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  • 1
    Electronic Resource
    Electronic Resource
    PACAP-38 is a chemorepellent and an agonist for the lysozyme receptor in Tetrahymena thermophila (2000)
    Springer
    Journal of comparative physiology 186 (2000), S. 39-43 
    Details
    ISSN: 1432-1351
    Keywords: Key words Chemorepellent ; PACAP-38 ; Tetrahymena ; Chemosensory transduction ; Behavioral adaptation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Pituitary adenylate cyclase activating peptide (PACAP-38) is a peptide hormone which functions in many mammalian systems, including the nervous and digestive systems. Using in vivo behavioral studies, we have found that this hormone functions as a chemorepellent in Tetrahymena thermophila with an EC50 of 10 nM. Cells previously adapted to PACAP-38 were found to be adapted to lysozyme, and vice versa. Furthermore, the in vivo behavioral activity of PACAP-38 was blocked by addition of the anti-lysozyme receptor antibody, 5545. Chemorepellent activity of PACAP-38 was also inhibited by the addition of neomycin sulfate (inhibition constant K i=0.080 μmol · l−1), a competitive inhibitor of lysozyme binding to its receptor. PACAP-38 is a more potent and specific agonist for the lysozyme receptor than either intact lysozyme or CB2, a 24-amino acid fragment of lysozyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s003590050005
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Altered lectin binding by colonic epithelial glycoconjugates in ulcerative colitis and Crohn's disease (1988)
    Springer
    Digestive diseases and sciences 33 (1988), S. 1359-1363 
    Details
    ISSN: 1573-2568
    Keywords: lectins ; glycoconjugates ; ulcerative colitis ; Crohn's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Evidence is accumulating that colonic mucin glycoconjugates are altered in ulcerative colitis. In order to investigate this further, the lectin-binding properties of rectal glycoconjugates have been studied in ulcerative colitis, Crohn's disease, and controls using lectin-peroxidase histochemistry. Ten lectins were used including peanut agglutinin (PNA) which is known to bind to malignant and adenomatous but not normal colonic mucins. Eight of 21 ulcerative colitis rectal biopsies and 10 of 17 Crohn's disease rectal biopsies showed PNA positivity, particularly in the supranuclear region of surface epithelial cells. There was no correlation between PNA positivity and duration of disease or inflammation, and none of the biopsies showed evidence of dysplasia. This abnormality in epithelial cell glycoconjugates seems to be commonly present in nondysplastic mucosa and occurs in both ulcerative colitis and Crohn's disease. It may reflect a fundamental abnormality in mucus glycoprotein synthesis in inflammatory bowel disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01536988
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Stress proteins in colorectal mucosa (1993)
    Springer
    Digestive diseases and sciences 38 (1993), S. 1994-2000 
    Details
    ISSN: 1573-2568
    Keywords: heat shock protein ; mucin ; ulcerative colitis ; Crohn's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Stress (heat shock) proteins are ubiquitous intracellular proteins that can be inducedin vitro by physiological stress events that occur during inflammation. We have used an indirect immunoperoxidase method to locate 60-kDa stress proteins in biopsies taken from normal and inflamed colorectal mucosa. An anti-60-kDa monoclonal antibody (ML30) produced specific staining of surface epithelial cells localized to the site of the Golgi apparatus. In ulcerative colitis, there was an increased concentration of this stress protein compared with controls (P≤0.002) and also with a small group of active Crohn's colitis (P≤0.01), but no relationship between its concentration and disease activity. All biopsies also showed staining of goblet cells by ML30, suggesting a possible cross-reaction with mucin; electroblotting of crude but not purified mucin showed a faint 60-kDa band with ML30. We conclude that the 60-kDa stress protein is present in normal colorectal epithelial cells and is markedly inducedin vivo in ulcerative colitis. Further, we suggest that since the 60-kDa protein functions as a molecular chaperone, it may associate with colonic mucin aiding in its synthesis and/or secretion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01297075
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    Paper (German National Licenses)
    Fulltext
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