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1.
Int Endod J ; 50(2): 117-125, 2017 Feb.
Article in English | MEDLINE | ID: mdl-26715408

ABSTRACT

AIM: To assess the outcome of mineral trioxide aggregate (MTA) complete pulpotomy in permanent teeth with carious exposures. METHODOLOGY: Fifty-two permanent molar teeth with fully developed roots and vital pulps in 43 patients aged 11-51 years were included. Preoperative pulpal and periapical diagnosis was established. After informed consent, each tooth was anaesthetized, isolated with dental dam and disinfected with 5% NaOCl before caries excavation; subsequently, a full pulpotomy was performed. Haemostasis was achieved, and Grey MTA (Angelus, Londrina, Brazil) was placed as the pulpotomy agent; a moist cotton pellet was placed, and the tooth was temporized with the intermediate restorative material (IRM). Permanent restorations were placed 1 week later if the tooth was asymptomatic, and a postoperative periapical radiograph was taken. Clinical and radiographic evaluation was completed at 3 months, 6 months, 1 year and 3 years postoperatively. RESULTS: Clinical signs and symptoms suggestive of irreversible pulpitis were established in 44/52 teeth, and periapical rarefaction was present in 14 teeth. Immediate failure occurred in one tooth. The recall rate ranged from 92% at 3 months to 80.3% at 3 years, with an overall 100% clinical and 97.5% radiographic success during the first year, and 92.7% success at 3 years. All cases with periapical rarefaction were associated with improvement in the periapical index (PAI) score. Two cases had new periapical rarefaction associated with dislodgment of the permanent restoration. A hard tissue barrier was detected radiographically in 5 cases and canal narrowing in 7 cases. CONCLUSION: MTA full pulpotomy was a successful treatment option for cariously exposed pulps in mature permanent molar teeth.


Subject(s)
Aluminum Compounds , Calcium Compounds , Dental Caries/surgery , Oxides , Pulpotomy/methods , Silicates , Adolescent , Adult , Child , Drug Combinations , Humans , Middle Aged
2.
Int J Biomed Sci ; 10(4): 236-42, 2014 Dec.
Article in English | MEDLINE | ID: mdl-25598753

ABSTRACT

Tacazzea apiculata is used by traditional medical practitioners for the treatment of wide range of diseases. The current work investigated the hypoglycemic and antioxidant properties of Tacazzea apiculata Oliv. on alloxan induced diabetes mellitus. Five groups (n=10) of rats were fed on commercial diet. The rats were divided into Group 1 (NUT) as non-diabetic and untreated, group 2 (NDT) as non-diabetic and treated, group 3 (DT) diabetic and treated. Group 4 (DUT) as diabetic and untreated. Group five (CP) were diabetic treated with Chlorpropamide, a drug used in the management of diabetic mellitus, with no known antioxidant property. Diabetic induction was done by intra-peritoneal injection of 100 mg/kg b. wt with alloxan. Fasting blood glucose was estimated seven days after induction to determine the severity of glucose elevation among the induced groups. Methanolic extract of T. apiculata leaf was administered to alloxan induced diabetic and non-diabetic control rats at 100mg/kg body weight for four weeks and blood glucose estimated on weekly basis. Malondialdehyde level was also estimated in the sera of the rats. Blood glucose level was monitored for additional 2 weeks post treatment. The results indicated that the extracts possess significant hypoglycemic effect on the diabetic rats (DT) having the mean glucose of (95.2 ± 9.12 mg/dl) compared to the diabetic untreated control group (DUT) with a mean glucose of (238.91 ± 4.42 mg/dl, p<0.05). The effect was sustained even on withdrawal of the extracts for two weeks. This was accompanied by a progressive increase in weight among all treated diabetic rats and non diabetic treated (DT and NDT) compared with diabetic untreated control rat (DUT) (p<0.05). A raised level in malondialdehyde was also observed among the diabetic rat prior to treatment and significantly decreased after the treatment. In conclusion the research demonstrated the hypoglycaemic and antioxidant potential of methanolic leaf extract of T. apiculata in alloxan induced rats.

3.
Appl Biochem Biotechnol ; 81(3): 205-17, 1999 Sep.
Article in English | MEDLINE | ID: mdl-15304777

ABSTRACT

Lipase from Candida rugosa was immobilized by entrapment on poly(N-vinyl- 2-pyrrolidone-co-2-hydroxyethyl methacrylate) (poly[VP-co-HEMA]) hydrogel, and divinylbenzene was the crosslinking agent. The immobilized enzymes were used in the esterification reaction of oleic acid and butanol in hexane. The activities of the immobilized enzymes and the leaching ability of the enzyme from the support with respect to the different compositions of the hydrogels were investigated. The thermal, solvent, and storage stability of the immobilized lipases was also determined. Increasing the percentage of composition of VP from 0 to 90, which corresponds to the increase in the hydrophilicity of the hydrogels, increased the activity of the immobilized enzyme. Lipase immobilized on VP(%):HEMA(%) 90:10 exhibited the highest activity. Lipase immobilized on VP(%):HEMA(%) 50:50 showed the highest thermal, solvent, storage, and operational stability compared to lipase immobilized on other compositions of hydrogels as well as the native lipase.

5.
Mol Reprod Dev ; 47(3): 341-50, 1997 Jul.
Article in English | MEDLINE | ID: mdl-9170114

ABSTRACT

When the plasma membranes of caput and cauda epididymal spermatozoa of hamster were evaluated for their ability to undergo phosphorylation, a differential phosphorylation of the membrane proteins was observed. In the plasma membranes of the caput epididymal spermatozoa (immature), twelve proteins were phosphorylated (100, 76, 67, 65, 55, 52, 47, 42, 38, 32, 30, and 20 kD), whereas in the plasma membranes of cauda epididymal spermatozoa (mature), a differential phosphorylation pattern was observed with respect to the 94, 67, 52, and 47 kD proteins. The 94 kD protein was found to be phosphorylated and the 67 kD protein was found to be not phosphorylated in cauda spermatozoal plasma membrane (Cd SPM) in contrast to this protein in caput spermatozoal plasma membrane (Cpt SPM). The 52 and 47 kD proteins were also more intensely phosphorylated in Cd SPM than Cpt SPM. The 100 kilodalton protein, although present in both Cpt and Cd sperm plasma membranes, was found to be phosphorylated at the tyrosine residues only in the Cd SPM, as indicated by the Western blot using antiphosphotyrosine antibody. Further, a differential phosphorylation of the substrate proteins present in the Cpt and Cd SPM was seen when Mg2+ in the assay buffer was replaced by other divalent cations. For instance, Zn2+ stimulated the phosphorylation of an 85 kD protein in cauda SPM and not in the caput SPM and Ca2+ stimulated the phosphorylation of a 76 kD protein only in the cauda SPM. The phosphoproteins in both the plasma membranes were found to be phosphorylated predominantly at the tyrosine residue. The differential phosphorylation at a 100 kD protein at tyrosine in the Cd SPM (Western blot), which is absent in the immature Cpt SPM, also indicated that certain proteins in the hamster spermatozoa are phosphorylated in a maturation-specific manner.


Subject(s)
Membrane Proteins/metabolism , Protein Kinases/metabolism , Spermatozoa/metabolism , Acrosome/metabolism , Amino Acids/analysis , Animals , Calcium/metabolism , Cell Membrane/metabolism , Cricetinae , Enzyme Inhibitors/pharmacology , Epididymis/cytology , Fluorescent Antibody Technique, Indirect , Male , Phosphorylation , Protein Kinase Inhibitors , Spermatogenesis , Zinc/metabolism
6.
FEBS Lett ; 396(2-3): 123-6, 1996 Nov 04.
Article in English | MEDLINE | ID: mdl-8914971

ABSTRACT

Acrosomal membranes isolated from the caput and cauda epididymal spermatozoa of hamster exhibited protein kinase activity and the endogenous protein substrates that were phosphorylated in the acrosomal membranes of caput and cauda spermatozoa were not all the same. The kinase activity was identified as a cAMP independent type and the use of specific stimulators and inhibitors indicated that the activity was not due to casein kinase, protein kinase A or protein kinase C but due to a tyrosine specific protein kinase that was not inhibited by Genistein. Phosphotyrosine was identified as the predominant phosphorylated residue in the proteins.


Subject(s)
Acrosome/enzymology , Protein-Tyrosine Kinases/metabolism , 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine/pharmacology , Animals , Cricetinae , Cyclic AMP/pharmacology , Enzyme Inhibitors/pharmacology , Epididymis , Genistein , Heparin/pharmacology , Isoflavones/pharmacology , Male , Membrane Proteins/metabolism , Phosphorylation , Phosphotyrosine/metabolism , Protein-Tyrosine Kinases/antagonists & inhibitors , Spermidine/pharmacology , Spermine/pharmacology
7.
Cell Mol Biol (Noisy-le-grand) ; 41(4): 555-63, 1995 Jun.
Article in English | MEDLINE | ID: mdl-7549792

ABSTRACT

Human endometria were analysed for the synthesis and secretion of proteins following short term culture of human endometrial tissue in the presence of 35S-methionine. During the menstrual cycle secretory proteins of molecular weight (MW) 30, 35, 45, 50, 59, 74, 97 and 135 kDa showed increased synthesis during the proliferative phase. The synthesis of these proteins decreased in the secretory phase but the induction of a 26 kDa protein in the early secretory phase and a 28 kDa protein in the late secretory phase was observed. The synthesis of the above secretory proteins of the human endometrium was also confirmed by two dimensional gel electrophoresis. Further, the results demonstrated that the secretory protein profile of human decidual endometria and endometria exhibiting irregular ripening was identical to that of normal secretory phase endometria. But, endometria exhibiting hyperplasia, cystic glandular hyperplasia and adenomatous glandular hyperplasia presented similar secretory protein profiles which were identical with the secretory protein profile of normal proliferative phase endometrium. The present study confirms that a number of proteins are synthesised by the human endometrium during the normal menstrual cycle and during pregnancy. It also provides data for the first time on the proteins secreted by the endometria exhibiting irregular ripening, hyperplasia, cystic glandular hyperplasia and adenomatous glandular hyperplasia.


Subject(s)
Endometrial Hyperplasia/metabolism , Endometrium/metabolism , Menstrual Cycle/metabolism , Protein Biosynthesis , Adult , Electrophoresis, Gel, Two-Dimensional , Embryo Implantation , Endometrium/physiopathology , Female , Humans , Pregnancy , Proteins/metabolism
8.
J Steroid Biochem Mol Biol ; 52(6): 587-94, 1995 Jun.
Article in English | MEDLINE | ID: mdl-7779763

ABSTRACT

Changes in the concentrations of phosphorus containing metabolites were monitored by 31P NMR in the uteri of hamsters during the estrous cycle. Concentrations of phosphocreatine (PCr) and ATP were significantly increased in estrus animals compared to diestrus animals. Concentrations of these metabolites were also increased in immature female hamsters and ovariectomized (OVX) adult hamsters treated with estradiol indicating that estradiol was responsible for this effect. However, the steroid hormones progesterone and testosterone did not increase the concentrations of the phosphorus containing metabolites. Further, immature female hamsters also following treatment with estradiol showed an initial decline in phosphomonoester (PME), PCr, ATP and inorganic phosphate but by 24 h of treatment the concentrations returned to control levels. The NMR study also revealed that the intracellular pH of the hamster uterus was around 7.4 all through the estrous cycle.


Subject(s)
Estrus/metabolism , Phosphorus/metabolism , Uterus/metabolism , Adenosine Triphosphate/metabolism , Animals , Cricetinae , Estradiol/pharmacology , Female , Hydrogen-Ion Concentration , Intracellular Fluid/metabolism , Magnetic Resonance Spectroscopy , Mesocricetus , Ovariectomy , Phosphates/metabolism , Phosphocreatine/metabolism , Progesterone/pharmacology , Sexual Maturation/physiology , Testosterone/pharmacology , Uterus/drug effects
9.
J Steroid Biochem Mol Biol ; 51(1-2): 107-14, 1994 Oct.
Article in English | MEDLINE | ID: mdl-7947344

ABSTRACT

The present study was directed towards identification of proteins synthesized and secreted by the cervix, uterus and oviduct of immature hamsters and by the uterus of ovariectomized adult hamsters. Hamsters were treated with estradiol, progesterone or testosterone for 3 consecutive days after which the tissues were incubated in vitro and [35S]methionine labelled proteins were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. The results demonstrate a great degree of similarity between the proteins synthesized and secreted by the cervix, uterus and oviduct of hamsters. Treatment of hamsters with estradiol consistently increased the synthesis of a 60 kDa protein in the cervix, uterus and oviduct. Further, estradiol also consistently suppressed the synthesis of a 14, 30 and 72 kDa protein in the uterus but not in the cervix and oviduct. In the cervix, in addition to the 60 kDa protein estradiol also induced the synthesis of two other proteins (a 38 and 56 kDa protein). Testosterone and progesterone did not induce or suppress the synthesis of the secretory proteins in the hamster cervix, uterus and oviduct. In hamster the 60 kDa protein could serve as a marker of gene expression following hormone action.


Subject(s)
Cervix Uteri/drug effects , Fallopian Tubes/drug effects , Gonadal Steroid Hormones/pharmacology , Proteins/metabolism , Uterus/drug effects , Animals , Cervix Uteri/metabolism , Cricetinae , Estradiol/pharmacology , Fallopian Tubes/metabolism , Female , Mesocricetus , Molecular Weight , Organ Culture Techniques , Organ Size , Progesterone/pharmacology , Protein Biosynthesis , Proteins/chemistry , Testosterone/pharmacology , Uterus/metabolism
11.
Biochem J ; 215(1): 117-22, 1983 Oct 01.
Article in English | MEDLINE | ID: mdl-6626170

ABSTRACT

Apomyoglobin was reconstituted with deuterohaem derivatives under various conditions. The fraction of disordered component, which is characterized by a 180 degree rotation of the haem group, for the various preparations was determined by n.m.r. spectroscopy. By using the procedures described, it was shown that the fraction of disordered component is minimized if the reconstitution is carried out with high-spin ferric haem derivatives within an experimentally determined optimum pH range of 8-9.5. Use of low-spin derivatives in either the ferrous or ferric forms leads to substantial increases in the fraction of disordered form. Attempted removal of the disordered form by selective oxidation and chromatographic purification was not effective.


Subject(s)
Heme/analysis , Myoglobin/analogs & derivatives , Chromatography , Hemin/analogs & derivatives , Hydrogen-Ion Concentration , Magnetic Resonance Spectroscopy , Myoglobin/isolation & purification , Protein Conformation
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