RESUMO
OBJECTIVE: This study was designed to evaluate the transmucosal healing response of implants placed with the junction of the smooth surfaces, either crestal or subcrestal, into simulated extraction defects after healing periods of 1 and 3 months. MATERIALS AND METHODS: A total of 23 Straumann SP v3.3 mm NN, SLA 10 mm implants were placed in the mandibular premolar regions of three greyhound dogs 3 months after the teeth were removed. Five control implants were placed at the crestal bone level, and test implants with surgically created peri-implant defects of 1.25 mm wide x 5 mm depth were placed either at the crestal (nine implants) or at the 2 mm subcrestal (nine implants) bone level. Implants on the right side were placed 1 month before the dogs were sacrificed, and implants on the left side were placed 3 months before sacrifice. All dogs had daily plaque control following surgery and were sacrificed 3 months after implant placement for histological and histometric analyses. RESULTS: Mesial-distal ground sections of the control and test implant specimens showed a greater %BIC in the coronal defect region after 3 months of healing. This healing response was incomplete for the test implants compared with the control implants after a 1-month healing period. The histometric measurements for test implants placed at the crestal bone level or 2 mm subcrestal with surgically created peri-implant defects were more coronal or closer to the implant margin compared with the control implants. Additionally, the degree of osseointegration between the newly formed bone and the implant surface was similar between the test implants. CONCLUSION: Peri-implant defects of 1.25 mm width healed with spontaneous bone regeneration around implants placed transmucosally at crestal or 2 mm subcrestal with a high degree of osseointegration after a 3-month healing period.
Assuntos
Implantação Dentária Endóssea/métodos , Mandíbula/cirurgia , Mucosa Bucal/fisiologia , Cicatrização/fisiologia , Animais , Implantes Dentários , Cães , Modelos Animais , Osseointegração/fisiologia , Fatores de Tempo , Extração DentáriaRESUMO
Ethnobotany/ethnopharmacology has contributed to the discovery of many important plant-derived drugs. Field explorations to seek and document indigenous/traditional medical knowledge (IMK/TMK), and/or the biodiversity with which the IMK/TMK is attached, and its conversion into a commercialized product is known as bioprospecting or biodiversity prospecting. When performed in a large-scale operation, the effort is referred to as mass bioprospecting. Experiences from the mass bioprospecting efforts undertaken by the United States National Cancer Institute, the National Cooperative Drug Discovery Groups (NCDDG) and the International Cooperative Biodiversity Groups (ICBG) programs demonstrate that mass bioprospecting is a complex process, involving expertise from diverse areas of human endeavors, but central to it is the Memorandum of Agreement (MOA) that recognizes issues on genetic access, prior informed consent, intellectual property and the sharing of benefits that may arise as a result of the effort. Future mass bioprospecting endeavors must take heed of the lessons learned from past and present experiences in the planning for a successful mass bioprospecting venture.
Assuntos
Etnobotânica , Etnofarmacologia , Propriedade Intelectual , Conservação dos Recursos Naturais , Etnobotânica/ética , Etnobotânica/tendências , Etnofarmacologia/ética , Etnofarmacologia/tendências , Humanos , Medicina TradicionalRESUMO
This study was designed to determine the effects of the A1-receptor selective agonist N6-cyclopentyladenosine (CPA), and the A2-selective agonist, 2-p-(2-carboxyethyl)-phenethylamino-5'-N-ethylcarboxamidoadenosine-hydrochloride (CGS-21680) on consumptive behaviour and body temperature in rats in relation to the non-selective A1/A2 adenosine agonist, N-ethylcarboxamidoadenosine (NECA), and to morphine. It was shown that two subcutaneous injections of 0.1 and 0.3 mg kg(-1) CPA caused a similar decrease in food consumption to NECA (2 x 0.03 mg kg(-1)) and morphine (2 x 10 mg kg(-1)). However, two doses of 0.03 mg kg(-1) CPA and 0.1 and 0.3 mg kg(-1)CGS-21680 enhanced feeding. These effects were not directly correlated to faecal output at all doses of the selective agonists, as NECA and morphine induced constipation. The doses of CPA and 0.1 and 0.3 mg kg(-1) of CGS-21680 enhanced water consumption, as did NECA, but not morphine. The stimulation of drinking by CPA was not absolutely associated with diuresis. Instead, urine output was reduced by 0.03 and 0.1 mg kg(-1) and increased by 0.3 mg kg(-1). CGS-21680 at 0.1 and 0.3 mg kg(-1) and NECA also induced diuresis, which was opposite to the effect of morphine. CPA and CGS-21680 both caused significant dose-dependent decreases in body temperature after the two-injection treatment, but their effects were significantly less after 36 h when four doses had been administered. The study indicates that highly selective A1 and A2A adenosine agonists might have the ability to interfere with consumptive behaviour, induce constipation, affect renal function and to lower body temperature.
Assuntos
Adenosina/análogos & derivados , Adenosina/farmacologia , Temperatura Corporal/efeitos dos fármacos , Ingestão de Líquidos/efeitos dos fármacos , Comportamento Alimentar/efeitos dos fármacos , Fenetilaminas/farmacologia , Agonistas do Receptor Purinérgico P1 , Adenosina-5'-(N-etilcarboxamida)/farmacologia , Animais , Defecação/efeitos dos fármacos , Diurese/efeitos dos fármacos , Relação Dose-Resposta a Droga , Feminino , Masculino , Morfina/farmacologia , Ratos , Ratos WistarRESUMO
A marine Antarctic psychrotolerant bacterium (strain ANT/505), isolated from sea ice-covered surface water from the Southern Ocean, showed pectinolytic activity on citrus pectin agar. The sequencing of the 16S rRNA of isolate ANT/505 indicates a taxonomic affiliation to Pseudoalteromonas haloplanktis. The supernatant of this strain showed three different pectinolytic activities after growth on citrus pectin. By activity screening of a genomic DNA library of isolate ANT/505 in Escherichia coli, two different pectinolytic clones could be isolated. Subcloning and sequencing revealed two open reading frames (ORF) of 1,671 and 1,968 nt, corresponding to proteins of 68 and 75 kDa, respectively. The deduced amino acid sequence of the two ORFs showed homology to pectate lyases from Erwinia chrysanthemi and Aspergillus nidulans. The pectate lyases contain signal peptides of 17 and 26 amino acids that were correctly processed after overexpression in E. coli BL21. Both enzymes were purified by anionic exchange chromatography. Maximal enzymatic activities for both pectate lyases were observed at 30 degrees C and a pH range of 9 to 10. The Km values of both lyases for pectate and citrus pectin were 1 g l(-1) and 5 g l(-1), respectively. Calcium was required for activity on pectic substrates, whereas the addition of 1 mM ethylenediaminetetraacetic acid (EDTA) resulted in complete inhibition of the enzymes. These two enzymes represent the first pectate lyases isolated and characterized from a cold-adapted marine bacterium.
Assuntos
Gammaproteobacteria/enzimologia , Gammaproteobacteria/genética , Polissacarídeo-Liases/genética , Polissacarídeo-Liases/metabolismo , Água do Mar/microbiologia , Sequência de Aminoácidos , Regiões Antárticas , Clonagem Molecular , Temperatura Baixa , Estabilidade Enzimática , Genes Bacterianos , Sedimentos Geológicos/microbiologia , Concentração de Íons de Hidrogênio , Dados de Sequência Molecular , Pectinas/metabolismo , Polissacarídeo-Liases/química , Polissacarídeo-Liases/isolamento & purificação , Especificidade por Substrato , TemperaturaRESUMO
We have isolated a genomic clone encoding trichobakin (TBK), a type I ribosome-inactivating protein from the plant Trichosanthes sp. Bac Kan 8-98 (family Cucurbitaceae), by PCR using specific primers designed from the cDNA sequences of alpha-trichosanthin. The sequence encoding mature TBK was constructed in the pET-21d(+) vector for overexpression in Escherichia coli strain BL21(DE3). The recombinant protein was purified to homogeneity by CM-Sepharose chromatography on FPLC with a final yield of about 55 mg/l of culture. The protein has a molecular mass of about 27 kDa, as shown by SDS/PAGE and matrix-assisted laser-desorption ionization MS. It was found that the protein inhibited luciferase mRNA translation in the rabbit reticulocyte cell-free system with an IC(50) value (that which causes a 50% reduction of residual translational activity) of about 3.5 pM. The rRNA N-glycosidase activity of the protein was also proved at the above-mentioned concentration after rRNAs were treated with acid aniline.