Development of a high-specificity sandwich ELISA system for the quantification of human intestinal fatty acid-binding protein (I-FABP) concentrations.

Intestinal fatty acid-binding protein (I-FABP), a low molecular mass (approximately 15 kDa) cytoplasmic protein, is specifically located in epithelial cells of small bowel mucosal layer. This protein is rapidly released into the circulation after injury and/or destruction of these cells due to poor mesenteric blood flow and necrosis. Therefore, it can be used as a potential diagnostic biomarker for small bowel disease.

Establishment and characterization of monoclonal and polyclonal antibodies against human intestinal fatty acid-binding protein (I-FABP) using synthetic regional peptides and recombinant I-FABP.

We have succeeded in raising highly specific anti-human intestinal fatty acid-binding protein (I-FABP) monoclonal antibodies by immunizing animals with three synthetic regional peptides, i.e., the amino terminal (RP-1: N-acetylated 1-19-cysteine), middle portion (RP-2: cysteinyl-91-107) and carboxylic terminal (RP-3: cysteinyl-121-131) regions of human I-FABP, and the whole I-FABP molecule as antigens.

Clinical evaluation of point-of-care-testing of heart-type fatty acid-binding protein (H-FABP) for the diagnosis of acute myocardial infarction.

The present study was carried out for clinical evaluation of point-of-care-testing (POCT) of heart-type fatty acid-binding protein (H-FABP), Rapicheck H-FABP, for the diagnosis of acute myocardial infarction (AMI), in comparison with conventional cardiac biochemical markers such as myoglobin, creatine kinase isoenzyme MB (CK-MB), and cardiac troponin T. Whole blood samples from patients with confirmed AMI (n = 53), patients with non-AMI cardiac diseases (n = 24), and patients with non-cardiac diseases with chest pain (n = 6) were used. When a test line appeared within 15 min after the addition of 150 microL of whole blood, it was designated to be positive for H-FABP.

Development and evaluation of a direct sandwich enzyme-linked immunosorbent assay for the quantification of guinea-pig immunoglobulin e.

The purpose of this study was to develop and evaluate a direct sandwich enzyme-linked immunosorbent assay (ELISA) for the immunoglobulin E (IgE) in serum and plasma from guinea pig using mouse monoclonal antibodies specific for guinea-pig IgE. Mouse monoclonal antibodies were raised against purified IgE protein. The ELISA was performed using a combination of two anti-IgE monoclonal antibodies.

Thiamine attenuates the hypertension and metabolic abnormalities in CD36-defective SHR: uncoupling of glucose oxidation from cellular entry accompanied with enhanced protein O-GlcNAcylation in CD36 deficiency.

Background And Objectives: The spontaneous hypertensive rat (SHR) is a widely studied model of hypertension that exhibits metabolic abnormalities, which share features with the human metabolic syndrome. Genetic linkage studies have revealed a defective CD36 gene, encoding a membrane fatty acid (FA) transporter, in hyperinsulinemia of the SHR. However, there is no unifying mechanism that can explain these phenotypes as a consequence of a defective CD36 gene.