@article {3476, title = {Influence of urine volume on the assessment of intestinal permeability in affected children by multiple sugar probes.}, journal = {Clin Chem Lab Med}, volume = {52}, year = {2014}, month = {2014 Feb}, pages = {227-35}, abstract = {

BACKGROUND: In this study we have looked at the reliability of a multi-sugar test in a pediatric patient population and its accuracy at small urine volumes to evaluate intestinal permeability.

METHODS: Out of 117 subjects enrolled, 31 were healthy and 86 were sick. A solution containing lactulose, rhamnose, sucrose, and sucralose was administered to subjects who were on fasting; the urine excreted during 5 h was collected and measured. Samples were analyzed by gas chromatography-tandem mass spectrometry and results were expressed as percentage of sugar recoveries and lactulose/rhamnose (L/R) ratio.

RESULTS: The analyses showed a clear effect of low urinary volumes (<=240 mL) particularly affecting rhamnose excretion in healthy subjects and sucrose and sucralose recovery in diseased children. Despite the low rhamnose recovery, as lactulose is not similarly affected, the diagnostic reliability of L/R ratio is well preserved at low diuresis conditions. However, this ratio can be useful to discriminate acute conditions vs. clinical remissions only at high urine volumes. Data also suggest potential diagnostic applicability of sucrose and sucralose in children at high urine volumes.

CONCLUSIONS: In conclusion, the multi-sugar test has a good predictivity in pediatric subjects but results must be carefully interpreted in the face of reduced diuresis.

}, keywords = {Carbohydrates, Child, Preschool, Diuresis, Female, Gas Chromatography-Mass Spectrometry, Gastrointestinal Diseases, Humans, Infant, Intestines, Lactulose, Male, Permeability, Rhamnose, Sucrose}, issn = {1437-4331}, doi = {10.1515/cclm-2013-0626}, author = {Addobbati, Riccardo and Pascolo, Lorella and Di Toro, Nicola and Sebastiani, Giulia B and Martellossi, Stefano and Not, Tarcisio} } @article {1602, title = {The active Zot domain (aa 288-293) increases ZO-1 and myosin 1C serine/threonine phosphorylation, alters interaction between ZO-1 and its binding partners, and induces tight junction disassembly through proteinase activated receptor 2 activation.}, journal = {FASEB J}, volume = {25}, year = {2011}, month = {2011 Jan}, pages = {144-58}, abstract = {

Vibrio cholerae-derived zonula occludins toxin (Zot) is a multifunctional protein that reversibly disassembles intestinal tight junctions (tjs). Zot structure-function analysis has mapped this activity to aa 288-293, named AT1002. AT1002 reduced transepithelial electrical resistance across rat small intestine, ex vivo, as did Zot and its processed mature form, ΔG. AT1002 increased in vivo permeability to sugar tracers, whereas scrambled control peptides did not. Binding and barrier assays in proteinase activated receptor (PAR)(2)-expressing and PAR(2)-null cells established AT1002 activity to be PAR(2) dependent. Coincident with the increased intestinal permeability, confocal microscopy of AT1002-exposed rat intestinal IEC6 cells revealed displacement of ZO-1 and occludin from intercellular boundaries. In coimmunoprecipitation assays, AT1002 decreased ZO-1-occludin and ZO-1-claudin 1 interactions coincident with PKCα-dependent ZO-1 serine/threonine phosphorylation. Further, AT1002 increased serine phosphorylation of myosin 1C and, at the same time, transiently diminished its association with ZO-1. The COOH-terminal domain of ZO-1 was required for its association with myosin 1C. These data indicate that the NH(2)-terminal portion of active Zot contains a PAR(2)-activating motif, FCIGRL, that increases PKCα-dependent ZO-1 and myosin 1C serine/threonine phosphorylation. These modifications provoke selective disengagement of ZO-1 from its binding partners, occludin, claudin 1, and myosin 1C, coincident with opening of tjs.

}, keywords = {Amino Acid Sequence, Animals, Caco-2 Cells, Cell Line, Cells, Cultured, Cholera Toxin, Epithelial Cells, Humans, Immunoblotting, Male, Membrane Proteins, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Myosins, Oligopeptides, Phosphoproteins, Phosphorylation, Protein Binding, Protein Kinase C-alpha, Rats, Rats, Wistar, Receptor, PAR-2, RNA Interference, Serine, Threonine, Tight Junctions, Zonula Occludens-1 Protein}, issn = {1530-6860}, doi = {10.1096/fj.10-158972}, author = {Goldblum, Simeon E and Rai, Usha and Tripathi, Amit and Thakar, Manjusha and De Leo, Luigina and Di Toro, Nicola and Not, Tarcisio and Ramachandran, Rithwik and Puche, Adam C and Hollenberg, Morley D and Fasano, Alessio} } @article {1797, title = {Anti-α-enolase Antibodies in Serum from Pediatric Patients Affected by Inflammatory Diseases: Diagnostic and Pathogenetic Insights.}, journal = {Int J Rheumatol}, volume = {2011}, year = {2011}, month = {2011}, pages = {870214}, abstract = {

Human glycolytic enzyme α-enolase was associated with human diseases and with inflammation. An ELISA test was developed to measure anti-α-enolase AAE IgG and AAE IgA in the serum from patients affected by inflammatory diseases with the purpose to evaluate it as a novel diagnostic marker. 80 healthy blood donors and 194 paediatric patients affected by Juvenile idiopathic arthritis (JIA), celiac disease (CD), Crohn{\textquoteright}s Disease (CrD), hereditary periodic fever (HPF), and PFAPA syndrome were included in the study. HPF patients showed high levels of AAE antibodies, whereas JIA, CD, and CrD presented only partial results. Benign fevers such as PFAPA were almost negative for AAE Abs. These findings suggested that the genetic dysfunction of inflammasome associated with HPF could lead to the formation of AAE Abs that could be used for an early and easy diagnosis.

}, issn = {1687-9279}, doi = {10.1155/2011/870214}, author = {Pontillo, Alessandra and Di Toro, Nicola and Edomi, Paolo and Shadlow, A and Ammadeo, A and Gattorno, M and Not, T and Lepore, L and Crovella, S} } @article {1653, title = {Fasting increases tobramycin oral absorption in mice.}, journal = {Antimicrob Agents Chemother}, volume = {54}, year = {2010}, month = {2010 Apr}, pages = {1644-6}, abstract = {

The pharmacokinetics of the aminoglycoside tobramycin was evaluated after oral administration to fed or fasting (15 h) mice. As expected, under normal feeding conditions, oral absorption was negligible; however, fasting induced a dramatic increase in tobramycin bioavailability. The dual-sugar test with lactulose and l-rhamnose confirmed increased small bowel permeability via the paracellular route in fasting animals. When experiments aimed at increasing the oral bioavailability of hydrophilic compounds are performed, timing of fasting should be extremely accurate.

}, keywords = {Administration, Oral, Animals, Anti-Bacterial Agents, Biological Availability, Fasting, Injections, Intramuscular, Injections, Intravenous, Intestinal Absorption, Lactulose, Male, Mice, Mice, Inbred BALB C, Rhamnose, Tobramycin}, issn = {1098-6596}, doi = {10.1128/AAC.01172-09}, author = {De Leo, Luigina and Di Toro, Nicola and Decorti, Giuliana and Malus{\`a}, Noelia and Ventura, Alessandro and Not, Tarcisio} }