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Jens Christian Jensenius

On the site of C4 deposition upon complement activation via the mannan-binding lectin pathway or the classical pathway

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On the site of C4 deposition upon complement activation via the mannan-binding lectin pathway or the classical pathway. / Møller-Kristensen, M; Thiel, S; Hansen, A G; Jensenius, Jens Christian.

In: Scandinavian Journal of Immunology, Vol. 57, No. 6, 2003, p. 556-61.

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

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Møller-Kristensen, M et al. "On the site of C4 deposition upon complement activation via the mannan-binding lectin pathway or the classical pathway". Scandinavian Journal of Immunology. 2003, 57(6). 556-61.

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@article{987bc9b1ff7b4c63b8563959b5589aa8,
title = "On the site of C4 deposition upon complement activation via the mannan-binding lectin pathway or the classical pathway",
abstract = "The mannan-binding lectin (MBL) pathway and the classical pathway of complement activation are initiated by the binding of the recognition structure of the initiator complexes, MBL and C1q, respectively, to their ligands, i.e. carbohydrate structures or immune complexes. Proenzymes associated with MBL or C1q are then activated and generate C3 convertase through the activation of C4 and C2. The cleavage product of C4, C4b, attaches covalently to nearby hydroxyl or amino groups. The current picture is that C2 must then attach to C4b before being cleaved by the same associated proteases into the enzymatically active fragment, C2b. This suggests a stringent requirement for the deposition of C4b very close to the initiator complex, or indeed onto the initiator complex. We examined the possibility of C4b being bound to the initiator complex by a solid-phase assay, allowing for the selective elution of the initiator complexes, followed by quantification of the C4b being eluted and the C4b remaining on the solid phase. Also, we estimated the generation of complexes between the released initiator complex and C4b. More than 99% of deposited C4b was bound directly to the solid phase rather than to the initiator complex. Our approach cannot answer the question of the whereabouts of the C2 when it is cleaved.",
keywords = "Binding Sites, Complement Activation, Complement C3-C5 Convertases, Complement C4, Complement Pathway, Classical, Complement Pathway, Mannose-Binding Lectin, Humans, Macromolecular Substances, Models, Immunological",
author = "M M{\o}ller-Kristensen and S Thiel and Hansen, {A G} and Jensenius, {Jens Christian}",
year = "2003",
language = "English",
volume = "57",
pages = "556--61",
journal = "Scandinavian Journal of Immunology",
issn = "0300-9475",
publisher = "Wiley-Blackwell Publishing Ltd.",
number = "6",

}

RIS

TY - JOUR

T1 - On the site of C4 deposition upon complement activation via the mannan-binding lectin pathway or the classical pathway

AU - Møller-Kristensen, M

AU - Thiel, S

AU - Hansen, A G

AU - Jensenius, Jens Christian

PY - 2003

Y1 - 2003

N2 - The mannan-binding lectin (MBL) pathway and the classical pathway of complement activation are initiated by the binding of the recognition structure of the initiator complexes, MBL and C1q, respectively, to their ligands, i.e. carbohydrate structures or immune complexes. Proenzymes associated with MBL or C1q are then activated and generate C3 convertase through the activation of C4 and C2. The cleavage product of C4, C4b, attaches covalently to nearby hydroxyl or amino groups. The current picture is that C2 must then attach to C4b before being cleaved by the same associated proteases into the enzymatically active fragment, C2b. This suggests a stringent requirement for the deposition of C4b very close to the initiator complex, or indeed onto the initiator complex. We examined the possibility of C4b being bound to the initiator complex by a solid-phase assay, allowing for the selective elution of the initiator complexes, followed by quantification of the C4b being eluted and the C4b remaining on the solid phase. Also, we estimated the generation of complexes between the released initiator complex and C4b. More than 99% of deposited C4b was bound directly to the solid phase rather than to the initiator complex. Our approach cannot answer the question of the whereabouts of the C2 when it is cleaved.

AB - The mannan-binding lectin (MBL) pathway and the classical pathway of complement activation are initiated by the binding of the recognition structure of the initiator complexes, MBL and C1q, respectively, to their ligands, i.e. carbohydrate structures or immune complexes. Proenzymes associated with MBL or C1q are then activated and generate C3 convertase through the activation of C4 and C2. The cleavage product of C4, C4b, attaches covalently to nearby hydroxyl or amino groups. The current picture is that C2 must then attach to C4b before being cleaved by the same associated proteases into the enzymatically active fragment, C2b. This suggests a stringent requirement for the deposition of C4b very close to the initiator complex, or indeed onto the initiator complex. We examined the possibility of C4b being bound to the initiator complex by a solid-phase assay, allowing for the selective elution of the initiator complexes, followed by quantification of the C4b being eluted and the C4b remaining on the solid phase. Also, we estimated the generation of complexes between the released initiator complex and C4b. More than 99% of deposited C4b was bound directly to the solid phase rather than to the initiator complex. Our approach cannot answer the question of the whereabouts of the C2 when it is cleaved.

KW - Binding Sites

KW - Complement Activation

KW - Complement C3-C5 Convertases

KW - Complement C4

KW - Complement Pathway, Classical

KW - Complement Pathway, Mannose-Binding Lectin

KW - Humans

KW - Macromolecular Substances

KW - Models, Immunological

M3 - Journal article

C2 - 12791093

VL - 57

SP - 556

EP - 561

JO - Scandinavian Journal of Immunology

JF - Scandinavian Journal of Immunology

SN - 0300-9475

IS - 6

ER -