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mannose/infarction
Врската е зачувана во таблата со исечоци
Страница 1 од 58 резултати
Influence of functional deficiency of complement mannose-binding lectin on outcome of patients with acute ST-elevation myocardial infarction undergoing primary percutaneous coronary intervention.
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OBJECTIVE
Experimental data point towards a favourable effect of low serum concentrations of complement mannose-binding lectin (MBL) on myocardial ischaemia/reperfusion (I/R) injury. As comparable data on the role of MBL in human I/R injury is lacking, we investigated the influence of low serum MBL
Mannose binding lectin and soluble Toll-like receptor 2 in heart failure following acute myocardial infarction.
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BACKGROUND
To determine the relationship between markers of innate immunity and clinical outcomes in patients with heart failure (HF) after acute myocardial infarction (AMI). Atherogenesis and HF is associated with the altered control of inflammation by innate immune defenses that include
Mannose-binding lectin deficiency is associated with myocardial infarction: the HUNT2 study in Norway.
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OBJECTIVE
Mannose-binding lectin (MBL) and ficolins activate the complement cascade, which is involved in atherogenesis. Based on a pilot study, we hypothesized that functional polymorphisms in the MBL gene (MBL2) leading to dysfunctional protein are related to development of myocardial infarction
Mannose-binding lectin genotype and phenotype in patients with type 2 diabetes and myocardial infarction: a report from the DIGAMI 2 trial.
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OBJECTIVE
The present study characterizes mannose-binding lectin (MBL), an activator of the complement system and thereby important for inflammatory activation, in patients with diabetes and myocardial infarction.
METHODS
Serum (S)-MBL was determined at hospital admission in 387 patients with type 2
Mannose-binding lectin deficiency is associated with smaller infarction size and favorable outcome in ischemic stroke patients.
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BACKGROUND
The Mannose-binding lectin (MBL) pathway of complement plays a pivotal role in the pathogenesis of ischemia/reperfusion (I/R) injury after experimental ischemic stroke. As comparable data in human ischemic stroke are limited, we investigated in more detail the association of MBL
Mannose-binding lectin: an ancient molecule with new implications in myocardial infarction.
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Serum levels of mannose-binding lectin and the risk of future coronary artery disease in apparently healthy men and women.
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OBJECTIVE
To determine the association between serum levels of mannose-binding lectin (MBL) and the risk of future coronary artery disease (CAD) in apparently healthy men and women.
RESULTS
We performed a prospective case-control study among apparently healthy men and women nested in the
Mannose-binding lectin plays a critical role in myocardial ischaemia and reperfusion injury in a mouse model of diabetes.
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OBJECTIVE
Diabetic patients are at increased risk of cardiomyopathy, acute myocardial infarction and loss of cardiac progenitor cells (CPCs), but the aetiology is poorly understood. We hypothesised a significant role for mannose-binding lectin (MBL) in cardiomyopathies associated with
IGF-II/mannose-6-phosphate receptor signaling induced cell hypertrophy and atrial natriuretic peptide/BNP expression via Galphaq interaction and protein kinase C-alpha/CaMKII activation in H9c2 cardiomyoblast cells.
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The role played by IGF-II in signal transduction through the IGF-II/mannose-6-phosphate receptor (IGF2R) in heart tissue has been poorly understood. In our previous studies, we detected an increased expression of IGF-II and IGF2R in cardiomyocytes that had undergone pathological hypertrophy. We
IGF-II/mannose 6-phosphate receptor activation induces metalloproteinase-9 matrix activity and increases plasminogen activator expression in H9c2 cardiomyoblast cells.
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The IGF-II/mannose 6-phosphate receptor (IGF2R) function in extracellular matrix (ECM) remodeling is known to occur as a result of transforming growth factor-beta (TGF-beta) activation and plasmin in the proteolytic cleavage level caused by the interaction between latent TGF-beta and urokinase
Classically and alternatively activated macrophages contribute to tissue remodelling after myocardial infarction.
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An important goal in cardiology is to minimize myocardial necrosis and to support a discrete but resilient scar formation after myocardial infarction (MI). Macrophages are a type of cells that influence cardiac remodelling during MI. Therefore, the goal of the present study was to investigate their
Association between lectin complement pathway initiators, C-reactive protein and left ventricular remodeling in myocardial infarction-a magnetic resonance study.
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BACKGROUND
Lectin complement pathway (LP) activation is an important mechanism in myocardial ischemia reperfusion injury (IRI). LP is activated via the recognition molecules mannose-binding lectin (MBL), ficolins-2 and-3 and is regulated by MBL/Ficolin-associated Protein-1 (MAP-1). Also, C-reactive
[Level of mannose-binding lectin and phagocytic activity of leukocytes in patients with acute coronary syndrome].
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Mannose-binding lectin (MBL) is a key component of innate immunity that starts one of the ways of complement activation. Factors of neutrophil activation are cell factors of innate and acquired immunity.
OBJECTIVE
to study MBL levels and factors of neutrophil activation in patients with acute
[Cardiovascular diseases and mannose-binding lectin].
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The role of innate immunity factors in the pathogens of ACS is not well studied, although there is evidence in the literature about their impact on the course of cardiovascular diseases. Mannose-binding lectin (MBL)--one of the key factors of the humoral innate immune system that activates one of
Mannose-binding lectin variant alleles and the risk of arterial thrombosis in systemic lupus erythematosus.
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BACKGROUND
Cardiovascular disease is an important complication in patients with systemic lupus erythematosus (SLE). Variant alleles of the mannose-binding lectin gene are associated with SLE as well as with severe atherosclerosis. We determined whether mannose-binding lectin variant alleles were
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