نتایج جستجو برای: associated serine protease masp

تعداد نتایج: 1584019  

2016
Mo-fei Li Jun Li Li Sun

In teleost fish, the immune functions of mannan-binding lectin (MBL) associated protein (MAP) and MBL associated serine protease (MASP) are scarcely investigated. In the present study, we examined the biological properties both MAP (CsMAP34) and MASP (CsMASP1) molecules from tongue sole (Cynoglossus semilaevis). We found that CsMAP34 and CsMASP1 expressions occurred in nine different tissues an...

Journal: :The Journal of biological chemistry 2007
Russell Wallis Alister W Dodds Daniel A Mitchell Robert B Sim Kenneth B M Reid Wilhelm J Schwaeble

Activation of component C3 is central to the pathways of complement and leads directly to neutralization of pathogens and stimulation of adaptive immune responses. The convertases that catalyze this reaction assemble from fragments of complement components via multistep reactions. In the lectin pathway, mannose-binding lectin (MBL) and ficolins bind to pathogens and activate MBL-associated seri...

2016
Hye-Jung Kim Seong Joon Ahn Se Joon Woo Hye Kyoung Hong Eui Jin Suh Jeeyun Ahn Ji Hyun Park Na-Kyung Ryoo Ji Eun Lee Ki Woong Kim Kyu Hyung Park Cheolju Lee

Age-related macular degeneration (AMD) is a major cause of severe, progressive visual loss among the elderly. There are currently no established serological markers for the diagnosis of AMD. In this study, we carried out a large-scale quantitative proteomics analysis to identify plasma proteins that could serve as potential AMD biomarkers. We found that the plasma levels of phospholipid transfe...

Journal: :Journal of immunology 2005
Nicholas J Lynch Saeed-ul-Hassan Khan Cordula M Stover Sara M Sandrini Denise Marston Julia S Presanis Wilhelm J Schwaeble

The lectin pathway of complement is activated by multimolecular complexes that recognize and bind to microbial polysaccharides. These complexes comprise a multimeric carbohydrate recognition subunit (either mannan-binding lectin (MBL) or a ficolin), three MBL-associated serine proteases (MASP-1, -2, and -3), and MAp19 (a truncated product of the MASP-2 gene). In this study we report the cloning...

Journal: :Journal of immunology 2003
Yuichi Endo Masaru Nonaka Hidetoshi Saiga Yuji Kakinuma Akiko Matsushita Minoru Takahashi Misao Matsushita Teizo Fujita

Mannose-binding lectin-associated serine proteases (MASPs) are involved in complement activation through the lectin pathway. To elucidate the phylogenetic origin of MASP and a primordial complement system, we cloned two MASP cDNAs from amphioxus (Branchiostoma belcheri) of the cephalochordates, considered to be the closest relative of vertebrates. The two sequences, orthologues of mammalian MAS...

Journal: :The Journal of clinical investigation 2006
Barbro Selander Ulla Mårtensson Andrej Weintraub Eva Holmström Misao Matsushita Steffen Thiel Jens C Jensenius Lennart Truedsson Anders G Sjöholm

Lectin pathway activation of C3 is known to involve target recognition by mannan-binding lectin (MBL) or ficolins and generation of classical pathway C3 convertase via cleavage of C4 and C2 by MBL-associated serine protease 2 (MASP-2). We investigated C3 activation in C2-deficient human sera and in sera with other defined defects of complement to assess other mechanisms through which MBL might ...

2014
Péter K. Jani Erika Kajdácsi Márton Megyeri József Dobó Zoltán Doleschall Krisztina Futosi Csaba I. Tímár Attila Mócsai Veronika Makó Péter Gál László Cervenak

Microbial infection urges prompt intervention by the immune system. The complement cascade and neutrophil granulocytes are the predominant contributors to this immediate anti-microbial action. We have previously shown that mannan-binding lectin-associated serine protease-1 (MASP-1), the most abundant enzyme of the complement lectin pathway, can induce p38-MAPK activation, NFkappaB signaling, an...

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