Evaluation of the expression of p53, MDM2, and SUMO-1 in oral lichen planus

Objective: The objective of this study was to compare the expression of proteins p53, MDM2, and SUMO-1 in oral lichen planus (OLP) lesions, epithelial dysplasia, and squamous cell carcinoma. Materials and Methods: The sample consisted of the following five groups of cheek mucosa lesions: normal mucosa (NM), inflammatory fibrous hyperplasia (IFH), lichen planus, epithelial dysplasia, and squamous cell carcinoma. The tissue samples were stained with hematoxylin-eosin and submitted to immunohistochemistry using anti-p53, anti-MDM2, and anti-SUMO-1 antibodies. Results: The results of this study demonstrated similar expression of p53 and MDM2 between OLP, oral epithelial dysplasia and, to a lesser extent, between OLP and oral squamous cell carcinoma (OSCC). However, for SUMO-1 a similar expression was observed in OLP, NM, and IFH. Conclusions: The results demonstrated overexpression of important proteins (p53 and MDM2) related to regulatory mechanisms of apoptosis in OLP, suggesting that there is a favorable environment for malignant transformation. The expression of SUMO-1 in OLP was similar to NM and IFH, suggesting that alterations of this protein occur at later stages of carcinogenesis, because important overexpression occurred in oral epithelial dysplasia and OSCC. © 2013 John Wiley & Sons A/S.

Study of MDM2 and SUMO-1 expression in actinic cheilitis and lip cancer

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

In Vivo Effects of Bothrops jararaca Venom on Metabolic Profile and on Muscle Protein Metabolism in Rats

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Muscle protein metabolism in neonatal alloxan-administered rats: effects of continuous and intermittent swimming training

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Protein levels for heat-exposed broilers: Performance, nutrients digestibility, and energy and protein metabolism

Heat stress causes significant economic losses on broilers production due to poorer performance and carcass quality. Considering that protein has the highest heat increment among nutrients, it has been suggested that protein levels should be reduced in diets for heat-exposed broilers. Nevertheless, there are no conclusive results on the benefits of such practice, and further studies should be performed to elucidate some reported discrepancies. Thus, a trial was carried out to evaluate the effects of dietary protein levels (17, 20 and 23%) and environmental temperature (22 and 32°C) on the performance, nutrients digestibility, and energy and protein metabolism of broiler chickens from 21 to 42 days of age. Nutrients digestibility was determined by total excreta collection, and energy and protein metabolism was evaluated by comparative slaughter method. It was concluded that (1) heat exposure impairs broilers performance and increases nitrogen excretion, but do not change nutrients digestibility; (2) high-protein diets are technically feasible and promotes lower heat production for broilers reared under thermoneutral or hot environments, however, high-protein diets increases nitrogen excretion. © Asian Network for Scientific Information, 2007.

Avaliação da expressão das proteínas p53, MDM2 e SUMO-1 em líquen plano bucal, displasia epitelial bucal e carcinoma de células escamosas bucal

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Production of recombinant EMA-1 protein and its application for the diagnosis of Theileria equi using an enzyme immuno assay in horses from São Paulo State, Brazil

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Protective effects of the galectin-1 protein on in vivo and in vitro models of ocular inflammation

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Immunohistochemical detection of metalloproteinase-9 (MMP-9), anti-oxidant like 1 protein (AOP-1) and synaptosomal-associated protein (SNAP-25) in the cerebella of dogs naturally infected with spontaneous canine distemper

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Kaposi's sarcoma-associated herpesvirus latency-associated nuclear antigen 1 mimics Epstein-Barr virus EBNA1 immune evasion through central repeat domain effects on protein processing

Kaposi's sarcoma-associated herpesvirus (KSHV/human herpesvirus 8 [HHV8]) and Epstein-Barr virus (EBV/HHV4) are distantly related gammaherpesviruses causing tumors in humans. KSHV latency-associated nuclear antigen 1 (LANA1) is functionally similar to the EBV nuclear antigen-1 (EBNA1) protein expressed during viral latency, although they have no amino acid similarities. EBNA1 escapes cytotoxic lymphocyte (CTL) antigen processing by inhibiting its own proteosomal degradation and retarding its own synthesis to reduce defective ribosomal product processing. We show here that the LANA1 QED-rich central repeat (CR) region, particularly the CR2CR3 subdomain, also retards LANA1 synthesis and markedly enhances LANA1 stability in vitro and in vivo. LANA1 isoforms have half-lives greater than 24 h, and fusion of the LANA1 CR2CR3 domain to a destabilized heterologous protein markedly decreases protein turnover. Unlike EBNA1, the LANA1 CR2CR3 subdomain retards translation regardless of whether it is fused to the 5′ or 3′ end of a heterologous gene construct. Manipulation of sequence order, orientation, and composition of the CR2 and CR3 subdomains suggests that specific peptide sequences rather than RNA structures are responsible for synthesis retardation. Although mechanistic differences exist between LANA1 and EBNA1, the primary structures of both proteins have evolved to minimize provoking CTL immune responses. Simple strategies to eliminate these viral inhibitory regions may markedly improve vaccine effectiveness by maximizing CTL responses. Copyright © 2007, American Society for Microbiology. All Rights Reserved.