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A Novel Diagnostic Approach for Hepatocellular Carcinoma Using Glycosylated Ferritin
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
Glomerular plasmalemma vesicle‐associated protein‐1 (PV‐1/PLVAP) identifies dynamic endothelial remodelling in chronic active antibody‐mediated rejection (caABMR), complementing glomerular C4d, which reflects a static footprint of complement activation. Combined assessment of PV‐1 and C4d captures complementary dimensions of microvascular pathology and
Yuto Igarashi +7 more
wiley +1 more source
TB serum selectively disrupts monocyte‐dependent PHA T cell activation and cytokines associated with proliferation while preserving SEB T cell and Pam3/PHA monocyte cytokine responses. ABSTRACT Pulmonary tuberculosis in humans is characterised by features of immunopathology, which influence both antimycobacterial therapy and the long‐term prognosis. In
Joseph F. Arthur +20 more
wiley +1 more source
Immune Evasion of Helicobacter pylori and Extra‐Gastric Cancer Risk
ABSTRACT Helicobacter pylori (H. pylori) is a group 1 gastric carcinogen that plays a significant role in extra‐gastric digestive system cancers. H. pylori disrupts host cell homeostasis through expression of virulence factors leading to immune evasion as well as persistent gastric mucosal colonization. H. pylori infection has been shown to play a role
Evren Doruk Engin +2 more
wiley +1 more source
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Activation of the lectin complement pathway by ficolins
International Immunopharmacology, 2001Mannose-binding lectin (MBL), a serum lectin specific for mannose or N-acetylglucosamine (GlcNAc), which contains both a collagen-like domain and a carbohydrate-recognition domain (CRD), plays a role in innate immunity by acting as an opsonin and activating complement in association with MBL-associated serine protease (MASP) via the lectin pathway ...
Naotaka Hamasaki, Teizo Fujita
exaly +3 more sources
Immunopharmacology, 1999
Lysis via the newly discovered lectin pathway of complement activation is reviewed. Mannan-coated erythrocytes sensitized with MBL are lysed in human serum containing Mg-EGTA via the lectin pathway by a process which requires alternative pathway amplification.
Yonghong Zhang +2 more
exaly +3 more sources
Lysis via the newly discovered lectin pathway of complement activation is reviewed. Mannan-coated erythrocytes sensitized with MBL are lysed in human serum containing Mg-EGTA via the lectin pathway by a process which requires alternative pathway amplification.
Yonghong Zhang +2 more
exaly +3 more sources
Lupus, 2011
The objective of the present study was to elucidate the association between glomerular complement depositions belonging to the alternative (AP) and lectin (LP) pathways, and clinical findings of lupus nephritis (LN). Immunofluorescence (IF) was performed on 17 LN patients using antibodies against factor B, factor H, properdin, mannose-binding lectin ...
I Ohsawa, S Nagamachi, Akira Toki
exaly +3 more sources
The objective of the present study was to elucidate the association between glomerular complement depositions belonging to the alternative (AP) and lectin (LP) pathways, and clinical findings of lupus nephritis (LN). Immunofluorescence (IF) was performed on 17 LN patients using antibodies against factor B, factor H, properdin, mannose-binding lectin ...
I Ohsawa, S Nagamachi, Akira Toki
exaly +3 more sources
A journey through the lectin pathway of complement—MBL and beyond
Immunological Reviews, 2016Peter Garred +2 more
exaly +2 more sources
Ficolins and the lectin complement pathway
Immunological Reviews, 2001Summary:Ficolins, found in various tissues, are a group of proteins containing both a collagen‐like and a fibrinogen‐like domain. Recently, it was shown that ficolins present in serum are lectins with a common binding specificity for N‐acetylglucosamine (GlcNAc). The fibrinogen‐like domain is responsible for the carbohydrate binding.
M, Matsushita, T, Fujita
openaire +2 more sources

