scholarly journals Promising Role of Calcium Hypochlorite as a Disinfectant: An in vitro Evaluation Regarding its Effect on Type V Dental Stone

2012 ◽  
Vol 13 (6) ◽  
pp. 856-866
Author(s):  
Prasanta Kumar Swain ◽  
Sharanbasappa C Nagaral ◽  
Pawan Kumar Kamalapurker ◽  
Ravishankar Damineni
Keyword(s):  
Tensile Strength ◽  
Bacillus Subtilis ◽  
Deleterious Effect ◽  
Strength Testing ◽  
Calcium Hypochlorite ◽  
Resistant Species ◽  
Type V ◽  
Mixing Water

ABSTRACT Aim The current study has been chosen to evaluate the efficacy of calcium hypochlorite as a disinfecting additive for the gypsum products and its effect on compressive and tensile strength of the set material. It is hypothesized that, the addition of calcium hypochlorite to type V dental stone in sufficient quantity to disinfect the material would have no deleterious effect on compressive or tensile strength. Materials and methods Total of 160 samples made up of type V dental stone were divided broadly into two groups of 80 samples each for the sake of compressive and tensile strength testing in dry and wet conditions: Out of each group, 10 samples without addition of any disinfectant (0% calcium hypochlorite) was compared with other group of 30 samples after adding disinfectant, i.e. each subgroup containing 10 samples each (0.5, 1.0 and 1.5% calcium hypochlorite). Conclusion Within limitations of this in vitro study it is assumed to prepare type V dental stone that contains a disinfectant, has adequate compressive strength and tensile strength, and can significantly act against a resistant species like Bacillus subtilis. Clinical significance When calcium hypochlorite was added to dental stone, extra mixing water was required to produce a material of nearly same pouring consistency. The samples, which were put to microbiological tests, showed effective action of disinfectant on Bacillus subtilis. No deleterious effect on compressive or tensile strength could be found after putting the selected samples with calcium hypochlorite. How to cite this article Swain PK, Nagaral SC, Kamalapurker PK, Damineni R. Promising Role of Calcium Hypochlorite as a Disinfectant: An in vitro Evaluation Regarding its Effect on Type V Dental Stone. J Contemp Dent Pract 2012;13(6):856-866.

Coordinate expression of secretory phospholipase A2 and cyclooxygenase-2 in activated human keratinocytes

2000 ◽  
Vol 278 (4) ◽  
pp. C822-C833 ◽  
Author(s):  
Krystyna E. Rys-Sikora ◽  
Raymond L. Konger ◽  
John W. Schoggins ◽  
Rama Malaviya ◽  
Alice P. Pentland
Keyword(s):  
Wound Repair ◽  
Human Keratinocytes ◽  
Plating Density ◽  
Coordinate Expression ◽  
Cox 2 ◽  
Type V ◽  
In Vitro Wounding

PGE2 levels are altered in human epidermis after in vivo wounding; however, mechanisms modulating PGE2 production in activated keratinocytes are unclear. In previous studies, we showed that PGE2 is a growth-promoting autacoid in human primary keratinocyte cultures, and its production is modulated by plating density, suggesting that regulated PGE2 synthesis is an important component of wound healing. Here, we examine the role of phospholipase A2(PLA2) and cyclooxygenase (COX) enzymes in modulation of PGE2 production. We report that the increased PGE2 production that occurs in keratinocytes grown in nonconfluent conditions is also observed after in vitro wounding, indicating that similar mechanisms are involved. This increase was associated with coordinate upregulation of both COX-2 and secretory PLA2 (sPLA2) proteins. Increased sPLA2 activity was also observed. By RT-PCR, we identified the presence of type IIA and type V sPLA2, along with the M-type sPLA2 receptor. Thus the coordinate expression of sPLA2 and COX-2 may be responsible for the increased prostaglandin synthesis in activated keratinocytes during wound repair.

scholarly journals In Vivo Effect of Mutations at the PRPP Binding Site of the Bacillus subtilis Purine Repressor

2003 ◽  
Vol 185 (22) ◽  
pp. 6728-6731 ◽  
Author(s):  
Pekka Rappu ◽  
Terhi Pullinen ◽  
Pekka Mäntsälä
Keyword(s):  
Bacillus Subtilis ◽  
Binding Site ◽  
Binding Motif

ABSTRACT The Bacillus subtilis PurR mediates adenine repression and guanosine induction of purA. PRPP inhibits binding of PurR to DNA in vitro. Mutations in the PRPP binding motif of PurR caused strong repression regardless of purine exclusions or additions, establishing the role of PRPP as regulator of PurR.

scholarly journals Biochemical and Mutational Analyses of AcuA, the Acetyltransferase Enzyme That Controls the Activity of the Acetyl Coenzyme A Synthetase (AcsA) in Bacillus subtilis

2008 ◽  
Vol 190 (14) ◽  
pp. 5132-5136 ◽  
Author(s):  
Jeffrey G. Gardner ◽  
Jorge C. Escalante-Semerena
Keyword(s):  
Bacillus Subtilis ◽  
Coenzyme A ◽  
Effective Means ◽  
Wild Type ◽  
Modification System ◽  
Vitro Assay ◽  
Acetyl Coenzyme A ◽  
Acetyl Coenzyme

ABSTRACT The acuABC genes of Bacillus subtilis comprise a putative posttranslational modification system. The AcuA protein is a member of the Gcn5-related N-acetyltransferase (GNAT) superfamily, the AcuC protein is a class I histone deacetylase, and the role of the AcuB protein is not known. AcuA controls the activity of acetyl coenzyme A synthetase (AcsA; EC 6.2.1.1) in this bacterium by acetylating residue Lys549. Here we report the kinetic analysis of wild-type and variant AcuA proteins. We contrived a genetic scheme for the identification of AcuA residues critical for activity. Changes at residues H177 and G187 completely inactivated AcuA and led to its rapid turnover. Changes at residues R42 and T169 were less severe. In vitro assay conditions were optimized, and an effective means of inactivating the enzyme was found. The basic kinetic parameters of wild-type and variant AcuA proteins were obtained and compared to those of eukaryotic GNATs. Insights into how the isolated mutations may exert their deleterious effect were investigated by using the crystal structure of an AcuA homolog.

scholarly journals The structure of the Myo4p globular tail and its function in ASH1 mRNA localization

2010 ◽  
Vol 189 (3) ◽  
pp. 497-510 ◽  
Author(s):  
Alexander Heuck ◽  
Ingrid Fetka ◽  
Daniel N. Brewer ◽  
Daniela Hüls ◽  
Mary Munson ◽  
...  
Keyword(s):  
Mrna Localization ◽  
Surface Patch ◽  
X Ray ◽  
Membrane Tethering ◽  
Dividing Cells ◽  
Dependent Transport ◽  
Type V ◽  
Ash1 Mrna

Type V myosin (MyoV)–dependent transport of cargo is an essential process in eukaryotes. Studies on yeast and vertebrate MyoV showed that their globular tails mediate binding to the cargo complexes. In Saccharomyces cerevisiae, the MyoV motor Myo4p interacts with She3p to localize asymmetric synthesis of HO 1 (ASH1) mRNA into the bud of dividing cells. A recent study showed that localization of GFP-MS2–tethered ASH1 particles does not require the Myo4p globular tail, challenging the supposed role of this domain. We assessed ASH1 mRNA and Myo4p distribution more directly and found that their localization is impaired in cells expressing globular tail–lacking Myo4p. In vitro studies further show that the globular tail together with a more N-terminal linker region is required for efficient She3p binding. We also determined the x-ray structure of the Myo4p globular tail and identify a conserved surface patch important for She3p binding. The structure shows pronounced similarities to membrane-tethering complexes and indicates that Myo4p may not undergo auto-inhibition of its motor domain.

scholarly journals Role of PhoP∼P in Transcriptional Regulation of Genes Involved in Cell Wall Anionic Polymer Biosynthesis in Bacillus subtilis

1998 ◽  
Vol 180 (15) ◽  
pp. 4007-4010 ◽  
Author(s):  
Ying Qi ◽  
F. Marion Hulett
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Teichoic Acid ◽  
Acid Synthesis ◽  
In Vitro Transcription ◽  
Anionic Polymer ◽  
Transcription System ◽  
Teichuronic Acid

ABSTRACT tagA, tagD, and tuaA operons are responsible for the synthesis of cell wall anionic polymer, teichoic acid, and teichuronic acid, respectively, in Bacillus subtilis. Under phosphate starvation conditions, teichuronic acid is synthesized while teichoic acid synthesis is inhibited. Expression of these genes is controlled by PhoP-PhoR, a two-component system. It has been proposed that PhoP∼P plays a key role in the activation oftuaA and the repression of tagA andtagD. In this study, we demonstrated the role of PhoP∼P in the switch process from teichoic acid synthesis to teichuronic acid synthesis, by using an in vitro transcription system. The results indicate that PhoP∼P is sufficient to repress the transcription of the tagA and tagD promoters and also to activate the transcription of the tuaA promoter.

scholarly journals Phosphorylation and RsbX-Dependent Dephosphorylation of RsbR in the RsbR-RsbS Complex of Bacillus subtilis

2004 ◽  
Vol 186 (20) ◽  
pp. 6830-6836 ◽  
Author(s):  
Chien-Cheng Chen ◽  
Michael D. Yudkin ◽  
Olivier Delumeau
Keyword(s):  
Bacillus Subtilis ◽  
Kinase Activity ◽  
Positive Regulator ◽  
Enhanced Activity

ABSTRACT In the pathway that controls σB activity, the RsbR-RsbS complex plays an important role by trapping RsbT, a positive regulator of σB of Bacillus subtilis. We have proposed that at the onset of stress, RsbR becomes phosphorylated, resulting in an enhanced activity of RsbT towards RsbS. RsbT is then free to interact with and activate RsbU, which in turn ultimately activates σB. In this study with purified proteins, we used mutant RsbR proteins to analyze the role of its phosphorylatable threonine residues. The results show that the phosphorylation of either of the two RsbT-phosphorylatable threonine residues (T171 and T205) in RsbR enhanced the kinase activity of RsbT towards RsbS. However, it appeared that RsbT preferentially phosphorylates T171. We also present in vitro evidence that identifies RsbX as a potential phosphatase for RsbR T205.

scholarly journals Role of Spore Coat Proteins in the Resistance of Bacillus subtilis Spores to Caenorhabditis elegans Predation

2008 ◽  
Vol 190 (18) ◽  
pp. 6197-6203 ◽  
Author(s):  
Maria-Halima Laaberki ◽  
Jonathan Dworkin
Keyword(s):  
Bacillus Subtilis ◽  
Caenorhabditis Elegans ◽  
Spore Coat ◽  
Coat Proteins ◽  
Host Interaction ◽  
Wide Range ◽  
In The Wild

ABSTRACT Bacterial spores are resistant to a wide range of chemical and physical insults that are normally lethal for the vegetative form of the bacterium. While the integrity of the protein coat of the spore is crucial for spore survival in vitro, far less is known about how the coat provides protection in vivo against predation by ecologically relevant hosts. In particular, assays had characterized the in vitro resistance of spores to peptidoglycan-hydrolyzing enzymes like lysozyme that are also important effectors of innate immunity in a wide variety of hosts. Here, we use the bacteriovorous nematode Caenorhabditis elegans, a likely predator of Bacillus spores in the wild, to characterize the role of the spore coat in an ecologically relevant spore-host interaction. We found that ingested wild-type Bacillus subtilis spores were resistant to worm digestion, whereas vegetative forms of the bacterium were efficiently digested by the nematode. Using B. subtilis strains carrying mutations in spore coat genes, we observed a correlation between the degree of alteration of the spore coat assembly and the susceptibility to the worm degradation. Surprisingly, we found that the spores that were resistant to lysozyme in vitro can be sensitive to C. elegans digestion depending on the extent of the spore coat structure modifications.

scholarly journals Interaction of Bacillus subtilis CsaA with SecA and precursor proteins

2000 ◽  
Vol 348 (2) ◽  
pp. 367-373 ◽  
Author(s):  
Jörg P. MÜLLER ◽  
Jörg OZEGOWSKI ◽  
Stefan VETTERMANN ◽  
Jelto SWAVING ◽  
Karel H. M. VAN WELY ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Specific Interaction ◽  
Membrane Vesicles ◽  
Protein Export ◽  
E Coli ◽  
Bacterium Bacillus Subtilis ◽  
Bacterium Bacillus

CsaA from the Gram-positive bacterium Bacillus subtilis has been identified previously as a suppressor of the growth and protein-export defect of Escherichia coli secA(Ts) mutants. CsaA has chaperone-like activities in vivo and in vitro. To examine the role of CsaA in protein export in B. subtilis, expression of the csaA gene was repressed. While export of most proteins remained unaffected, export of at least two proteins was significantly reduced upon CsaA depletion. CsaA co-immunoprecipitates and co-purifies with the SecA proteins of E. coli and B. subtilis, and binds the B. subtilis preprotein prePhoB. Purified CsaA stimulates the translocation of prePhoB into E. coli membrane vesicles bearing the B. subtilis translocase, whereas it interferes with the SecB-mediated translocation of proOmpA into membrane vesicles of E. coli. The specific interaction with the SecA translocation ATPase and preproteins suggests that CsaA acts as a chaperone that promotes the export of a subset of preproteins in B. subtilis.

The Role of an Adhesive (Histoacryl) in Tendon Repair

1992 ◽  
Vol 17 (5) ◽  
pp. 544-549 ◽  
Author(s):  
I. A. TRAIL ◽  
E. S. POWELL ◽  
J. NOBLE ◽  
S. CRANK
Keyword(s):  
Tensile Strength ◽  
Stainless Steel ◽  
Tendon Repair ◽  
Mechanical Analysis ◽  
In Vitro Experiments

Two in vitro experiments have been done comparing various techniques of tendon repair. These include repairs using an adhesive, 2-butyl cyanoacrylate (Histoacryl), and repairs by the modified Kessler technique, using 4/0 braided polyester and 4/0 stainless steel. Mechanical analysis has shown that by replacing the circumferential suture of a modified Kessler tendon repair with Histoacryl, the tensile strength of the repair and the force needed to produce a gap can be increased by 30% to 40%. This improvement was statistically significant ( P < 0.05).

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