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  • 1
    Keywords: Germany ; human ; DISEASE ; DISEASES ; PROTEIN ; MICE ; PATIENT ; ACID ; HUMANS ; mass spectrometry ; tandem mass spectrometry ; TANDEM MASS-SPECTROMETRY ; PATHOGENESIS ; MASS-SPECTROMETRY ; STRATEGIES ; RANDOMIZED-TRIAL ; ULCERATIVE-COLITIS ; CROHNS-DISEASE ; rodent ; INFLAMMATORY-BOWEL-DISEASE ; COLITIS ; GASTRIC-MUCOSA ; GASTRODUODENAL MUCOSAL PROTECTION ; inflammatory bowel disease ; phosphatidylcholine ; SPHINGOMYELIN ; USA ; ACID-RESIDUES ; NOV ; lipid ; PULMONARY SURFACTANT ; therapeutic ; STRATEGY ; INVESTIGATE ; CD ; COLONIC-MUCOSA ; EXTRACTS ; G-Protein ; GASTROINTESTINAL MUCUS ; lysophosphatidylcholine ; nano ESI mass spectrometry
    Abstract: Background: Phospholipids are essential for the normal function of the intestinal mucus barrier. The objective of this study was to systematically investigate phospholipids in the intestinal mucus of humans Suffering from inflammatory bowel diseases, where it barrier defect is strongly supposed to be pathogenetic. Methods: Optimal mucus recovery was first validated in healthy mice and the method was then transferred to the endoscopic acquisition of ileal and colonic mucus from 21 patients with ulcerative colitis (UC), 10 patients with Crohn's disease (CD), and 29 healthy controls. Nano-electrospray ionization tandem mass spectrometry (ESI-MS/MS) was used to determine phosphatidylcholine (PC), lysophosphatidylcholine (LPC), and sphingomyelin (SM) in lipid extracts of mucus specimens. Results: Human and rodent mucus contained very similar phospholipid species. In the ileal and colonic mucus from patients suffering from UC, the concentration of PC was highly significantly lower (607 +/- 147 pmol/100 mu g protein and 745 +/- 148 pmol/100 mu g protein) compared to that of patients with CD (3223 +/- 1519 pmol/100 mu g protein and 2450 +/- 431 pmol/100 mu g protein) and to controls (3870 +/- 760 pmol/100 mu g protein and 2790 +/- 354 pmol/100 mu g protein), overall, P = 0.0002 for ileal specimens and P 〈 0.0001 tor colonic specimens. Independent of disease activity, patients suffering from UC showed an increased Saturation grade of PC fatty acid residues and it higher LPC-to-PC ratio. Conclusions: The intestinal mucus barrier of patients with UC is significantly altered concerning its phospholipid concentration and species composition. These alterations may be very important for the pathogenesis of this disease and underline new therapeutic strategies
    Type of Publication: Journal article published
    PubMed ID: 19504612
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  • 2
    Keywords: GENE ; CELL-SURFACE ; ENDOPLASMIC-RETICULUM ; COILED COILS ; COPI-COATED VESICLES ; BREFELDIN-A ; RETROGRADE TRANSPORT ; BIOLOGICAL-MEMBRANES ; MAMMALIAN KDEL RECEPTOR ; CRISP FAMILY
    Abstract: Group 1 of plant pathogenesis-related proteins (PR-1) and a variety of related mammalian proteins constitute a superfamily of proteins that share structural similarities. Little is known about their function, but all the family members identified to date are co-translationally translocated to the lumen of the endoplasmic reticulum and are secreted as soluble proteins or are targeted to vacuoles. Here we report the identification of a novel family member that localizes to the cytosolic site of the endomembrane system in mammalian cells. After detergent solubilization of isolated Golgi membranes, a 17 kDa protein was found associated with a low-density detergent-insoluble fraction. The amino-acid sequence, determined by microsequencing and molecular cloning, revealed a significant homology with the superfamily of PR-1 proteins. Golgi-associated PR-1 protein (GAPR-1) showed a brefeldin-A-sensitive Golgi localization in immunofluorescence. Interestingly, the protein remained associated with the microdomain fraction in the presence of Brefeldin A. By mass spectrometry, GAPR-1 was shown to be myristoylated. Immunoprecipitation of GAPR- 1 from Golgi membranes resulted in the coimmunoprecipitation of caveolin-1, indicating a direct interaction between these two proteins. Myristoylation, together with protein-protein or electrostatic interactions at physiological pH owing to the highly basic pI of GAPR-1 (pI 9.4) could explain the strong membrane association of GAPR-1. Tissue screening revealed that GAPR-1 is not detectably expressed in liver, heart or adrenal glands. High expression was found in monocytes, leukocytes, lung, spleen and embryonic tissue. Consistent with the involvement of PR-1 proteins in the plant immune system, these data could indicate that GAPR-1 is involved in the immune system.
    Type of Publication: Journal article published
    PubMed ID: 11865038
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