Necrotizing sialometaplasia as a cause of a non-ulcerated nodule in the hard palate: a case report

<p>Abstract</p> <p>Introduction</p> <p>Necrotizing sialometaplasia is a benign, self-limiting and rare inflammatory disease which, on clinical and histological examination, mimics malignant neoplasms.</p> <p>Case report</p> <p>We report the case of a healthy 25-year-old Caucasian woman with a three-week history of a painless lump on her hard palate. Oral examination revealed a nodule consisting of two lobules on the right side that measured 2.5 cm. Her mucosa was normal in color and a fluctuant area was detected in the posterior region upon palpation. Our patient was submitted to incisional biopsy and histopathological examination. The histological diagnosis was necrotizing sialometaplasia. The lesion had healed spontaneously after 30 days, with observed signs of involution of the nodule.</p> <p>Conclusion</p> <p>Histopathological examination is necessary for the diagnosis of necrotizing sialometaplasia because the clinical features of this condition can mimic other diseases, particularly malignant neoplasms.</p

Kinetic Model for Triglyceride Hydrolysis Using Lipase: Review

Triglyceride hydrolysis using lipase has been proposed as a novel method to produce raw materials in food andcosmetic industries such as diacylglycerol, monoacylglycerol, glycerol and fatty acid. In order to design a reactor forutilizing this reaction on industrial scale, constructing a kinetic model is important. Since the substrates are oil andwater, the hydrolysis takes place at oil-water interface. Furthermore, the triglyceride has three ester bonds, so that thehydrolysis stepwise proceeds. Thus, the reaction mechanism is very complicated. The difference between theinterfacial and bulk concentrations of the enzyme, substrates and products, and the interfacial enzymatic reactionmechanism should be considered in the model

Consecutive Reaction Model For Triglyceride Hydrolysis Using Lipase

Abstra

Ribosomal protein S1 influences trans-translation in vitro and in vivo

When the bacterial ribosome stalls on a truncated mRNA, transfer–messenger RNA (tmRNA) acts initially as a transfer RNA (tRNA) and then as a messenger RNA (mRNA) to rescue the ribosome and add a peptide tag to the nascent polypeptide that targets it for degradation. Ribosomal protein S1 binds tmRNA but its functional role in this process has remained elusive. In this report, we demonstrate that, in vitro, S1 is dispensable for the tRNA-like role of tmRNA but is essential for its mRNA function. Increasing or decreasing the amount of protein S1 in vivo reduces the overall amount of trans-translated proteins. Also, a truncated S1 protein impaired for ribosome binding can still trigger protein tagging, suggesting that S1 interacts with tmRNA outside the ribosome to keep it in an active state. Overall, these results demonstrate that S1 has a role in tmRNA-mediated tagging that is distinct from its role during canonical translation

Incontinentia pigmenti presenting as hypodontia in a 3-year-old girl: a case report

<p>Abstract</p> <p>Introduction</p> <p>Incontinentia pigmenti or Bloch-Sulzberger syndrome is a rare X-linked dominant disease that mainly affects the skin, eyes, hair, central nervous system and teeth. The disease is predominant among women. Although dermatologic manifestations are among the most important aspects for the diagnosis of the syndrome, they are less damaging to the patient and do not require treatment. However, oral involvement characterized by hypodontia of deciduous and permanent teeth is important for the diagnosis and treatment of the patient.</p> <p>Case presentation</p> <p>We report the case of a 3-year-old girl with ophthalmologic and neurologic disturbances, cutaneous manifestations and hypodontia. Since the patient did not present more damaging manifestations such as neurologic and/or ophthalmologic problems, her most severe complications were related to dental anomalies. The importance of integrated dental treatment, which combines pediatric dentistry, orthodontics and conventional prosthesis, is emphasized.</p> <p>Conclusion</p> <p>Hypodontia is a frequent finding in incontinentia pigmenti, and dentists should be aware of this condition in order to help with the diagnosis.</p

KINETIC MODEL FOR TRIGLYCERIDE HYDROLYSIS USING LIPASE: REVIEW

Triglyceride hydrolysis using lipase has been proposed as a novel method to produce raw materials in food andcosmetic industries such as diacylglycerol, monoacylglycerol, glycerol and fatty acid. In order to design a reactor forutilizing this reaction on industrial scale, constructing a kinetic model is important. Since the substrates are oil andwater, the hydrolysis takes place at oil-water interface. Furthermore, the triglyceride has three ester bonds, so that thehydrolysis stepwise proceeds. Thus, the reaction mechanism is very complicated. The difference between theinterfacial and bulk concentrations of the enzyme, substrates and products, and the interfacial enzymatic reactionmechanism should be considered in the model.Keywords: Lipase, kinetic model, enzymatic reaction mechanism, hydrolysis, triglycerid

KINETIC MODEL FOR TRIGLYCERIDE HYDROLYSIS USING LIPASE: REVIEW

Abstract Triglyceride hydrolysis using lipase has been proposed as a novel method to produce raw materials in food and cosmetic industries such as diacylglycerol, monoacylglycerol, glycerol and fatty acid. In order to design a reactor for utilizing this reaction on industrial scale, constructing a kinetic model is important. Since the substrates are oil and water, the hydrolysis takes place at oil-water interface. Furthermore, the triglyceride has three ester bonds, so that the hydrolysis stepwise proceeds. Thus, the reaction mechanism is very complicated. The difference between the interfacial and bulk concentrations of the enzyme, substrates and products, and the interfacial enzymatic reaction mechanism should be considered in the model

Mycobacterium tuberculosis ribosomal protein S1 (RpsA) and variants with truncated C-terminal end show absence of interaction with pyrazinoic acid.

Pyrazinamide (PZA) is an antibiotic used in first- and second-line tuberculosis treatment regimens. Approximately 50% of multidrug-resistant tuberculosis and over 90% of extensively drug-resistant tuberculosis strains are also PZA resistant. Despite the key role played by PZA, its mechanisms of action are not yet fully understood. It has been postulated that pyrazinoic acid (POA), the hydrolyzed product of PZA, could inhibit trans-translation by binding to Ribosomal protein S1 (RpsA) and competing with tmRNA, the natural cofactor of RpsA. Subsequent data, however, indicate that these early findings resulted from experimental artifact. Hence, in this study we assess the capacity of POA to compete with tmRNA for RpsA. We evaluated RpsA wild type (WT), RpsA ∆A438, and RpsA ∆A438 variants with truncations towards the carboxy terminal end. Interactions were measured using Nuclear Magnetic Resonance spectroscopy (NMR), Isothermal Titration Calorimetry (ITC), Microscale Thermophoresis (MST), and Electrophoretic Mobility Shift Assay (EMSA). We found no measurable binding between POA and RpsA (WT or variants). This suggests that RpsA may not be involved in the mechanism of action of PZA in Mycobacterium tuberculosis, as previously thought. Interactions observed between tmRNA and RpsA WT, RpsA ∆A438, and each of the truncated variants of RpsA ∆A438, are reported