Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway
(2007) In International Immunology 19(2). p.141-149- Abstract
- The complement system is an important part of the innate immune system. Three pathways, the classical, the alternative and the lectin pathway, lead to the cleavage of complement factor C3, a central event in the activation of the complement system. We investigated the deposition of C3b (solid-phase C3 activation product) on a mannan-coated surface at high concentration of human serum (17%). At these conditions, mannan-binding lectin (MBL) promoted the activation of C3 through the combined action of MBL-associated serine protease (MASP)-1 and MASP-2 without appreciable involvement of the alternative pathway. In serum depleted of MASP-1, MASP-2 and MASP-3, we observed synergetic effect of reconstitution with MASP-1 and MASP-2. This was... (More)
- The complement system is an important part of the innate immune system. Three pathways, the classical, the alternative and the lectin pathway, lead to the cleavage of complement factor C3, a central event in the activation of the complement system. We investigated the deposition of C3b (solid-phase C3 activation product) on a mannan-coated surface at high concentration of human serum (17%). At these conditions, mannan-binding lectin (MBL) promoted the activation of C3 through the combined action of MBL-associated serine protease (MASP)-1 and MASP-2 without appreciable involvement of the alternative pathway. In serum depleted of MASP-1, MASP-2 and MASP-3, we observed synergetic effect of reconstitution with MASP-1 and MASP-2. This was inhibited by MASP-3. No C3b deposition was observed with C2- or C4-depleted serum. Depletion of factor B had no effect on the MBL-MASP-promoted C3b deposition. Our results demonstrate a function of the orphan protease MASP-1 by providing evidence that this enzyme collaborates with MASP-2 in the generation of C3 convertase, a process observable at high serum concentration, but not at low serum concentration. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/676276
- author
- Moller-Kristensen, Mette ; Thiel, Steffen ; Sjöholm, Anders LU ; Matsushita, Misao and Jensenius, Jens C.
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- complement, lectin pathway, C3 activation, mannan-binding lectin
- in
- International Immunology
- volume
- 19
- issue
- 2
- pages
- 141 - 149
- publisher
- Oxford University Press
- external identifiers
-
- wos:000243805900004
- scopus:33846618236
- ISSN
- 1460-2377
- DOI
- 10.1093/intimm/dxl131
- language
- English
- LU publication?
- yes
- id
- 8f827532-4e8c-4bc5-818f-c24556f1195e (old id 676276)
- date added to LUP
- 2016-04-01 11:41:49
- date last changed
- 2022-01-26 08:55:59
@article{8f827532-4e8c-4bc5-818f-c24556f1195e,
abstract = {{The complement system is an important part of the innate immune system. Three pathways, the classical, the alternative and the lectin pathway, lead to the cleavage of complement factor C3, a central event in the activation of the complement system. We investigated the deposition of C3b (solid-phase C3 activation product) on a mannan-coated surface at high concentration of human serum (17%). At these conditions, mannan-binding lectin (MBL) promoted the activation of C3 through the combined action of MBL-associated serine protease (MASP)-1 and MASP-2 without appreciable involvement of the alternative pathway. In serum depleted of MASP-1, MASP-2 and MASP-3, we observed synergetic effect of reconstitution with MASP-1 and MASP-2. This was inhibited by MASP-3. No C3b deposition was observed with C2- or C4-depleted serum. Depletion of factor B had no effect on the MBL-MASP-promoted C3b deposition. Our results demonstrate a function of the orphan protease MASP-1 by providing evidence that this enzyme collaborates with MASP-2 in the generation of C3 convertase, a process observable at high serum concentration, but not at low serum concentration.}},
author = {{Moller-Kristensen, Mette and Thiel, Steffen and Sjöholm, Anders and Matsushita, Misao and Jensenius, Jens C.}},
issn = {{1460-2377}},
keywords = {{complement; lectin pathway; C3 activation; mannan-binding lectin}},
language = {{eng}},
number = {{2}},
pages = {{141--149}},
publisher = {{Oxford University Press}},
series = {{International Immunology}},
title = {{Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway}},
url = {{http://dx.doi.org/10.1093/intimm/dxl131}},
doi = {{10.1093/intimm/dxl131}},
volume = {{19}},
year = {{2007}},
}