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

Mixed salivary pools of normal subjects and patients with galvanism, yeast-induced stomatitis, and diabetes mellitus were examined. The examinations have revealed elevated alpha-amylase levels in the patients with galvanism and still higher levels of this enzyme in yeast-induced stomatitis and diabetes mellitus. These diseases are also associated with a rise of lactoferrin content and with appearance of fibrinogen degradation products.
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PMID:[The proteins of human mixed saliva in galvanism and yeast-induced stomatitis]. 262 95

When vesicular stomatitis virus was incubated with Saccharomyces cerevisiae spheroplasts at 37 degrees C, part of the virus was internalized by the spheroplasts as shown by the following criteria. (i) The spheroplast-associated virus was protected from proteinase K digestion, which releases surface-bound virus by degrading the envelope glycoproteins. (ii) The spheroplast-associated virus was resistant to mild Triton X-100 treatment, which readily solubilizes the virus. The same results were obtained with Semliki Forest virus. Internalization of the two viruses followed linear kinetics up to 90 min at 37 degrees C. Internalization was concentration- and temperature-dependent. At 11 degrees C no uptake could be detected for at least 2 h. Homogenization and organelle fractionation protocols were designed for the S. cerevisiae spheroplasts to study the compartments into which the virions were internalized. Three compartments containing both marker viruses could be separated in density gradients. One coincided with vacuole markers, one banded at a slightly higher and one at a similar density to the plasma membrane markers. Thus, S. cerevisiae spheroplasts appear to have the capability of endocytosing particulate markers like viruses. The companion paper describes internalization of two soluble macromolecules, alpha-amylase and fluorescent dextran, into intact cells.
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PMID:Endocytosis in Saccharomyces cerevisiae: internalization of enveloped viruses into spheroplasts. 299 48

Mouse interferon-beta (IFN-beta) cDNA, whose signal sequence had been removed by BAL 31 digestion, was introduced into a Bacillus subtilis secretion vector constructed by using the promoter and signal sequence of the B. subtilis alpha-amylase gene. The resultant chimeric plasmids were transferred into B. subtilis 207-25. Four kanamycin-resistant transformants were selected by both colony hybridization and a new immunoblot method for secretory proteins. They secrete the proteins which cross-react with sheep anti-mouse IFN-beta serum into the culture medium. One of them expressed a high IFN-beta activity as assayed by the L cell and vesicular stomatitis virus system, while the other three showed weak or little IFN activities. Based on our previous study [Ohmura et al., Nucl. Acids Res. 12 (1984) 5307-5319], it was suggested that the secreted IFN molecules are hybrid proteins in which the NH2-terminal region consists of part of the alpha-amylase signal peptide. Nucleotide sequence analysis revealed that plasmid pTUB502, which expressed high IFN activity, is joined to the mouse IFN-beta gene from the codon position 6 of its mature protein. The other three plasmids, pTUB506, pTUB509, and pTUB519, contain the mouse IFN-beta gene from the codon positions 3, 1, and -5, respectively. The NH2-terminal region of the mouse IFN-beta seems to be closely related to its biological activity.
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PMID:Synthesis and secretion of biologically active mouse interferon-beta using a Bacillus subtilis alpha-amylase secretion vector. 392 34

The formation of a salivary pellicle is a protective mechanism of the body for all surfaces in the oral cavity. The nature of the substrate may influence the composition of the pellicle. The aim of this study was to investigate the quantitative composition and individual variation of the salivary pellicle formed on denture base material (PMMA). Cylindrical specimens of PMMA were carried in the mouth and then desorbed with a 0.5-M sodium chloride solution. The solution was analysed for total protein, alpha-amylase, total proteases, protease inhibitors, secretory immunoglobulin A, immunoglobulin G, peroxidases, thiocyanate, lysozyme, and calcium content. All investigated salivary components could be found unequivocally in the desorption solution, indicating that a salivary pellicle had formed on the surface of the PMMA. Large coefficients of variation indicate large individual variations in the adsorbed amounts. The data also point to large intraindividual variations for the bound salivary components. Only the protease inhibitors revealed a strong positive correlation of the bound activity to the salivary activity. It is hypothesised that differences in the bound amounts of antimicrobial components might influence the microbial colonisation of denture bases and that protease inhibitors could be meaningful for the spread of the yeast Candida albicans from denture base material to the oral mucosa and thus might be an explanation for different susceptibility to denture base stomatitis.
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PMID:Quantitative determination of salivary components in the pellicle on PMMA denture base material. 1248 38