dc.contributor.author |
Megyeri, Márton |
|
dc.contributor.author |
Jani, Péter Károly |
|
dc.contributor.author |
Kajdácsi, Erika |
|
dc.contributor.author |
Dobó, József |
|
dc.contributor.author |
Schwaner E |
|
dc.contributor.author |
Major, Balázs |
|
dc.contributor.author |
Rigó, János |
|
dc.contributor.author |
Závodszky, Péter |
|
dc.contributor.author |
Thiel S |
|
dc.contributor.author |
Cervenak, László |
|
dc.contributor.author |
Gál, Péter |
|
dc.date.accessioned |
2015-09-08T12:28:34Z |
|
dc.date.available |
2015-09-08T12:28:34Z |
|
dc.date.issued |
2014 |
|
dc.identifier |
84892841357 |
|
dc.identifier.citation |
pagination=39-45;
journalVolume=59;
journalIssueNumber=1;
journalTitle=MOLECULAR IMMUNOLOGY; |
|
dc.identifier.uri |
http://repo.lib.semmelweis.hu//handle/123456789/2086 |
|
dc.identifier.uri |
doi:10.1016/j.molimm.2014.01.001 |
|
dc.description.abstract |
The complement system plays an important role in the induction of inflammation. In this study we demonstrate that the initiation complexes of the lectin pathway, consisting of mannose-binding lectin (MBL) and associated serine proteases (MASPs) elicit Ca2+ signaling in cultured endothelial cells (HUVECs). This is in agreement with our previous results showing that the recombinant catalytic fragment of MASP-1 activates endothelial cells by cleaving protease activated receptor 4. Two other proteases, MASP-2 and MASP-3 are also associated with MBL. Earlier we showed that recombinant catalytic fragment of MASP-2 cannot activate HUVECs, and in this study we demonstrate that the same fragment of MASP-3 has also no effect. We find the same to be the case if we use recombinant forms of the N-terminal parts of MASP-1 and MASP-2 which only contain non-enzymatic domains. Moreover, stable zymogen mutant form of MASP-1 was also ineffective to stimulate endothelial cells, which suggests that in vivo MASP-1 have the ability to activate endothelial cells directly as well as to activate the lectin pathway simultaneously. We show that among the components of the MBL-MASPs complexes only MASP-1 is able to trigger response in HUVECs and the proteolytic activity of MASP-1 is essential. Our results strengthen the view that MASP-1 plays a central role in the early innate immune response. |
|
dc.relation.ispartof |
urn:issn:0161-5890 |
|
dc.title |
Serum MASP-1 in complex with MBL activates endothelial cells. |
|
dc.type |
Journal Article |
|
dc.date.updated |
2015-07-28T12:31:56Z |
|
dc.language.rfc3066 |
en |
|
dc.identifier.mtmt |
2523886 |
|
dc.identifier.wos |
000334089000005 |
|
dc.identifier.pubmed |
24472859 |
|
dc.contributor.department |
SE/AOK/K/I. Sz. Szülészeti és Nőgyógyászati Klinika |
|
dc.contributor.department |
SE/AOK/K/III. Sz. Belgyógyászati Klinika |
|
dc.contributor.institution |
Semmelweis Egyetem |
|