Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0038362 (stomatitis)
 8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An account has been given of a patient with denture sore mouth caused by allergy to the denture material (Part I). In the continued investigation the residual monomer or part thereof was found to be the allergen. Patch testing of the skin with drillings from the upper and lower dentures made of a "warm-polymerized" methyl methacrylate resin was carried out with special reference to the topography of the distribution of the allergenic factor within the dentures. Only that surface of the upper denture that is in contact with the hard palate and the maxillary crista were allergenic. All other surfaces of the upper denture as well as the complete lower denture were non-allergenic. The resin was, in other words, inhomogeneous as regards the allergenic factor. An analysis of the test castings showed that the allergenic properties in the resin are located in the surface and that the resin was free from allergens below the "allergenic film" (Parts I and II). A non-allergenic, extraordinarily well-fitting denture was produced from the same make of acrylic as that used for the non-tolerated denture. It was made by a new technique, "directed polymerization," comprising initial application of heat centrally in the cuvette (a metal cup surrounding the gypsum), including tin-foiling of the palatal half of the mould. The production of the denture was based on experience from tests with test castings. A check-up 18 months later showed no stomatitis and the retention and stability of the denture were very satisfactory, and tests with the original model of the upper gum showed that it had an excellent fit.
 ...
PMID:Location of the allergenic monomer in warm-polymerized acrylic dentures. Part II: Experiments aimed at establishing guidelines for production of acrylic dentures suited for patients allergic to acrylic monomer and complementary investigations. 701 Jun 54

We have reconstituted polarized protein transport in streptolysin O-permeabilized MDCK cells from the TGN to the basolateral surface and to the apical surface. These transport steps are dependent on temperature, energy and exogenously supplied cytosol. Using this in vitro system we show that a whole tail peptide (WT peptide) corresponding to the cytoplasmic tail of a basolaterally sorted protein, the vesicular stomatitis virus glycoprotein (VSV G) inhibits the TGN to basolateral transport but does not affect any other transport step. Inhibition of VSV G transport to basolateral surface by WT peptide did not result in missorting of the protein to the apical surface. Mutation of the single tyrosine residue in the WT peptide reduced its inhibitory potency four- to fivefold. These results suggest that the VSV G tail physically interacts with a component of the sorting machinery. Using a cross-linking approach, we have identified proteins that associate with the cytoplasmic tail domain of VSV G. One of these polypeptides, Tin-2 (Tail interacting protein-2), associates with VSV G in the TGN, the site of protein sorting, but not in the ER nor at the cell surface. Tin-2 does not associate with apically targeted hemagglutinin. WT peptide that inhibited the basolateral transport of VSV G also inhibited the association of Tin-2 with VSV G. Together, these properties make Tin-2 a candidate basolateral sorter. The results demonstrate the usefulness of the SLO-permeabilized cell system in dissecting the sorting machinery.
 ...
PMID:Basolateral protein transport in streptolysin O-permeabilized MDCK cells. 819 86