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Urokinase-type Plasminogen Activator-like Proteases in Teleosts Lack Genuine Receptor-binding Epidermal Growth Factor-like Domains

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Urokinase-type Plasminogen Activator-like Proteases in Teleosts Lack Genuine Receptor-binding Epidermal Growth Factor-like Domains. / Bager, René; Kristensen, Thomas Kielsgaard; Jensen, Jan Kristian; Szczur, Agnieszka; Christensen, Anni; Andersen, Lisbeth Moreau; Johansen, Jesper Sanderhoff; Larsen, Niels; Baatrup, Erik; Huang, Mingdong; Ploug, Michael; Andreasen, Peter.

I: Journal of Biological Chemistry, Bind 287, Nr. 33, 2012, s. 27526-27536.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Bager, R, Kristensen, TK, Jensen, JK, Szczur, A, Christensen, A, Andersen, LM, Johansen, JS, Larsen, N, Baatrup, E, Huang, M, Ploug, M & Andreasen, P 2012, 'Urokinase-type Plasminogen Activator-like Proteases in Teleosts Lack Genuine Receptor-binding Epidermal Growth Factor-like Domains', Journal of Biological Chemistry, bind 287, nr. 33, s. 27526-27536. https://doi.org/10.1074/jbc.M112.369207

APA

Bager, R., Kristensen, T. K., Jensen, J. K., Szczur, A., Christensen, A., Andersen, L. M., Johansen, J. S., Larsen, N., Baatrup, E., Huang, M., Ploug, M., & Andreasen, P. (2012). Urokinase-type Plasminogen Activator-like Proteases in Teleosts Lack Genuine Receptor-binding Epidermal Growth Factor-like Domains. Journal of Biological Chemistry, 287(33), 27526-27536. https://doi.org/10.1074/jbc.M112.369207

CBE

Bager R, Kristensen TK, Jensen JK, Szczur A, Christensen A, Andersen LM, Johansen JS, Larsen N, Baatrup E, Huang M, Ploug M, Andreasen P. 2012. Urokinase-type Plasminogen Activator-like Proteases in Teleosts Lack Genuine Receptor-binding Epidermal Growth Factor-like Domains. Journal of Biological Chemistry. 287(33):27526-27536. https://doi.org/10.1074/jbc.M112.369207

MLA

Vancouver

Author

Bager, René ; Kristensen, Thomas Kielsgaard ; Jensen, Jan Kristian ; Szczur, Agnieszka ; Christensen, Anni ; Andersen, Lisbeth Moreau ; Johansen, Jesper Sanderhoff ; Larsen, Niels ; Baatrup, Erik ; Huang, Mingdong ; Ploug, Michael ; Andreasen, Peter. / Urokinase-type Plasminogen Activator-like Proteases in Teleosts Lack Genuine Receptor-binding Epidermal Growth Factor-like Domains. I: Journal of Biological Chemistry. 2012 ; Bind 287, Nr. 33. s. 27526-27536.

Bibtex

@article{b1892b379dc541d1a3013c64635f35f4,
title = "Urokinase-type Plasminogen Activator-like Proteases in Teleosts Lack Genuine Receptor-binding Epidermal Growth Factor-like Domains",
abstract = "Plasminogen activation catalyzed by urokinase-type plasminogen activator (uPA) plays an important role in normal and pathological tissue remodeling processes. Since its discovery in the mid-1980s, the cell membrane-anchored urokinase-type plasminogen activator receptor (uPAR) has been believed to be central to the functions of uPA, as uPA-catalyzed plasminogen activation activity appeared to be confined to cell surfaces through the binding of uPA to uPAR. However, a functional uPAR has so far only been identified in mammals. We have now cloned, recombinantly produced, and characterized two zebrafish proteases, zfuPA-a and zfuPA-b, which by several criteria are the fish orthologs of mammalian uPA. Thus, both proteases catalyze the activation of fish plasminogen efficiently and both proteases are inhibited rapidly by plasminogen activator inhibitor-1 (PAI-1). But zfuPA-a differs from mammalian uPA by lacking the exon encoding the uPAR-binding epidermal growth factor-like domain; zfuPA-b differs from mammalian uPA by lacking two cysteines of the epidermal growth factor-like domain and a uPAR-binding sequence comparable with that found in mammalian uPA. Accordingly, no zfuPA-b binding activity could be found in fish white blood cells or fish cell lines. We therefore propose that the current consensus of uPA-catalyzed plasminogen activation taking place on cell surfaces, derived from observations with mammals, is too narrow. Fish uPAs appear incapable of receptor binding in the manner known from mammals and uPA-catalyzed plasminogen activation in fish may occur mainly in solution. Studies with nonmammalian vertebrate species are needed to obtain a comprehensive understanding of the mechanism of plasminogen activation.",
author = "Ren{\'e} Bager and Kristensen, {Thomas Kielsgaard} and Jensen, {Jan Kristian} and Agnieszka Szczur and Anni Christensen and Andersen, {Lisbeth Moreau} and Johansen, {Jesper Sanderhoff} and Niels Larsen and Erik Baatrup and Mingdong Huang and Michael Ploug and Peter Andreasen",
year = "2012",
doi = "10.1074/jbc.M112.369207",
language = "English",
volume = "287",
pages = "27526--27536",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "33",

}

RIS

TY - JOUR

T1 - Urokinase-type Plasminogen Activator-like Proteases in Teleosts Lack Genuine Receptor-binding Epidermal Growth Factor-like Domains

AU - Bager, René

AU - Kristensen, Thomas Kielsgaard

AU - Jensen, Jan Kristian

AU - Szczur, Agnieszka

AU - Christensen, Anni

AU - Andersen, Lisbeth Moreau

AU - Johansen, Jesper Sanderhoff

AU - Larsen, Niels

AU - Baatrup, Erik

AU - Huang, Mingdong

AU - Ploug, Michael

AU - Andreasen, Peter

PY - 2012

Y1 - 2012

N2 - Plasminogen activation catalyzed by urokinase-type plasminogen activator (uPA) plays an important role in normal and pathological tissue remodeling processes. Since its discovery in the mid-1980s, the cell membrane-anchored urokinase-type plasminogen activator receptor (uPAR) has been believed to be central to the functions of uPA, as uPA-catalyzed plasminogen activation activity appeared to be confined to cell surfaces through the binding of uPA to uPAR. However, a functional uPAR has so far only been identified in mammals. We have now cloned, recombinantly produced, and characterized two zebrafish proteases, zfuPA-a and zfuPA-b, which by several criteria are the fish orthologs of mammalian uPA. Thus, both proteases catalyze the activation of fish plasminogen efficiently and both proteases are inhibited rapidly by plasminogen activator inhibitor-1 (PAI-1). But zfuPA-a differs from mammalian uPA by lacking the exon encoding the uPAR-binding epidermal growth factor-like domain; zfuPA-b differs from mammalian uPA by lacking two cysteines of the epidermal growth factor-like domain and a uPAR-binding sequence comparable with that found in mammalian uPA. Accordingly, no zfuPA-b binding activity could be found in fish white blood cells or fish cell lines. We therefore propose that the current consensus of uPA-catalyzed plasminogen activation taking place on cell surfaces, derived from observations with mammals, is too narrow. Fish uPAs appear incapable of receptor binding in the manner known from mammals and uPA-catalyzed plasminogen activation in fish may occur mainly in solution. Studies with nonmammalian vertebrate species are needed to obtain a comprehensive understanding of the mechanism of plasminogen activation.

AB - Plasminogen activation catalyzed by urokinase-type plasminogen activator (uPA) plays an important role in normal and pathological tissue remodeling processes. Since its discovery in the mid-1980s, the cell membrane-anchored urokinase-type plasminogen activator receptor (uPAR) has been believed to be central to the functions of uPA, as uPA-catalyzed plasminogen activation activity appeared to be confined to cell surfaces through the binding of uPA to uPAR. However, a functional uPAR has so far only been identified in mammals. We have now cloned, recombinantly produced, and characterized two zebrafish proteases, zfuPA-a and zfuPA-b, which by several criteria are the fish orthologs of mammalian uPA. Thus, both proteases catalyze the activation of fish plasminogen efficiently and both proteases are inhibited rapidly by plasminogen activator inhibitor-1 (PAI-1). But zfuPA-a differs from mammalian uPA by lacking the exon encoding the uPAR-binding epidermal growth factor-like domain; zfuPA-b differs from mammalian uPA by lacking two cysteines of the epidermal growth factor-like domain and a uPAR-binding sequence comparable with that found in mammalian uPA. Accordingly, no zfuPA-b binding activity could be found in fish white blood cells or fish cell lines. We therefore propose that the current consensus of uPA-catalyzed plasminogen activation taking place on cell surfaces, derived from observations with mammals, is too narrow. Fish uPAs appear incapable of receptor binding in the manner known from mammals and uPA-catalyzed plasminogen activation in fish may occur mainly in solution. Studies with nonmammalian vertebrate species are needed to obtain a comprehensive understanding of the mechanism of plasminogen activation.

U2 - 10.1074/jbc.M112.369207

DO - 10.1074/jbc.M112.369207

M3 - Journal article

C2 - 22733817

VL - 287

SP - 27526

EP - 27536

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 33

ER -