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Jens Christian Jensenius

A second serine protease associated with mannan-binding lectin that activates complement

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A second serine protease associated with mannan-binding lectin that activates complement. / Thiel, S; Vorup-Jensen, T; Stover, C M; Schwaeble, W; Laursen, Simon; Poulsen, K; Willis, A C; Eggleton, P; Hansen, S; Holmskov, Uffe Laurits; Reid, K B; Jensenius, Jens Christian.

In: Nature, Vol. 386, No. 6624, 1997, p. 506-10.

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

Harvard

Thiel, S, Vorup-Jensen, T, Stover, CM, Schwaeble, W, Laursen, S, Poulsen, K, Willis, AC, Eggleton, P, Hansen, S, Holmskov, UL, Reid, KB & Jensenius, JC 1997, 'A second serine protease associated with mannan-binding lectin that activates complement', Nature, vol. 386, no. 6624, pp. 506-10. https://doi.org/10.1038/386506a0

APA

CBE

Thiel S, Vorup-Jensen T, Stover CM, Schwaeble W, Laursen S, Poulsen K, Willis AC, Eggleton P, Hansen S, Holmskov UL, Reid KB, Jensenius JC. 1997. A second serine protease associated with mannan-binding lectin that activates complement. Nature. 386(6624):506-10. https://doi.org/10.1038/386506a0

MLA

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Author

Thiel, S ; Vorup-Jensen, T ; Stover, C M ; Schwaeble, W ; Laursen, Simon ; Poulsen, K ; Willis, A C ; Eggleton, P ; Hansen, S ; Holmskov, Uffe Laurits ; Reid, K B ; Jensenius, Jens Christian. / A second serine protease associated with mannan-binding lectin that activates complement. In: Nature. 1997 ; Vol. 386, No. 6624. pp. 506-10.

Bibtex

@article{872ed8ec4f3746dcb7979c299a3d6e13,
title = "A second serine protease associated with mannan-binding lectin that activates complement",
abstract = "The complement system comprises a complex array of enzymes and non-enzymatic proteins that is essential for the operation of the innate as well as the adaptive immune defence. The complement system can be activated in three ways: by the classical pathway which is initiated by antibody-antigen complexes, by the alternative pathway initiated by certain structures on microbial surfaces, and by an antibody-independent pathway that is initiated by the binding of mannan-binding lectin (MBL; first described as mannan-binding protein) to carbohydrates. MBL is structurally related to the complement C1 subcomponent, C1q, and seems to activate the complement system through an associated serine protease known as MASP (ref. 4) or p100 (ref. 5), which is similar to C1r and C1s of the classical pathway. MBL binds to specific carbohydrate structures found on the surface of a range of microorganisms, including bacteria, yeasts, parasitic protozoa and viruses, and exhibits antibacterial activity through killing mediated by the terminal, lytic complement components or by promoting phagocytosis. The level of MBL in plasma is genetically determined, and deficiency is associated with frequent infections in childhood, and possibly also in adults (for review, see ref. 6). We have now identified a new MBL-associated serine protease (MASP-2) which shows a striking homology with the previously reported MASP (MASP-1) and the two C1q-associated serine proteases C1r and C1s. Thus complement activation through MBL, like the classical pathway, involves two serine proteases and may antedate the development of the specific immune system of vertebrates.",
keywords = "Amino Acid Sequence, Carrier Proteins, Cloning, Molecular, Collectins, Complement Activation, Complement C4, Humans, Lectins, Liver, Mannose-Binding Protein-Associated Serine Proteases, Molecular Sequence Data, Polymerase Chain Reaction, Sequence Homology, Amino Acid, Serine Endopeptidases",
author = "S Thiel and T Vorup-Jensen and Stover, {C M} and W Schwaeble and Simon Laursen and K Poulsen and Willis, {A C} and P Eggleton and S Hansen and Holmskov, {Uffe Laurits} and Reid, {K B} and Jensenius, {Jens Christian}",
year = "1997",
doi = "10.1038/386506a0",
language = "English",
volume = "386",
pages = "506--10",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6624",

}

RIS

TY - JOUR

T1 - A second serine protease associated with mannan-binding lectin that activates complement

AU - Thiel, S

AU - Vorup-Jensen, T

AU - Stover, C M

AU - Schwaeble, W

AU - Laursen, Simon

AU - Poulsen, K

AU - Willis, A C

AU - Eggleton, P

AU - Hansen, S

AU - Holmskov, Uffe Laurits

AU - Reid, K B

AU - Jensenius, Jens Christian

PY - 1997

Y1 - 1997

N2 - The complement system comprises a complex array of enzymes and non-enzymatic proteins that is essential for the operation of the innate as well as the adaptive immune defence. The complement system can be activated in three ways: by the classical pathway which is initiated by antibody-antigen complexes, by the alternative pathway initiated by certain structures on microbial surfaces, and by an antibody-independent pathway that is initiated by the binding of mannan-binding lectin (MBL; first described as mannan-binding protein) to carbohydrates. MBL is structurally related to the complement C1 subcomponent, C1q, and seems to activate the complement system through an associated serine protease known as MASP (ref. 4) or p100 (ref. 5), which is similar to C1r and C1s of the classical pathway. MBL binds to specific carbohydrate structures found on the surface of a range of microorganisms, including bacteria, yeasts, parasitic protozoa and viruses, and exhibits antibacterial activity through killing mediated by the terminal, lytic complement components or by promoting phagocytosis. The level of MBL in plasma is genetically determined, and deficiency is associated with frequent infections in childhood, and possibly also in adults (for review, see ref. 6). We have now identified a new MBL-associated serine protease (MASP-2) which shows a striking homology with the previously reported MASP (MASP-1) and the two C1q-associated serine proteases C1r and C1s. Thus complement activation through MBL, like the classical pathway, involves two serine proteases and may antedate the development of the specific immune system of vertebrates.

AB - The complement system comprises a complex array of enzymes and non-enzymatic proteins that is essential for the operation of the innate as well as the adaptive immune defence. The complement system can be activated in three ways: by the classical pathway which is initiated by antibody-antigen complexes, by the alternative pathway initiated by certain structures on microbial surfaces, and by an antibody-independent pathway that is initiated by the binding of mannan-binding lectin (MBL; first described as mannan-binding protein) to carbohydrates. MBL is structurally related to the complement C1 subcomponent, C1q, and seems to activate the complement system through an associated serine protease known as MASP (ref. 4) or p100 (ref. 5), which is similar to C1r and C1s of the classical pathway. MBL binds to specific carbohydrate structures found on the surface of a range of microorganisms, including bacteria, yeasts, parasitic protozoa and viruses, and exhibits antibacterial activity through killing mediated by the terminal, lytic complement components or by promoting phagocytosis. The level of MBL in plasma is genetically determined, and deficiency is associated with frequent infections in childhood, and possibly also in adults (for review, see ref. 6). We have now identified a new MBL-associated serine protease (MASP-2) which shows a striking homology with the previously reported MASP (MASP-1) and the two C1q-associated serine proteases C1r and C1s. Thus complement activation through MBL, like the classical pathway, involves two serine proteases and may antedate the development of the specific immune system of vertebrates.

KW - Amino Acid Sequence

KW - Carrier Proteins

KW - Cloning, Molecular

KW - Collectins

KW - Complement Activation

KW - Complement C4

KW - Humans

KW - Lectins

KW - Liver

KW - Mannose-Binding Protein-Associated Serine Proteases

KW - Molecular Sequence Data

KW - Polymerase Chain Reaction

KW - Sequence Homology, Amino Acid

KW - Serine Endopeptidases

U2 - 10.1038/386506a0

DO - 10.1038/386506a0

M3 - Journal article

C2 - 9087411

VL - 386

SP - 506

EP - 510

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6624

ER -