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)

Little information is available about the acquired pellicle layer that is formed on denture surfaces or its role in regulating microbial colonization of the prosthetic surface. Because denture-induced stomatitis is associated with increased numbers of Candida albicans and other microorganisms on the denture surface, the acquired denture pellicle (ADP) may play a role in modulating this colonization. This study examined and compared ADP from healthy patients and patients with stomatitis by chemical and immunochemical methods. The ADP was found to be composed of a selectively adsorbed layer containing salivary amylase, high molecular weight mucin (MG1), lysozyme, albumin, and sIgA. Salivary cystatins, proline-rich proteins, and low molecular weight mucin (MG2) were not detected. ADP amino acid composition was distinct from any of the ductal salivas, but had many similarities with enamel pellicle. Immunoblots of ADP from patients with stomatitis identified additional serum components, degradation products, and C. albicans cell components that were not detected in ADP from healthy patients. Quantification of these molecules in ADP could lead to a diagnostic test for oral mucosal disease underlying a denture base. Identification of specific molecules in denture pellicle that promote adhesion of C. albicans may elucidate a mechanism of fungal cell colonization on the denture surface. Future studies that chemically modify the denture acrylic resin surface to immobilize antimicrobial proteins may be a means of decreasing pathogenic plaque development.
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PMID:Characterization of acquired denture pellicle from healthy and stomatitis patients. 140 50

Members of the Bunyaviridae family mature by a budding process in the Golgi complex. The site of maturation is thought to be largely determined by the accumulation of the two spike glycoproteins, G1 and G2, in this organelle. Here we show that the signal for localizing the Uukuniemi virus (a phlebovirus) spike protein complex to the Golgi complex resides in the cytoplasmic tail of G1. We constructed chimeric proteins in which the ectodomain, transmembrane domain (TMD), and cytoplasmic tail (CT) of Uukuniemi virus G1 were exchanged with the corresponding domains of either vesicular stomatitis virus G protein (VSV G), chicken lysozyme, or CD4, all proteins readily transported to the plasma membrane. The chimeras were expressed in HeLa or BHK-21 cells by using either the T7 RNA polymerase-driven vaccinia virus system or the Semliki Forest virus system. The fate of the chimeric proteins was monitored by indirect immunofluorescence, and their localizations were compared by double labeling with markers specific for the Golgi complex. The results showed that the ectodomain and TMD (including the 10 flanking residues on either side of the membrane) of G1 played no apparent role in targeting chimeric proteins to the Golgi complex. Instead, all chimeras containing the CT of G1 were efficiently targeted to the Golgi complex and colocalized with mannosidase II, a Golgi-specific enzyme. Conversely, replacing the CT of G1 with that from VSV G resulted in the efficient transport of the chimeric protein to the cell surface. Progressive deletions of the G1 tail suggested that the Golgi retention signal maps to a region encompassing approximately residues 10 to 50, counting from the proposed border between the TMD and the tail. Both G1 and G2 were found to be acylated, as shown by incorporation of [3H]palmitate into the viral proteins. By mutational analyses of CD4-G1 chimeras, the sites for palmitylation were mapped to two closely spaced cysteine residues in the G1 tail. Changing either or both of these cysteines to alanine had no effect on the targeting of the chimeric protein to the Golgi complex.
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PMID:A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein. 915 65

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

Egg white of marine turtle Caretta caretta contains a small cationic protein but lacks lysozyme. The protein was sequenced by a combination of sequential Edman degradation, carboxypeptidase digestion, nuclear magnetic resonance (NMR) and electrospray ionization tandem mass spectrometry. The protein contains 36 amino acid residues of which six are half-cysteines. The three-dimensional structure of the protein was deduced from two-dimensional NMR experiments and was observed to be similar to vertebrate beta-defensins. However, disulfide connectivity is C1-C6/C2-C5/C3-C4; different from that of the vertebrate beta-defensins. The protein showed strong antibacterial activity against Escherichia coli and Salmonella typhimurium. The protein also showed significant antiviral activity against an enveloped rhabdovirus, Chandipura virus, which is an emerging human pathogen. This virus is also closely related to the vesicular stomatitis virus, whose growth was also inhibited. This small cationic protein is part of the innate immunity of this organism and replaces lysozyme in the egg. It has the potential to be developed as an antibacterial and antiviral agent.
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PMID:Small cationic protein from a marine turtle has beta-defensin-like fold and antibacterial and antiviral activity. 1670 51

A 2-year-old, spayed female domestic shorthair cat was referred with a history of anorexia and depression of 1 week duration. On physical examination, the cat was lethargic and febrile, with splenomegaly, anisocoria and ulcerative stomatitis. A complete blood count (CBC) and a biochemistry profile showed leukocytosis, numerous blast cells in the peripheral blood, thrombocytopenia, hyperglobulinaemia and a positive test for feline leukaemia virus antigen. A diagnosis of acute myelomonocytic leukaemia was made on the basis of the results of bone marrow cytology, histopathology, and immunochemistry (CD3, CD79a, lysozyme, and myeloperoxidase) tests. Following an unexpected 1-month period of clinical and clinicopathological remission without chemotherapy, the cat relapsed and died 1 week later.
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PMID:Acute myelomonocytic leukaemia with short-term spontaneous remission in a cat. 1849 58