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Jens Christian Jensenius

MAp19, the alternative splice product of the MASP2 gene

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Standard

MAp19, the alternative splice product of the MASP2 gene. / Degn, Søren Egedal; Thiel, Steffen; Nielsen, Ole et al.
I: Journal of Immunological Methods, Bind 373, Nr. 1-2, 2011, s. 89-101.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

Harvard

Degn, SE, Thiel, S, Nielsen, O, Hansen, AG, Steffensen, R & Jensenius, JC 2011, 'MAp19, the alternative splice product of the MASP2 gene', Journal of Immunological Methods, bind 373, nr. 1-2, s. 89-101. https://doi.org/10.1016/j.jim.2011.08.006

APA

Degn, S. E., Thiel, S., Nielsen, O., Hansen, A. G., Steffensen, R., & Jensenius, J. C. (2011). MAp19, the alternative splice product of the MASP2 gene. Journal of Immunological Methods, 373(1-2), 89-101. https://doi.org/10.1016/j.jim.2011.08.006

CBE

Degn SE, Thiel S, Nielsen O, Hansen AG, Steffensen R, Jensenius JC. 2011. MAp19, the alternative splice product of the MASP2 gene. Journal of Immunological Methods. 373(1-2):89-101. https://doi.org/10.1016/j.jim.2011.08.006

MLA

Degn, Søren Egedal et al. "MAp19, the alternative splice product of the MASP2 gene". Journal of Immunological Methods. 2011, 373(1-2). 89-101. https://doi.org/10.1016/j.jim.2011.08.006

Vancouver

Degn SE, Thiel S, Nielsen O, Hansen AG, Steffensen R, Jensenius JC. MAp19, the alternative splice product of the MASP2 gene. Journal of Immunological Methods. 2011;373(1-2):89-101. doi: 10.1016/j.jim.2011.08.006

Author

Degn, Søren Egedal ; Thiel, Steffen ; Nielsen, Ole et al. / MAp19, the alternative splice product of the MASP2 gene. I: Journal of Immunological Methods. 2011 ; Bind 373, Nr. 1-2. s. 89-101.

Bibtex

@article{24b21042a58542e482606ccd06ee2f58,
title = "MAp19, the alternative splice product of the MASP2 gene",
abstract = "The lectin pathway of complement is a central part of innate immunity, but as a powerful inducer of inflammation it needs to be tightly controlled. The MASP2 gene encodes two proteins, MASP-2 and MAp19. MASP-2 is the serine protease responsible for lectin pathway activation. The smaller alternative splice product, MAp19, lacks a catalytic domain but retains two of three domains involved in association with the pattern-recognition molecules (PRMs): mannan-binding lectin (MBL), H-ficolin, L-ficolin and M-ficolin. MAp19 reportedly acts as a competitive inhibitor of MASP-2-mediated complement activation. In light of a ten times lower affinity of MAp19, versus MASP-2, for association with the PRMs, much higher serum concentrations of MAp19 than MASP-2 would be required for MAp19 to exert such an inhibitory activity. Just four amino acid residues distinguish MAp19 from MASP-2, and these are conserved between man, mouse and rat. Nonetheless we generated monoclonal rat anti-MAp19 antibodies and established a quantitative assay. We found the concentration of MAp19 in serum to be 217 ng/ml, i.e., 11nM, comparable to the 7 nM of MASP-2. In serum all MASP-2, but only a minor fraction of MAp19, was associated with PRMs. In contrast to previous reports we found that MAp19 could not compete with MASP-2 for binding to MBL, nor could it inhibit MASP-2-mediated complement activation. Immunohistochemical analyses combined with qRT-PCR revealed that both MAp19 and MASP-2 were mainly expressed in hepatocytes. High levels of MAp19 were found in urine, where MASP-2 was absent.",
keywords = "Alternative Splicing, Animals, Antibodies, Monoclonal, Antibody Affinity, Blotting, Western, Cytoplasm, Gene Expression Profiling, HEK293 Cells, Hepatocytes, Humans, Hybridomas, Immunohistochemistry, Kidney, Lectins, Macrophages, Alveolar, Mannose-Binding Lectin, Mannose-Binding Protein-Associated Serine Proteases, Mice, Protein Binding, Protein Isoforms, Rats, Reverse Transcriptase Polymerase Chain Reaction",
author = "Degn, {S{\o}ren Egedal} and Steffen Thiel and Ole Nielsen and Hansen, {Annette G} and Rudi Steffensen and Jensenius, {Jens C}",
note = "Copyright {\textcopyright} 2011 Elsevier B.V. All rights reserved.",
year = "2011",
doi = "10.1016/j.jim.2011.08.006",
language = "English",
volume = "373",
pages = "89--101",
journal = "Journal of Immunological Methods",
issn = "0022-1759",
publisher = "Elsevier BV",
number = "1-2",

}

RIS

TY - JOUR

T1 - MAp19, the alternative splice product of the MASP2 gene

AU - Degn, Søren Egedal

AU - Thiel, Steffen

AU - Nielsen, Ole

AU - Hansen, Annette G

AU - Steffensen, Rudi

AU - Jensenius, Jens C

N1 - Copyright © 2011 Elsevier B.V. All rights reserved.

PY - 2011

Y1 - 2011

N2 - The lectin pathway of complement is a central part of innate immunity, but as a powerful inducer of inflammation it needs to be tightly controlled. The MASP2 gene encodes two proteins, MASP-2 and MAp19. MASP-2 is the serine protease responsible for lectin pathway activation. The smaller alternative splice product, MAp19, lacks a catalytic domain but retains two of three domains involved in association with the pattern-recognition molecules (PRMs): mannan-binding lectin (MBL), H-ficolin, L-ficolin and M-ficolin. MAp19 reportedly acts as a competitive inhibitor of MASP-2-mediated complement activation. In light of a ten times lower affinity of MAp19, versus MASP-2, for association with the PRMs, much higher serum concentrations of MAp19 than MASP-2 would be required for MAp19 to exert such an inhibitory activity. Just four amino acid residues distinguish MAp19 from MASP-2, and these are conserved between man, mouse and rat. Nonetheless we generated monoclonal rat anti-MAp19 antibodies and established a quantitative assay. We found the concentration of MAp19 in serum to be 217 ng/ml, i.e., 11nM, comparable to the 7 nM of MASP-2. In serum all MASP-2, but only a minor fraction of MAp19, was associated with PRMs. In contrast to previous reports we found that MAp19 could not compete with MASP-2 for binding to MBL, nor could it inhibit MASP-2-mediated complement activation. Immunohistochemical analyses combined with qRT-PCR revealed that both MAp19 and MASP-2 were mainly expressed in hepatocytes. High levels of MAp19 were found in urine, where MASP-2 was absent.

AB - The lectin pathway of complement is a central part of innate immunity, but as a powerful inducer of inflammation it needs to be tightly controlled. The MASP2 gene encodes two proteins, MASP-2 and MAp19. MASP-2 is the serine protease responsible for lectin pathway activation. The smaller alternative splice product, MAp19, lacks a catalytic domain but retains two of three domains involved in association with the pattern-recognition molecules (PRMs): mannan-binding lectin (MBL), H-ficolin, L-ficolin and M-ficolin. MAp19 reportedly acts as a competitive inhibitor of MASP-2-mediated complement activation. In light of a ten times lower affinity of MAp19, versus MASP-2, for association with the PRMs, much higher serum concentrations of MAp19 than MASP-2 would be required for MAp19 to exert such an inhibitory activity. Just four amino acid residues distinguish MAp19 from MASP-2, and these are conserved between man, mouse and rat. Nonetheless we generated monoclonal rat anti-MAp19 antibodies and established a quantitative assay. We found the concentration of MAp19 in serum to be 217 ng/ml, i.e., 11nM, comparable to the 7 nM of MASP-2. In serum all MASP-2, but only a minor fraction of MAp19, was associated with PRMs. In contrast to previous reports we found that MAp19 could not compete with MASP-2 for binding to MBL, nor could it inhibit MASP-2-mediated complement activation. Immunohistochemical analyses combined with qRT-PCR revealed that both MAp19 and MASP-2 were mainly expressed in hepatocytes. High levels of MAp19 were found in urine, where MASP-2 was absent.

KW - Alternative Splicing

KW - Animals

KW - Antibodies, Monoclonal

KW - Antibody Affinity

KW - Blotting, Western

KW - Cytoplasm

KW - Gene Expression Profiling

KW - HEK293 Cells

KW - Hepatocytes

KW - Humans

KW - Hybridomas

KW - Immunohistochemistry

KW - Kidney

KW - Lectins

KW - Macrophages, Alveolar

KW - Mannose-Binding Lectin

KW - Mannose-Binding Protein-Associated Serine Proteases

KW - Mice

KW - Protein Binding

KW - Protein Isoforms

KW - Rats

KW - Reverse Transcriptase Polymerase Chain Reaction

U2 - 10.1016/j.jim.2011.08.006

DO - 10.1016/j.jim.2011.08.006

M3 - Journal article

C2 - 21871896

VL - 373

SP - 89

EP - 101

JO - Journal of Immunological Methods

JF - Journal of Immunological Methods

SN - 0022-1759

IS - 1-2

ER -