Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma

Wilharm E, Parry MAA, Friebel R, Tschesche H, Matschiner G, Sommerhoff CP, Jenne DE (1999)
JOURNAL OF BIOLOGICAL CHEMISTRY 274(38): 27331-27337.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Granzymes are granule-stored lymphocyte serine proteases that are implicated in T- and natural killer cell-mediated cytotoxic defense reactions after target cell recognition. A fifth human granzyme (granzyme 3, lymphocyte tryptase-2), renamed as granzyme K (gene name GZMK), has recently been cloned from lymphocyte tissue. For its further characterization we successfully generated catalytically active enzyme in milligram quantities per liter of Escherichia coli culture. The natural preform of granzyme K with the amino-terminal propeptide Met-Glu was expressed as inclusion bodies and converted to its active enzyme by cathepsin C after refolding of precursor molecules. Recombinant granzyme K cleaves synthetic thiobenzyl ester substrates after Lys and Arg with k(cat)/K-m values of 3.7 x 10(4) and 4.4 x 10(4) M-1 s(-1), respectively. Granzyme K activity was shown to be inhibited by the synthetic compounds Phe-Pro-Arg-chloromethyl ketone, phenylmethylsulfonyl fluoride, PefablocSC, and benzamidine, by the Kunitz-type inhibitor aprotinin and by human blood plasma. The plasma-derived inter-alpha-trypsin inhibitor complex, its bikunin subunit, and the second carboxyl-terminal Kunitz-type domain of bikunin were identified as genuine physiologic inhibitors with K-i values of 64, 50, and 22 nM, respectively. Inter-alpha-trypsin inhibitor and free bikunin have the potential to neutralize extracellular granzyme K activity after T cell degranulation and may thus control unspecific damage of bystander cells at sites of inflammatory reactions.
Erscheinungsjahr
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
274
Zeitschriftennummer
38
Seite
27331-27337
ISSN
PUB-ID

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Wilharm E, Parry MAA, Friebel R, et al. Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma. JOURNAL OF BIOLOGICAL CHEMISTRY. 1999;274(38):27331-27337.
Wilharm, E., Parry, M. A. A., Friebel, R., Tschesche, H., Matschiner, G., Sommerhoff, C. P., & Jenne, D. E. (1999). Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma. JOURNAL OF BIOLOGICAL CHEMISTRY, 274(38), 27331-27337. doi:10.1074/jbc.274.38.27331
Wilharm, E., Parry, M. A. A., Friebel, R., Tschesche, H., Matschiner, G., Sommerhoff, C. P., and Jenne, D. E. (1999). Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma. JOURNAL OF BIOLOGICAL CHEMISTRY 274, 27331-27337.
Wilharm, E., et al., 1999. Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma. JOURNAL OF BIOLOGICAL CHEMISTRY, 274(38), p 27331-27337.
E. Wilharm, et al., “Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 274, 1999, pp. 27331-27337.
Wilharm, E., Parry, M.A.A., Friebel, R., Tschesche, H., Matschiner, G., Sommerhoff, C.P., Jenne, D.E.: Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma. JOURNAL OF BIOLOGICAL CHEMISTRY. 274, 27331-27337 (1999).
Wilharm, E, Parry, MAA, Friebel, R, Tschesche, Harald, Matschiner, G, Sommerhoff, CP, and Jenne, DE. “Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma”. JOURNAL OF BIOLOGICAL CHEMISTRY 274.38 (1999): 27331-27337.

38 Zitationen in Europe PMC

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A quarter century of granzymes.
Ewen CL, Kane KP, Bleackley RC., Cell Death Differ 19(1), 2012
PMID: 22052191
Mouse granzyme K has pro-inflammatory potential.
Joeckel LT, Wallich R, Martin P, Sanchez-Martinez D, Weber FC, Martin SF, Borner C, Pardo J, Froelich C, Simon MM., Cell Death Differ 18(7), 2011
PMID: 21311565
Promiscuous processing of human alphabeta-protryptases by cathepsins L, B, and C.
Le QT, Min HK, Xia HZ, Fukuoka Y, Katunuma N, Schwartz LB., J Immunol 186(12), 2011
PMID: 21562164
Processing of human protryptase in mast cells involves cathepsins L, B, and C.
Le QT, Gomez G, Zhao W, Hu J, Xia HZ, Fukuoka Y, Katunuma N, Schwartz LB., J Immunol 187(4), 2011
PMID: 21742978
Functional expression of granzyme B in human plasmacytoid dendritic cells: a role in allergic inflammation.
Bratke K, Nielsen J, Manig F, Klein C, Kuepper M, Geyer S, Julius P, Lommatzsch M, Virchow JC., Clin Exp Allergy 40(7), 2010
PMID: 20412137
Orphan granzymes find a home.
Bovenschen N, Kummer JA., Immunol Rev 235(1), 2010
PMID: 20536559
Death by a thousand cuts: granzyme pathways of programmed cell death.
Chowdhury D, Lieberman J., Annu Rev Immunol 26(), 2008
PMID: 18304003
Granzyme K cleaves the nucleosome assembly protein SET to induce single-stranded DNA nicks of target cells.
Zhao T, Zhang H, Guo Y, Zhang Q, Hua G, Lu H, Hou Q, Liu H, Fan Z., Cell Death Differ 14(3), 2007
PMID: 17008916
Altered levels and molecular forms of granzyme k in plasma from septic patients.
Rucevic M, Fast LD, Jay GD, Trespalcios FM, Sucov A, Siryaporn E, Lim YP., Shock 27(5), 2007
PMID: 17438453
Expression of enzymatically active human granzyme 3 in Escherichia coli for analysis of its substrate specificity.
Hirata Y, Inagaki H, Shimizu T, Li Q, Nagahara N, Minami M, Kawada T., Arch Biochem Biophys 446(1), 2006
PMID: 16405860
Decrease of cytotoxic T cells in allergic asthma correlates with total serum immunglobulin E.
Bratke K, Haupt F, Kuepper M, Bade B, Faehndrich S, Luttmann W, Virchow JC., Allergy 61(11), 2006
PMID: 17002713
Expression, refolding, and purification of recombinant human granzyme B.
Lorentsen RH, Fynbo CH, Thøgersen HC, Etzerodt M, Holtet TL., Protein Expr Purif 39(1), 2005
PMID: 15596356
Pathophysiology and diagnostic value of urinary trypsin inhibitors.
Pugia MJ, Lott JA., Clin Chem Lab Med 43(1), 2005
PMID: 15653436
Plasma bikunin: half-life and tissue uptake.
Kaczmarczyk A, Blom AM, Alston-Smith J, Sjöquist M, Fries E., Mol Cell Biochem 271(1-2), 2005
PMID: 15881656
Immune response in silico (IRIS): immune-specific genes identified from a compendium of microarray expression data.
Abbas AR, Baldwin D, Ma Y, Ouyang W, Gurney A, Martin F, Fong S, van Lookeren Campagne M, Godowski P, Williams PM, Chan AC, Clark HF., Genes Immun 6(4), 2005
PMID: 15789058
Differential expression of the granzymes A, K and M and perforin in human peripheral blood lymphocytes.
Bade B, Boettcher HE, Lohrmann J, Hink-Schauer C, Bratke K, Jenne DE, Virchow JC, Luttmann W., Int Immunol 17(11), 2005
PMID: 16186162
Killing of target cells by redirected granzyme B in the absence of perforin.
Kurschus FC, Kleinschmidt M, Fellows E, Dornmair K, Rudolph R, Lilie H, Jenne DE., FEBS Lett 562(1-3), 2004
PMID: 15044006
Inter-alpha-trypsin inhibitor, a covalent protein-glycosaminoglycan-protein complex.
Zhuo L, Hascall VC, Kimata K., J Biol Chem 279(37), 2004
PMID: 15151994
The protease inhibitor bikunin, a novel anti-metastatic agent.
Kobayashi H, Suzuki M, Hirashima Y, Terao T., Biol Chem 384(5), 2003
PMID: 12817471
Crystal structure of the apoptosis-inducing human granzyme A dimer.
Hink-Schauer C, Estébanez-Perpiñá E, Kurschus FC, Bode W, Jenne DE., Nat Struct Biol 10(7), 2003
PMID: 12819770
Identification of an alternative splicing variant of cathepsin C/dipeptidyl-peptidase I.
Matsui K, Yuyama N, Akaiwa M, Yoshida NL, Maeda M, Sugita Y, Izuhara K., Gene 293(1-2), 2002
PMID: 12137938
The 2.2-A crystal structure of human pro-granzyme K reveals a rigid zymogen with unusual features.
Hink-Schauer C, Estébanez-Perpiñá E, Wilharm E, Fuentes-Prior P, Klinkert W, Bode W, Jenne DE., J Biol Chem 277(52), 2002
PMID: 12384499

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