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Jens Christian Jensenius

Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2

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Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2. / Rossi, V; Cseh, S; Bally, I; Thielens, N M; Jensenius, Jens Christian; Arlaud, G J.

In: Journal of Biological Chemistry, Vol. 276, No. 44, 2001, p. 40880-7.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

Harvard

Rossi, V, Cseh, S, Bally, I, Thielens, NM, Jensenius, JC & Arlaud, GJ 2001, 'Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2', Journal of Biological Chemistry, vol. 276, no. 44, pp. 40880-7. https://doi.org/10.1074/jbc.M105934200

APA

Rossi, V., Cseh, S., Bally, I., Thielens, N. M., Jensenius, J. C., & Arlaud, G. J. (2001). Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2. Journal of Biological Chemistry, 276(44), 40880-7. https://doi.org/10.1074/jbc.M105934200

CBE

Rossi V, Cseh S, Bally I, Thielens NM, Jensenius JC, Arlaud GJ. 2001. Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2. Journal of Biological Chemistry. 276(44):40880-7. https://doi.org/10.1074/jbc.M105934200

MLA

Vancouver

Rossi V, Cseh S, Bally I, Thielens NM, Jensenius JC, Arlaud GJ. Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2. Journal of Biological Chemistry. 2001;276(44):40880-7. https://doi.org/10.1074/jbc.M105934200

Author

Rossi, V ; Cseh, S ; Bally, I ; Thielens, N M ; Jensenius, Jens Christian ; Arlaud, G J. / Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 44. pp. 40880-7.

Bibtex

@article{feb1eaa8619645da8dc6389cde908c8b,
title = "Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2",
abstract = "Mannan-binding lectin (MBL)-associated serine proteases-1 and 2 (MASP-1 and MASP-2) are homologous modular proteases that each interact with MBL, an oligomeric serum lectin involved in innate immunity. To precisely determine their substrate specificity, human MASP-1 and MASP-2, and fragments from their catalytic regions were expressed using a baculovirus/insect cells system. Recombinant MASP-2 displayed a rather wide, C1s-like esterolytic activity, and specifically cleaved complement proteins C2 and C4, with relative efficiencies 3- and 23-fold higher, respectively, than human C1s. MASP-2 also showed very weak C3 cleaving activity. Recombinant MASP-1 had a lower and more restricted esterolytic activity. It showed marginal activity toward C2 and C3, and no activity on C4. The enzymic activity of both MASP-1 and MASP-2 was specifically titrated by C1 inhibitor, and abolished at a 1:1 C1 inhibitor:protease ratio. Taken together with previous findings, these and other data strongly support the hypothesis that MASP-2 is the protease that, in association with MBL, triggers complement activation via the MBL pathway, through combined self-activation and proteolytic properties devoted to C1r and C1s in the C1 complex. In view of the very low activity of MASP-1 on C3 and C2, our data raise questions about the implication of this protease in complement activation.",
keywords = "Base Sequence, Catalysis, Complement Activation, DNA Primers, Electrophoresis, Polyacrylamide Gel, Esters, Humans, Hydrolysis, Kinetics, Mannose-Binding Protein-Associated Serine Proteases, Recombinant Proteins, Serine Endopeptidases, Serine Proteinase Inhibitors, Substrate Specificity",
author = "V Rossi and S Cseh and I Bally and Thielens, {N M} and Jensenius, {Jens Christian} and Arlaud, {G J}",
year = "2001",
doi = "10.1074/jbc.M105934200",
language = "English",
volume = "276",
pages = "40880--7",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "44",

}

RIS

TY - JOUR

T1 - Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2

AU - Rossi, V

AU - Cseh, S

AU - Bally, I

AU - Thielens, N M

AU - Jensenius, Jens Christian

AU - Arlaud, G J

PY - 2001

Y1 - 2001

N2 - Mannan-binding lectin (MBL)-associated serine proteases-1 and 2 (MASP-1 and MASP-2) are homologous modular proteases that each interact with MBL, an oligomeric serum lectin involved in innate immunity. To precisely determine their substrate specificity, human MASP-1 and MASP-2, and fragments from their catalytic regions were expressed using a baculovirus/insect cells system. Recombinant MASP-2 displayed a rather wide, C1s-like esterolytic activity, and specifically cleaved complement proteins C2 and C4, with relative efficiencies 3- and 23-fold higher, respectively, than human C1s. MASP-2 also showed very weak C3 cleaving activity. Recombinant MASP-1 had a lower and more restricted esterolytic activity. It showed marginal activity toward C2 and C3, and no activity on C4. The enzymic activity of both MASP-1 and MASP-2 was specifically titrated by C1 inhibitor, and abolished at a 1:1 C1 inhibitor:protease ratio. Taken together with previous findings, these and other data strongly support the hypothesis that MASP-2 is the protease that, in association with MBL, triggers complement activation via the MBL pathway, through combined self-activation and proteolytic properties devoted to C1r and C1s in the C1 complex. In view of the very low activity of MASP-1 on C3 and C2, our data raise questions about the implication of this protease in complement activation.

AB - Mannan-binding lectin (MBL)-associated serine proteases-1 and 2 (MASP-1 and MASP-2) are homologous modular proteases that each interact with MBL, an oligomeric serum lectin involved in innate immunity. To precisely determine their substrate specificity, human MASP-1 and MASP-2, and fragments from their catalytic regions were expressed using a baculovirus/insect cells system. Recombinant MASP-2 displayed a rather wide, C1s-like esterolytic activity, and specifically cleaved complement proteins C2 and C4, with relative efficiencies 3- and 23-fold higher, respectively, than human C1s. MASP-2 also showed very weak C3 cleaving activity. Recombinant MASP-1 had a lower and more restricted esterolytic activity. It showed marginal activity toward C2 and C3, and no activity on C4. The enzymic activity of both MASP-1 and MASP-2 was specifically titrated by C1 inhibitor, and abolished at a 1:1 C1 inhibitor:protease ratio. Taken together with previous findings, these and other data strongly support the hypothesis that MASP-2 is the protease that, in association with MBL, triggers complement activation via the MBL pathway, through combined self-activation and proteolytic properties devoted to C1r and C1s in the C1 complex. In view of the very low activity of MASP-1 on C3 and C2, our data raise questions about the implication of this protease in complement activation.

KW - Base Sequence

KW - Catalysis

KW - Complement Activation

KW - DNA Primers

KW - Electrophoresis, Polyacrylamide Gel

KW - Esters

KW - Humans

KW - Hydrolysis

KW - Kinetics

KW - Mannose-Binding Protein-Associated Serine Proteases

KW - Recombinant Proteins

KW - Serine Endopeptidases

KW - Serine Proteinase Inhibitors

KW - Substrate Specificity

U2 - 10.1074/jbc.M105934200

DO - 10.1074/jbc.M105934200

M3 - Journal article

C2 - 11527969

VL - 276

SP - 40880

EP - 40887

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 44

ER -