertases regulate insulin-like growth factor 1-induced membrane-type 1 matrix metalloproteinase in VSMCs via endoproteolytic activation of the insulin-like growth factor-1 receptor. Stawowy, P., Kallisch, H., Kilimnik, A., Margeta, C., Seidah, N.G., Chrétien, M., Fleck, E., Graf, K. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  22. Proparathyroid hormone processing by the proprotein convertase-7: comparison with furin and assessment of modulation of parathyroid convertase messenger ribonucleic acid levels by calcium and 1,25-dihydroxyvitamin D3. Canaff, L., Bennett, H.P., Hou, Y., Seidah, N.G., Hendy, G.N. Endocrinology (1999) [Pubmed]
  23. Distribution of the Kexin family proteases in pancreatic islets: PACE4C is specifically expressed in B cells of pancreatic islets. Nagamune, H., Muramatsu, K., Akamatsu, T., Tamai, Y., Izumi, K., Tsuji, A., Matsuda, Y. Endocrinology (1995) [Pubmed]
  24. Paradigmatic identification of MMP-2 and MT1-MMP activation systems in cardiac fibroblasts cultured as a monolayer. Guo, C., Jiang, J., Elliott, J.M., Piacentini, L. J. Cell. Biochem. (2005) [Pubmed]
  25. The CDX2 transcription factor regulates furin expression during intestinal epithelial cell differentiation. Gendron, F.P., Mongrain, S., Laprise, P., McMahon, S., Dubois, C.M., Blais, M., Asselin, C., Rivard, N. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  26. The distinct gene expression of the pro-hormone convertases in the rat heart suggests potential substrates. Beaubien, G., Schäfer, M.K., Weihe, E., Dong, W., Chrétien, M., Seidah, N.G., Day, R. Cell Tissue Res. (1995) [Pubmed]
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