A truncated form of mannose-binding lectin-associated serine protease (MASP)-2 expressed by alternative polyadenylation is a component of the lectin complement pathway [PDF]
International Immunology, 1999 The lectin complement pathway is initiated by binding of mannose-binding lectin (MBL) and MBL-associated serine protease (MASP) to carbohydrates. In the human lectin pathway, MASP-1 and MASP-2 are involved in the proteolysis of C4, C2 and C3. Here we report that the human MBL-MASP complex contains a new 22 kDa protein [small MBL-associated protein ...
M, Takahashi +3 more
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International Journal of General Medicine, 2023 Jiayi Li,1,2 Jiao Zhang,2 Xu Wang,2 Xumin Zheng,2 Hongmei Gao,2 Shimin Jiang,2 Wenge Li1,2 1Department of Nephrology, Peking University China-Japan Friendship School of Clinical Medicine, Beijing, People’s Republic of China; 2Department of ...
Li J +6 more
doaj
Ubiquitin and ubiquitin‐like modifications in the endoplasmic reticulum stress response
The FEBS Journal, EarlyView.Endoplasmic reticulum (ER) stress activates various proteostasis control processes, including the unfolded protein response, ribosome‐associated quality control, and ER‐associated degradation. Ubiquitin and ubiquitin‐like modifications dynamically regulate these processes to determine cell fate, promoting adaptation or inducing cell death.
Tony Avril +2 more
wiley +1 more source
Mannose‐binding Protein Recognizes Glioma Cells: In vitro Analysis of Complement Activation on Glioma Cells via the Lectin Pathway [PDF]
Japanese Journal of Cancer Research, 1995 The lectin pathway is a novel pathway for activation of the complement cascade, which is initiated by the binding of mannose‐binding protein (MBP) to its carbohydrate ligands. We investigated whether the complement system was activated in vitro by glioma cells through this pathway to the C3 level.
Fujita, Takashi +4 more
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Angewandte Chemie, Volume 138, Issue 28, 6 July 2026.We prepared five glycosylated liposomal nanoparticles (G‐LNPs) to investigate the role of glycosylation and protein corona in modulating the in vivo behavior of G‐LNPs. We show that IgG and complement C3 adsorption enhanced liposomal nanoparticle clearance, with IgG promoting subsequent C3 binding.
Yingjie Yu +18 more
wiley +2 more sources
A Novel Diagnostic Approach for Hepatocellular Carcinoma Using Glycosylated Ferritin
Hepatology Research, EarlyView.The percentage of glycosylated ferritin relative to total ferritin (%GF) is a novel biomarker for hepatocellular carcinoma (HCC), showing diagnostic performance comparable to that of AFP and DCP. We developed the GFAD index by integrating age, sex, %GF, AFP, and DCP, achieving improved diagnostic accuracy with high sensitivity and specificity. ABSTRACT
Akiyo Ishiguro +11 more
wiley +1 more source
Lectin Pathway of Bony Fish Complement: Identification of Two Homologs of the Mannose-Binding Lectin Associated with MASP2 in the Common Carp ( Cyprinus carpio ) [PDF]
The Journal of Immunology, 2006 Abstract The lectin pathway of complement is considered to be the most ancient complement pathway as inferred from identification of ancient homologs of mannose-binding lectin (MBL) and MBL-associated serine proteases (MASPs) in some invertebrates.
Miki, Nakao +8 more
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Mannose-Binding Lectin Inhibits the Motility of Pathogenic Salmonella by Affecting the Driving Forces of Motility and the Chemotactic Response. [PDF]
PLoS ONE, 2016 Mannose-binding lectin (MBL) is a key pattern recognition molecule in the lectin pathway of the complement system, an important component of innate immunity.
Jun Xu +8 more
doaj +1 more source
PlantRG: A Comprehensive and User‐Friendly Database for Plant Resistance Gene Analogs (RGAs)
Plant Biotechnology Journal, EarlyView.ABSTRACT Resistance genes are critical for plant defence against biotic stresses, and building a comprehensive, integrated data resource platform for these genes holds great significance for plant research and agriculture. Here, we developed PlantRG (http://plantrg.bio2db.com), a user‐friendly plant resistance gene database, which is built on 2 163 397
Jinghua He +9 more
wiley +1 more source
Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases and Activate Complement through the Lectin Pathway [PDF]
Journal of Biomedicine and Biotechnology, 2012 Ficolins are thought to be pathogen-associated-molecular-pattern-(PAMP-) recognition molecules that function to support innate immunity. Like mannose-binding lectins (MBLs), most mammalian ficolins form complexes with MBL-associated serine proteases (MASPs), leading to complement activationviathe lectin pathway. However, the ability of murine ficolin B,
Yuichi Endo +5 more
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