Inhibition of furin by serpin Spn4A from Drosophila melanogaster

Oley M, Letzel M, Ragg H (2004)
FEBS Letters 577(1-2): 165-169.

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The serpin gene Spn4 from Drosophila melanogaster encodes multiple isoforms with alternative reactive site loops (RSL). Here, we show that isoform Spn4A inhibits human furin with an apparent k(assoc) of 5.5 x 10(6) M-1 s(-1). The serpin forms SDS-stable complexes with the enzyme and the RSL of Spn4A is cleaved C-terminally to the sequence -Arg-Arg-Lys-Argdown arrow in accord with the recognition/cleavage site of furin. Immunofluorescence studies show that Spn4A is localized in the endoplasmic reticulum (ER), suggesting that the inhibitor is an interesting tool for investigating the cellular mechanisms regulating furin and for the design of agents controlling prohormone convertases. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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Oley M, Letzel M, Ragg H. Inhibition of furin by serpin Spn4A from Drosophila melanogaster. FEBS Letters. 2004;577(1-2):165-169.
Oley, M., Letzel, M., & Ragg, H. (2004). Inhibition of furin by serpin Spn4A from Drosophila melanogaster. FEBS Letters, 577(1-2), 165-169.
Oley, M., Letzel, M., and Ragg, H. (2004). Inhibition of furin by serpin Spn4A from Drosophila melanogaster. FEBS Letters 577, 165-169.
Oley, M., Letzel, M., & Ragg, H., 2004. Inhibition of furin by serpin Spn4A from Drosophila melanogaster. FEBS Letters, 577(1-2), p 165-169.
M. Oley, M. Letzel, and H. Ragg, “Inhibition of furin by serpin Spn4A from Drosophila melanogaster”, FEBS Letters, vol. 577, 2004, pp. 165-169.
Oley, M., Letzel, M., Ragg, H.: Inhibition of furin by serpin Spn4A from Drosophila melanogaster. FEBS Letters. 577, 165-169 (2004).
Oley, Mareke, Letzel, Matthias, and Ragg, Hermann. “Inhibition of furin by serpin Spn4A from Drosophila melanogaster”. FEBS Letters 577.1-2 (2004): 165-169.
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16 Citations in Europe PMC

Data provided by Europe PubMed Central.

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Wang Y, Koster K, Lummer M, Ragg H., PLoS ONE 9(5), 2014
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High resolution structure of cleaved Serpin 42 Da from Drosophila melanogaster.
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Identification and analysis of serpin-family genes by homology and synteny across the 12 sequenced Drosophilid genomes.
Garrett M, Fullaondo A, Troxler L, Micklem G, Gubb D., BMC Genomics 10(), 2009
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The serpin gene family in Anopheles gambiae.
Suwanchaichinda C, Kanost MR., Gene 442(1-2), 2009
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Ancestry and evolution of a secretory pathway serpin.
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Serpins in plants and green algae.
Roberts TH, Hejgaard J., Funct. Integr. Genomics 8(1), 2008
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Possible role of histone H1 in the regulation of furin-dependent proprotein processing.
Han J, Gu J, Chi C., Acta Biochim. Biophys. Sin. (Shanghai) 39(3), 2007
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Synthetic small molecule furin inhibitors derived from 2,5-dideoxystreptamine.
Jiao GS, Cregar L, Wang J, Millis SZ, Tang C, O'Malley S, Johnson AT, Sareth S, Larson J, Thomas G., Proc. Natl. Acad. Sci. U.S.A. 103(52), 2006
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The potent inhibitory activity of histone H1.2 C-terminal fragments on furin.
Han J, Zhang L, Shao X, Shi J, Chi C., FEBS J. 273(19), 2006
PMID: 16956366
Tip of another iceberg: Drosophila serpins.
Reichhart JM., Trends Cell Biol. 15(12), 2005
PMID: 16260136

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