Biomedical subjects

J M Granjeiro

Publications and source records attributed to J M Granjeiro.

8 recordsLinked to original sources

PubMed2006

Radiographic assessment of impacted mandibular third molar sockets filled with composite xenogenic bone graft.

OBJECTIVES: The main purpose of this study was to evaluate the radiographic aspect of the healing of extraction sockets filled with a xenogenic graft material (Gent-tech). METHODS: Thirty-nine patients ranging in age from 15 years to 25 years with bilateral impacted mandibular molars were chosen based on bilateral mandibular similarities. After tooth extraction, the socket was filled with the graft. The opposite site was left to heal naturally and served as a control. The experimental and control sites were chosen randomly. Bone density and crest healing were evaluated on digital radiographs taken immediately, 2 months and 6 months after surgery. The respective pixels values obtained with the Digora software were compared statistically. RESULTS: The results showed a significant decrease in the distance from the cemento-enamel junction to the alveolar bone crest, but no difference was found between the control and experimental groups. Bone density increased significantly, and there was difference between experimental and control groups. CONCLUSION: The analysed parameters observed by the authors were similar to those of the control group, suggesting xenogenic graft being an acceptable material and a graft option.

Absorbable Implants↗

PubMed2005

Bone morphogenetic proteins: from structure to clinical use.

Bone morphogenetic proteins (BMPs) are multi-functional growth factors belonging to the transforming growth factor ss superfamily. Family members are expressed during limb development, endochondral ossification, early fracture, and cartilage repair. The activity of BMPs was first identified in the 1960s but the proteins responsible for bone induction were unknown until the purification and cloning of human BMPs in the 1980s. To date, about 15 BMP family members have been identified and characterized. The signal triggered by BMPs is transduced through serine/threonine kinase receptors, type I and II subtypes. Three type I receptors have been shown to bind BMP ligands, namely: type IA and IB BMP receptors and type IA activin receptors. BMPs seem to be involved in the regulation of cell proliferation, survival, differentiation and apoptosis, but their hallmark is their ability to induce bone, cartilage, ligament, and tendon formation at both heterotopic and orthotopic sites. This suggests that, in the future, they may play a major role in the treatment of bone diseases. Several animal studies have illustrated the potential of BMPs to enhance spinal fusion, repair critical-size defects, accelerate union, and heal articular cartilage lesions. Difficulties in producing and purifying BMPs from bone tissue have prompted the attempts made by several laboratories, including ours, to express these proteins in the recombinant form in heterologous systems. This review focuses on BMP structure, molecular mechanisms of action and significance and potential applications in medical, dental and veterinary practice for the treatment of cartilage and bone-related diseases.

Animals↗

PubMed1998

Soybean seed acid phosphatases: unusual optimum temperature and thermal stability studies.

In contrast to other acid phosphatases, four cytoplasmic isoforms (AP1, AP2, AP3A, and AP3B) purified from mature soybean seeds presented high activities at temperatures above 80 degrees C, when p-nitrophenylphosphate (p-NPP) was utilized as substrate. However, with tyrosine phosphate and inorganic pyrophosphate as substrates, maximum activities were observed at temperature of 60 degrees C during 10 min reaction. In the absence of substrate, enzymes lost only 20% activity after 60 min at 60 degrees C; the isoforms AP3A and AP3B retained 30% of activity at 70 degrees C after 60 min and all the isoforms were inactivated at 80 degrees C, after 5 min. Thermal inactivation studies indicated that the soybean enzymes showed different temperature dependences in relation to most plant acid phosphatases. A best protective effect was observed when the isoforms were preincubated, at 70 degrees C, with phosphate (10 mM) and p-nitrophenol (10 mM) which indicates that the enzyme inactivation was prevented only in the presence of both reaction products.

Acid Phosphatase↗

PubMed1997

Bovine kidney low molecular weight acid phosphatase: FMN-dependent kinetics.

A low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0. Distinct activation energy values were obtained for p-nitrophenyl phosphate- (45.44 kJ mol-1) and flavin mononucleotide- (28.60 kJ mol-1) hydrolysis reactions. The FMN hydrolysis was strongly inhibited by Cu2 and pCMB, but activated by guanosine. Pyridoxal-phosphate and vanadate were competitive inhibitors for the FMN-dependent reaction.

Acid Phosphatase↗

PubMed1997

Purification and characterization of a low-molecular-weight bovine kidney acid phosphatase.

A relative low molecular mass bovine kidney acid phosphatase was purified 1,640-fold to homogeneity, with 7% recovery. The purified enzyme (specific activity 100 mumol min-1 mg-1) was electrophoretically homogeneous with a relative molecular mass of 17.8 kDa, as determined by SDS-polyacrylamide gel electrophoresis. A broad pH optimum of 4.0-5.5 and a maximal enzyme activity at 60 degrees C were determined for the p-nitrophenyl phosphate hydrolysis. Apparent Km values of 0.14 mM, 0.4 mM, 0.3 mM and 7.9 mM were obtained, at 37 degrees C and pH 5.0, for the best substrates p-nitrophenyl phosphate, beta-naphtyl-phosphate, flavin mononucleotide and tyrosine-phosphate, respectively. The enzyme activity was enhanced by guanosine but inhibited by ZnCl2 and CuSO4, p-cloromercuribenzoate and ammonium molybdate. Vanadate (Ki 0.47 microM), pyridoxal 5'-phosphate (Ki 2.2 microM), inorganic phosphate (Ki 0.77 microM) are competitive inhibitors. Both glycerol and methanol increased significantly the acid phosphatase activity, acting as good phosphate acceptors in the transphosphorylation reaction.

Acid Phosphatase↗

PubMedDate not supplied

Analysis of fingernails and urine as biomarkers of fluoride exposure from dentifrice and varnish in 4- to 7-year-old children.

The use of fingernails and urine as biomarkers of exposure to fluoride (F) from fluoridated dentifrice and varnish was evaluated in twenty 4- to 7-year-old children, who were divided into two groups: group A (9 caries-free children) and group B (11 children with past caries experience). They used a placebo dentifrice for 28 days, fluoridated dentifrice (1,570 ppm F) for the following 28 days, and placebo dentifrice for an additional 28 days, then returned to their usual dentifrices. Group B children also received 4-week applications of a varnish (2.26% F) while using the fluoridated dentifrice. Urinary collections were performed 24 h before the use of fluoridated dentifrice and 24 h (group A) or 48 h (group B) after. Fingernails were clipped every 2 weeks, for 26 weeks. Total F intake from diet and dentifrice was estimated. Fingernail F concentrations did not vary significantly throughout the study. Twenty-four-hour urinary F outputs (mean +/- SD, microg) were: 414 +/- 200 and 468 +/- 253 for placebo and F dentifrices, respectively (group A) and 402 +/-206, 691 +/- 345, 492 +/- 243 for placebo dentifrice, F dentifrice plus F varnish and F dentifrice, respectively (group B). The use of F dentifrice did not cause a significant increase in the urinary F output. However, when F varnish was used, a transitory increase in the urinary F output was detected (p = 0.001), returning to baseline levels in the last 24 h. Thus, F varnish is a safe method for topical F application even in children that use F dentifrice regularly. According to our protocol, urine was a suitable biomarker of exposure to F from dentifrice plus varnish, but not from dentifrice alone, while nails were not.

Analysis of Variance↗

PubMedDate not supplied

Kinetic characterization of bovine lung low-molecular-weight protein tyrosine phosphatase.

Protein tyrosine phosphatase is an important class of enzymes that plays an essential role in the cellular proliferation, differentiation, and oncogenesis. In this paper we report characterization of a low-molecular-weight protein tyrosine phosphatase purified from bovine lung. The enzyme activity was essentially independent of metal ions and sensitive to sulfhydryl reagents. Both vanadate and inorganic phosphate are competitive inhibitors, with Ki values of 0.38 microM and 0.28 mM, respectively. Besides p-nitrophenyl phosphate, the enzyme was also able to efficiently hydrolyze tyrosine phosphate, beta-naphthyl phosphate, and flavine mononucleotide.

Animals↗

PubMedDate not supplied

Fluoride content of infant formulas prepared with deionized, bottled mineral and fluoridated drinking water.

Usually infant milk formula is the major source of fluoride in infancy. Fluoride concentrations in ten samples of powdered milk formulas, prepared with deionized, bottled mineral, and fluoridated drinking water were determined after HMDS-facilitated diffusion, using a fluoride ion specific electrode(Orion 9609). Fluoride concentrations ranged from 0.01 to 0.75 ppm; from 0.02 to 1.37 ppm and from 0.91 to 1.65 ppm for formulas prepared with deionized, bottled mineral (0.02 to 0.69 ppm F) and fluorinated drinking water (0.9 ppm F), respectively. Possible fluoride ingestion per Kg body mass ws estimated. With deionized water, only the soy-based- formulas should provide a daily fluoride intake of above the suggested threshold for fluorosis. With water containing 0.9 ppm F, however, all of them would provide it. Hence, to limit fluoride intakes to amounts <0.1 mg/kg/day, it is necessary to avoid use fo fluoridated water (around 1 ppm) to dilute powdered infant formulas.

Animals↗