22 research outputs found

    Transportation Cost Optimization

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    Many manufacturing make their products in few locations and ship them to many different locations. In this paper we use Evolver, Excel Solver and Microsoft Solver Foundation in order to optimize transportation cost or to find the cheaper way to make and ship products to the customers and meet customers’ demands. “Proplast” company that manufactures doors and windows is located in three different places; in Ferizaj, Pristina and Prizren and supplies 9 shops in Kosovë, Albania, Macedonia, Montenegro and Serbia. Mathematically speaking, our goal is to find minimal transportation cost and this problem will be set up as a linear programming model with the below definition: * Minimize total production and transportation cost; * Constraints: -The amount shipped from each factory cannot exceed plant capacity, - Every shop must receive its required demand, - Transportation trucks have the limit of loading quantity and - Each shipping amount must be nonnegative. We will show Evolver, Excel Solver and Microsoft Solver Foundation results and will find the least expensive way. Also we will compare minimum and maximum cost for all software’s. DOI: 10.5901/ajis.2015.v4n2s1p4

    Neonatal isolated coronary artery dilatation: to treat (and how) or not to treat, that’s the question!

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    We describe the clinical presentation of a newborn, who received diagnosis of diffuse right coronary artery dilatation and a high origin of the same vessel, in the absence of intrauterine hypoxia or other identifiable causes of coronary artery ectasia. The relevance of the case is in the complex aetiology of congenital heart malformation. In addition, we also highlight the difficult therapeutic management of these patients, in lack of guidelines for newborn population

    Visual assessment versus computer-assisted gray scale analysis in the ultrasound evaluation of neonatal respiratory status

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    Lung ultrasound has been used to describe common respiratory diseases both by visual and computer-assisted gray scale analysis. In the present paper, we compare both methods in assessing neonatal respiratory status keeping two oxygenation indexes as standards. Neonates admitted to the NICU for respiratory distress were enrolled. Two neonatologists not attending the patients performed a lung scan, built a single frame database and rated the images with a standardized score. The same dataset was processed using the gray scale analysis implemented with textural features and machine learning analysis. Both the oxygenation ratio (PaO2/FiO2) and the alveolar arterial oxygen gradient (A-a) were kept as reference standards. Seventy-five neonates with different respiratory status were enrolled in the study and a dataset of 600 ultrasound frames was built. Visual assessment of respiratory status correlated significantly with PaO2/FiO2 (r = -0.55; p<0.0001) and the A-a (r = 0.59; p<0.0001) with a strong interobserver agreement (K = 0.91). A significant correlation was also found between both oxygenation indexes and the gray scale analysis of lung ultrasound scans using regions of interest corresponding to 50K (r = -0.42; p<0.002 for PaO2/FiO2; r = 0.46 p<0.001 for A-a) and 100K (r = -0.35 p<0.01 for PaO2/FiO2; r = 0.58 p<0.0001 for A-a) pixels regions of interest. A semi quantitative estimate of the degree of neonatal respiratory distress was demonstrated both by a validated scoring system and by computer assisted analysis of the ultrasound scan. This data may help to implement point of care ultrasound diagnostics in the NICU

    Enterocyte proliferation and signaling are constitutively altered in celiac disease.

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    Celiac disease (CD) occurs frequently, and is caused by ingestion of prolamins from cereals in subjects with a genetic predisposition. The small intestinal damage depends on an intestinal stress/innate immune response to certain gliadin peptides (e.g., A-gliadin P31-43) in association with an adaptive immune response to other gliadin peptides (e.g., A-gliadin P57-68). Gliadin and peptide P31-43 affect epithelial growth factor receptor (EGFR) signaling and CD enterocyte proliferation. The reason why the stress/innate immune and proliferative responses to certain gliadin peptides are present in CD and not in control intestine is so far unknown. The aim of this work is to investigate if, in CD, a constitutive alteration of enterocyte proliferation and signaling exists that may represent a predisposing condition to the damaging effects of gliadin. Immunofluorescence and immunohistochemistry were used to study signaling in CD fibroblasts and intestinal biopsies. Western blot (WB) analysis, immunoprecipitation, and quantitative PCR were also used. We found in CD enterocytes enhancement of both proliferation and Epidermal Growth Factor Receptor (EGFR)/ligand system. In CD enterocytes and fibroblasts we found increase of the phosphorylated downstream signaling molecule Extracellular Signal Regulated Kinase (ERK); block of the ERK activation normalizes enterocytes proliferation in CD mucosa. In conclusion the same pathway, which gliadin and gliadin peptide P31-43 can interfere with, is constitutively altered in CD cells. This observation potentially explains the specificity of the damaging effects of certain gliadin peptides on CD intestine

    A Celiac Cellular Phenotype, with Altered LPP Sub-Cellular Distribution, Is Inducible in Controls by the Toxic Gliadin Peptide P31-43.

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    Celiac disease (CD) is a frequent inflammatory intestinal disease, with a genetic background, caused by gliadin-containing food. Undigested gliadin peptides P31-43 and P57-68 induce innate and adaptive T cell-mediated immune responses, respectively. Alterations in the cell shape and actin cytoskeleton are present in celiac enterocytes, and gliadin peptides induce actin rearrangements in both the CD mucosa and cell lines. Cell shape is maintained by the actin cytoskeleton and focal adhesions, sites of membrane attachment to the extracellular matrix. The locus of the human Lipoma Preferred Partner (LPP) gene was identified as strongly associated with CD using genome-wide association studies (GWAS). The LPP protein plays an important role in focal adhesion architecture and acts as a transcription factor in the nucleus. In this study, we examined the hypothesis that a constitutive alteration of the cell shape and the cytoskeleton, involving LPP, occurs in a cell compartment far from the main inflammation site in CD fibroblasts from skin explants. We analyzed the cell shape, actin organization, focal adhesion number, focal adhesion proteins, LPP sub-cellular distribution and adhesion to fibronectin of fibroblasts obtained from CD patients on a Gluten-Free Diet (GFD) and controls, without and with treatment with A-gliadin peptide P31-43. We observed a "CD cellular phenotype" in these fibroblasts, characterized by an altered cell shape and actin organization, increased number of focal adhesions, and altered intracellular LPP protein distribution. The treatment of controls fibroblasts with gliadin peptide P31-43 mimics the CD cellular phenotype regarding the cell shape, adhesion capacity, focal adhesion number and LPP sub-cellular distribution, suggesting a close association between these alterations and CD pathogenesis

    A Celiac Cellular Phenotype, with Altered LPP Sub-Cellular Distribution, Is Inducible in Controls by the Toxic Gliadin Peptide P31-43

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    <div><p>Celiac disease (CD) is a frequent inflammatory intestinal disease, with a genetic background, caused by gliadin-containing food. Undigested gliadin peptides P31-43 and P57-68 induce innate and adaptive T cell-mediated immune responses, respectively. Alterations in the cell shape and actin cytoskeleton are present in celiac enterocytes, and gliadin peptides induce actin rearrangements in both the CD mucosa and cell lines. Cell shape is maintained by the actin cytoskeleton and focal adhesions, sites of membrane attachment to the extracellular matrix. The locus of the human Lipoma Preferred Partner (LPP) gene was identified as strongly associated with CD using genome-wide association studies (GWAS). The LPP protein plays an important role in focal adhesion architecture and acts as a transcription factor in the nucleus. In this study, we examined the hypothesis that a constitutive alteration of the cell shape and the cytoskeleton, involving LPP, occurs in a cell compartment far from the main inflammation site in CD fibroblasts from skin explants. We analyzed the cell shape, actin organization, focal adhesion number, focal adhesion proteins, LPP sub-cellular distribution and adhesion to fibronectin of fibroblasts obtained from CD patients on a Gluten-Free Diet (GFD) and controls, without and with treatment with A-gliadin peptide P31-43. We observed a “CD cellular phenotype” in these fibroblasts, characterized by an altered cell shape and actin organization, increased number of focal adhesions, and altered intracellular LPP protein distribution. The treatment of controls fibroblasts with gliadin peptide P31-43 mimics the CD cellular phenotype regarding the cell shape, adhesion capacity, focal adhesion number and LPP sub-cellular distribution, suggesting a close association between these alterations and CD pathogenesis.</p></div

    Proliferation of crypt enterocytes was increased in CD.

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    <p>A. Immunofluorescence images of crypts from duodenal biopsies from a control, from a CD patient with villous atrophy, from a potential CD patient who were on a gluten-containing diet and from a GFD CD patient. Biopsies were cultured for 24 h with BrdU and then stained for cytokeratin to identify epithelial cells (red) and for BrdU (green) to identify proliferating cells. One representative experiment is shown. B. Quantitation of BrdU incorporation in intestinal biopsies. More than 300 cytokeratin-positive cells were counted in several fields in each sample; the number of BrdU- positive cells was expressed as a proportion of the total cytokeratin-positive cells. Columns represent the mean, bars the standard deviation, N. is the number of biopsies tested * = P<0.05; *** = P<0.001 (Student's t-test). One-way analysis of variance (ANOVA): P value = 0.0037 (4 groups, F = 5.437, R squared = 0.3242).</p

    Phosphorylation of EGFR, ERK and total proteins was increased in skin fibroblasts of CD patients.

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    <p>Staining of total phosphorylated proteins in CD and controls fibroblasts. (a) Immunofluorescence of double staining with phalloidin (red) and anti-phosphotyrosin (green). Images obtained using a 63× objective (2× digital zoom) are shown. (b) Statistical analysis of fluorescence intensity/cell. For 5 patients and 4 controls, 3 independent experiments were done; in each experiment, the fluorescence intensity of 10 cells in random fields was measured. Columns represent means and bars standard deviation. * = P<0.05 (Student's t-test). B. Western blot analysis of total phosphorylated proteins in skin fibroblasts from CD patients on GFD and from controls. Phosphoproteins from CD patients and controls fibroblasts were lysates and immunoprecipitated (Ip), blotted and stained with anti-phosphotyrosine antibodies (blot anti-pY). The blots were stained again with anti-EGFR (blot anti-EGFR) and anti-ERK (blot anti-ERK) antibodies to identify the corresponding phosphorylated proteins. One representative experiment of 3 independent ones is shown for each subject (4 controls and 5 patients). C. Western blot analysis of phosphorylated ERK and EGFR in skin fibroblasts from CD patients on a GFD and from controls. (a) Western blot analysis of skin fibroblasts from CD patients and controls stained with anti-pY-ERK, anti-ERK and anti-tubulin antibodies. (b) Statistical analysis of WB obtained from 5 CD patients and 4 controls. Columns represent the mean, bars the standard deviation of the relative intensity of pY-ERK respect to total ERK protein. *** = P<0.001 (Student's t-test). (c) Western blot analysis of EGFR immunoprecipitated from skin fibroblasts and stained with anti-pY antibody. (d) Statistical analysis of WB obtained from 5 CD patients and 4 controls. Columns represent the mean, bars the standard deviation of the relative intensity of pY-EGFR respect to total EGFR protein** = P<0.01 (Student's t-test).</p
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