Enamel matrix derivative versus bioactive ceramic filler in the treatment of intrabony defects: 12-month results.

BACKGROUND: This study examined the clinical efficacy of enamel matrix derivative (EMD) and bioactive ceramic filler (BCF) in the treatment of intrabony periodontal defects and evaluated factors influencing the treatment outcome. METHODS: Thirteen chronic periodontitis patients, 41 to 74 years of age, who had two proximal intrabony defects in different jaw quadrants with > or =3 mm vertical radiographic bone loss were selected for this study. After initial therapy, the sites in each patient were randomly assigned to EMD or BCF treatment. Clinical attachment level (CAL), probing depth (PD), tooth mobility (TM), gingival recession (GR), bleeding on probing, and dental plaque were recorded at baseline and at 6 and 12 months. At surgery, the intrabony component was characterized by recording the number of bony walls, distance in millimeters from the buccal crest (BC) to the most apical point of the defect, distance from the cemento-enamel junction (CEJ) to the BC, and the mesio-distal width of the defect at the level of the bony crest. RESULTS: BCF treatment resulted in a significant gain in proximal CAL (P = 0.005) and a reduction in proximal PD at 6 months (P <0.001), but there was no further improvement from 6 to 12 months. Paired comparisons by time for the EMD group revealed a significant reduction in proximal PD at 12 months (P = 0.001), whereas the gain in proximal CAL approached significance (P = 0.056). Mean GR increased significantly from baseline to 6 months in both groups (P = 0.001). Regression analysis revealed that within the EMD group, smoking and TM negatively influenced the gain of attachment, whereas within the BCF group, gingival recession increased with age, increasing CEJ to BC distance, and increasing mesial-distal width of the defect. CONCLUSIONS: The gain in proximal attachment after treating intrabony defects by flap surgery with BCF was significant (P = 0.004) and twice that following treatment with EMD (P = 0.056). Patient and site variables affected the clinical outcome differently.

Diversity and antifungal susceptibility of Norwegian Candida glabrata clinical isolates.

BACKGROUND: Increasing numbers of immunocompromised patients have resulted in greater incidence of invasive fungal infections with high mortality. Candida albicans infections dominate, but during the last decade, Candida glabrata has become the second highest cause of candidemia in the United States and Northern Europe. Reliable and early diagnosis, together with appropriate choice of antifungal treatment, is needed to combat these challenging infections. OBJECTIVES: To confirm the identity of 183 Candida glabrata isolates from different human body sites using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) and VITEK(®)2, and to analyze isolate protein profiles and antifungal susceptibility. The minimum inhibitory concentration (MIC) of seven antifungal drugs was determined for the isolates to elucidate susceptibility. DESIGN: A total of 183 C. glabrata isolates obtained between 2002 and 2012 from Norwegian health-care units were analyzed. For species verification and differentiation, biochemical characterization (VITEK(®)2) and mass spectrometry (MALDI-TOF) were used. MIC determination for seven antifungal drugs was undertaken using E-tests(®). RESULTS: Using VITEK(®)2, 92.9% of isolates were identified as C. glabrata, while all isolates (100%) were identified as C. glabrata using MALDI-TOF. Variation in protein spectra occurred for all identified C. glabrata isolates. The majority of isolates had low MICs to amphotericin B (≤1 mg/L for 99.5%) and anidulafungin (≤0.06 mg/L for 98.9%). For fluconazole, 18% of isolates had MICs >32 mg/L and 82% had MICs in the range ≥0.016 mg/L to ≤32 mg/L. CONCLUSIONS: Protein profiles and antifungal susceptibility characteristics of the C. glabrata isolates were diverse. Clustering of protein profiles indicated that many azole resistant isolates were closely related. In most cases, isolates had highest susceptibility to amphotericin B and anidulafungin. The results confirmed previous observations of high MICs to fluconazole and flucytosine. MALDI-TOF was more definitive than VITEK(®)2 for C. glabrata identification.

Altered healing following mucogingival surgery in a patient with Crohn's disease: a literature review and case report.

BACKGROUND: Crohn's disease is a chronic inflammatory bowel disease characterized by uncertainty in etiology and pathogenesis occasionally with manifestations in oral mucous membranes. This report reviews the literature on Crohn's disease and presents a patient with Crohn's disease on continuous anti-inflammatory and immunosuppressive medication who showed adverse healing response following surgical treatment of gingival recession type defects. METHODS: A 28-year-old male in generally good health apart from his bowel disease requested treatment of multiple maxillary gingival recessions due to esthetic concerns and root sensitivity. Following oral hygiene instruction, 3 coronally advanced flap procedures were performed in the maxillary anterior region to cover the defects. In 2 of the surgical areas, the exposed root surfaces were treated by ethylenediaminetetraacetic acid (EDTA) in combination with enamel matrix derivative (EMD) before coronally positioning the buccal flap. Postoperatively, chlorhexidine gluconate was used for oral hygiene control. RESULTS: The first surgical procedure, performed as a coronally advanced flap, showed delayed and altered healing. Two weeks postoperatively, the flapped tissue remained intensely red and swollen. In the following 2 surgical sites where EDTA and EMD were applied the healing was uneventful. Differences in immediate tissue response, however, did not influence the 3-month treatment outcome with respect to root coverage. CONCLUSIONS: Patients with Crohn's disease on recommended systemic medications may show a delayed and altered wound healing indicating that periodontal surgery must be closely monitored. Treatment planning should take into account the potential wound healing promoting effects of enamel matrix derivative as well as adverse healing effects of chlorhexidine gluconate administration.

Characterization of strains of Vibrio splendidus and V. tapetis isolated from corkwing wrasse Symphodus melops suffering vibriosis.

Two vibrio bacteria pathogenic to the corkwing wrasse Symphodus melops were isolated. Vibriosis-inducing strain LP1 was isolated as the dominanting bacterium in kidney samples of dead and moribund wrasse from a population suffering vibriosis and high daily mortality in 1998 on the Norwegian west coast. The other vibriosis-inducing strain, LP2, was isolated from wrasse captured the following year. Re-infection experiments have confirmed that these strains cause vibriosis in corkwing wrasse. Both strains were typical vibrios sharing the traits of fermentative Gram-negative curved rods with motility and a positive oxidase reaction. Detailed biochemical and genetic characterisation revealed a close affiliation to known species of the marine environment. The first isolate, LP1, is a form of the ubiquitous seawater organism Vibrio splendidus, while the second isolate, LP2, is closely related to V. tapetis (previously only known as the brown ring disease agent in clams). Identification of the new wrasse pathogens V. splendidus LP1 and V. tapetis LP2 is facilitated by break points observed in this study.

Three independent techniques localize expression of transcript afp-11 and its bioactive peptide products to the paired AVK neurons in Ascaris suum: in situ hybridization, immunocytochemistry, and single cell mass spectrometry.

We utilized three independent techniques, immunocytochemistry (ICC), single cell mass spectrometry (MS), and in situ hybridization (ISH), to localize neuropeptides and their transcripts in the nervous system of the nematode Ascaris suum . AF11 (SDIGISEPNFLRFa) is an endogenous peptide with potent paralytic effects on A. suum locomotory behavior. A highly specific antibody to AF11 showed robust immunostaining for AF11 in the paired AVK neurons in the ventral ganglion. We traced the processes from the AVK neurons into the ventral nerve cord and identified them as ventral cord interneurons. MS and MS/MS of single dissected AVKs detected AF11, two previously characterized peptides (AF25 and AF26), seven novel sequence-related peptides, including several sharing a PNFLRFamide C-terminus, and peptide NY, a peptide with an unrelated sequence. Also present in a subset of AVKs was AF2, a peptide encoded by the afp-4 transcript. By sequencing the afp-11 transcript, we discovered that it encodes AF11, all the AF11-related peptides detected by MS in AVK, and peptide NY. ISH detected the afp-11 transcript in AVK neurons, consistent with other techniques. ISH did not detect afp-11 in the ALA neuron, although both ICC and MS found AF11 in ca. 30% of ALAs. All 10 AF11-related peptides reduced acetylcholine-induced muscle contraction, but they differed in their rate of reversal of inhibition after removal of the peptide.

Mapping neuropeptide expression by mass spectrometry in single dissected identified neurons from the dorsal ganglion of the nematode Ascaris suum.

We have developed a method for dissecting single neurons from the nematode Ascaris suum, in order to determine their peptide content by mass spectrometry (MS). In this paper, we use MALDI-TOF MS and tandem MS to enumerate and sequence the peptides present in the two neurons, ALA and RID, that comprise the dorsal ganglion. We compare the peptide content determined by MS with the results of immunocytochemistry and in situ hybridization of previously isolated peptides AF2, AF8 and 6 peptides encoded by the afp-1 transcript. We find complete agreement between the three techniques, which validates single neuron MS as a method for peptide localization. We also discovered and sequenced 6 novel peptides in the ALA neuron. Cloning of cDNAs and database searching of Genomic Survey Sequences showed that transcript afp-12 encodes peptide AF36 (VPSAADMMIRFamide), and afp-13 encodes AF19 (AEGLSSPLIRFamide), AF34 (DSKLMDPLIRFamide), AF35 (DPQQRIVTDETVLRFamide), and 3 non-amidated peptides (PepTT, PepTL, and PepGE). We have found no similarities with reported peptide expression in the nematode Caenorhabditis elegans. This method promises to be ideally suited for determining the peptide content of each of the 298 neurons in the nervous system of this nematode.