Complement pathway, mannose-binding lectin

Results 81 to 90 of about 23,299 (223)

Membrane array and multiplex bead analysis of tear cytokines in systemic sclerosis [PDF]

, 2016
Although serious ocular manifestations of systemicsclerosis (SSc) have been described, tear analysis ofpatients with SSc has not been performed in previousstudies.
Hársfalvi, Jolán +6 more
core +1 more source

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, Y, Endo, T, Fujita, M, Matsushita +3 more
openaire +2 more sources

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
openaire +2 more sources

Endoplasmic Reticulum Export of GPI-Anchored Proteins [PDF]

, 2019
Protein export from the endoplasmic reticulum (ER) is an essential process in all eukaryotes driven by the cytosolic coat complex COPII, which forms vesicles at ER exit sites for transport of correctly assembled secretory cargo to the Golgi apparatus ...
López Martín, Sergio +3 more
core +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
openaire +2 more sources

Higher Complement C4 Gene Copy Number Constitutes a Shared Genetic Risk Factor for Giant Cell Arteritis and IgA Vasculitis

Arthritis &Rheumatology, EarlyView.
Objective Low copy number (CN) of complement C4 isoforms and high CN of retroviral HERV‐K elements are known risk factors for many immune‐mediated inflammatory diseases (IMIDs), often showing sex‐biased effects. Here, we assessed whether CN variation within the C4 gene contributes to giant cell arteritis (GCA) and IgA vasculitis (IgAV), two complex ...
Laura Martínez‐Gutiérrez +295 more
wiley +1 more source

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

Influence of functional deficiency of complement mannose-binding lectin on outcome of patients with acute ST-elevation myocardial infarction undergoing primary percutaneous coronary intervention [PDF]

, 2017
Aims Experimental data point towards a favourable effect of low serum concentrations of complement mannose-binding lectin (MBL) on myocardial ischaemia/reperfusion (I/R) injury.
Armstrong, Paul +5 more
core

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
openaire +2 more sources

Quantifying Protein–Glycan Interactions Using Native Mass Spectrometry

Mass Spectrometry Reviews, EarlyView.
ABSTRACT Interactions between glycan‐binding proteins (GBPs) and carbohydrates (glycans) are essential to many biological processes relevant to human health and disease. For most GBPs, however, their glycan interactome—the repertoire of glycans recognized and their specificities—is poorly defined.
Duong T. Bui +4 more
wiley +1 more source

lectin pathway
complement
medicine

mbl
complement system
mannose-binding lectin

immunologic diseases
classical pathway
alternative pathway