RESUMO
RESUMO Estima-se que 80% da população mundial dependam das plantas medicinais no processo da atenção primária em saúde, e grande parte destes tem nas plantas a única fonte de medicamentos. O presente estudo teve como objetivo verificar a utilização de plantas medicinais pela comunidade, pertencente à equipe 10 da Estratégia Saúde da Família (ESF) da Unidade Básica de Saúde (UBS) Pinheiros, em Maringá, Paraná, Brasil. Os dados foram coletados no período de março de 2012 a maio de 2012. A equipe de pesquisadores aplicou 95 questionários intercalando os domicílios. Observou-se que 24,2% utilizam plantas medicinais com frequência, 40% utilizam esporadicamente e 35,8% não utilizam. Entre as pessoas que utilizam, observou-se que a forma mais citada foi o uso era pela indicação de amigos ou pelos ancestrais As plantas medicinais mais citadas foram: hortelã (Mentha sp.), boldo (Plectranthus barbatus), camomila (Matricaria recutita), erva cidreira (Melissa officinalis) e guaco (Mikania glomerata). Quando perguntados se o uso de plantas medicinais somente fazem bem à saúde, 68,5% dos participantes afirmaram que plantas medicinais não causam nenhum mal à saúde. A partir destes resultados, observou-se que a utilização de plantas medicinais é bem aceita pela população e que ainda existe uma lacuna grande a ser preenchida pelos profissionais da saúde no que diz respeito à orientação sobre o uso correto desse tipo de terapia.
ABSTRACT It is estimated that 80% of the population depends on herbal medicine regarding primary health care and most of these people use plants as their only source of drugs. The current study aimed to know the profile of the community served by the staff 10 of the Family Health Strategy (FHS) of Basic Unity of Health (BUH) Pinheiros, in Maringá, Paraná State, in regard to the use of medicinal plants. The data was collected between March of 2012 and May of the same year. Ninety-five questionnaires were applied. 24.2% of people employ medicinal plants frequently, 40% use it occasionally and 35.8% do not appeal to them at all. Most of them learnt about medicinal plants with family and friends. The most mentioned medicinal plants by population were the following: Mentha sp., Plectranthus barbatus, Matricaria recutita, Melissa officinalis and Mikania glomerata. 68.5% of the participants believe that medicinal plants do not cause any harm to health. From these results, we can notice that medicinal plants are widely accepted and there is a big gap to be filled by health professional in terms of proper orientation about the use of this kind of therapy.
Assuntos
Pacientes/estatística & dados numéricos , Plantas Medicinais/classificação , Características de Residência/classificação , Uso de Medicamentos/tendênciasRESUMO
Glucagon, the counter-regulatory hormone to insulin, is secreted from pancreatic alpha cells in response to low blood glucose. To examine the role of glucagon in glucose homeostasis, mice were generated with a null mutation of the glucagon receptor (Gcgr(-/-)). These mice display lower blood glucose levels throughout the day and improved glucose tolerance but similar insulin levels compared with control animals. Gcgr(-/-) mice displayed supraphysiological glucagon levels associated with postnatal enlargement of the pancreas and hyperplasia of islets due predominantly to alpha cell, and to a lesser extent, delta cell proliferation. In addition, increased proglucagon expression and processing resulted in increased pancreatic glucogen-like peptide 1 (GLP-1) (1-37) and GLP-1 amide (1-36 amide) content and a 3- to 10-fold increase in circulating GLP-1 amide. Gcgr(-/-) mice also displayed reduced adiposity and leptin levels but normal body weight, food intake, and energy expenditure. These data indicate that glucagon is essential for maintenance of normal glycemia and postnatal regulation of islet and alpha and delta cell numbers. Furthermore, the lean phenotype of Gcgr(-/-) mice suggests glucagon action may be involved in the regulation of whole body composition.
Assuntos
Glicemia/metabolismo , Glucagon/sangue , Ilhotas Pancreáticas/patologia , Receptores de Glucagon/genética , Receptores de Glucagon/fisiologia , Animais , Peso Corporal , Calorimetria , Divisão Celular , AMP Cíclico/metabolismo , Epididimo/metabolismo , Epinefrina/farmacologia , Glucose/metabolismo , Hormônios/metabolismo , Hiperplasia , Imuno-Histoquímica , Insulina/metabolismo , Fígado/metabolismo , Masculino , Camundongos , Camundongos Endogâmicos C57BL , Microscopia de Fluorescência , Fenótipo , Fatores de TempoRESUMO
In common forms of obesity, hyperphagia, hyperinsulinemia, and hyperleptinemia coexist. Here, we demonstrate rapid induction of insulin and leptin resistance by short-term overfeeding. After 3 and 7 days on the assigned diet regimen, rats were tested for their biological responses to acute elevations in plasma insulin and leptin concentrations. Severe resistance to the metabolic effects of both leptin and insulin ensued after just 3 days of overfeeding. During the insulin clamp studies, glucose production was decreased by approximately 70% in control rats and 28-53% in overfed rats. Similarly, leptin infusion doubled the contribution of gluconeogenesis to glucose output in control rats but failed to modify gluconeogenesis in overfed animals. These findings demonstrate a paradoxical and rapid collapse of the leptin system in response to nutrient excess. This partial failure is tightly coupled with the onset of insulin resistance.
Assuntos
Resistência a Medicamentos , Hiperfagia/complicações , Resistência à Insulina , Leptina/farmacologia , Animais , Dieta , Ingestão de Alimentos/efeitos dos fármacos , Gluconeogênese , Glucose/biossíntese , Insulina/administração & dosagem , Insulina/sangue , Leptina/administração & dosagem , Leptina/análise , Masculino , Ratos , Ratos Sprague-Dawley , Fatores de TempoRESUMO
The v-Ki-Ras oncoprotein dedifferentiates thyroid cells and inhibits nuclear accumulation of the catalytic subunit of cAMP-dependent protein kinase. After activation of v-Ras or protein kinase C, the regulatory subunit of type II protein kinase A, RIIbeta, translocates from the membranes to the cytosol. RIIbeta mRNA and protein were eventually depleted. These effects were mimicked by expressing AKAP45, a truncated version of the RII anchor protein, AKAP75. Because AKAP45 lacks membrane targeting domains, it induces the translocation of PKAII to the cytoplasm. Expression of AKAP45 markedly decreased thyroglobulin mRNA levels and inhibited accumulation of C-PKA in the nucleus. Our results suggest that: 1) The localization of PKAII influences cAMP signaling to the nucleus; 2) Ras alters the localization and the expression of PKAII; 3) Translocation of PKAII to the cytoplasm reduces nuclear C-PKA accumulation, resulting in decreased expression of cAMP-dependent genes, including RIIbeta, TSH receptor, and thyroglobulin. The loss of RIIbeta permanently down-regulates thyroid-specific gene expression.
Assuntos
Proteínas Adaptadoras de Transdução de Sinal , Proteínas Quinases Dependentes de AMP Cíclico/metabolismo , Genes ras , Transdução de Sinais , Proteínas de Ancoragem à Quinase A , Animais , Western Blotting , Proteínas de Transporte , Linhagem Celular , Transformação Celular Neoplásica , AMP Cíclico/farmacologia , Subunidade RIIbeta da Proteína Quinase Dependente de AMP Cíclico , Proteína Quinase Tipo II Dependente de AMP Cíclico , Proteínas Quinases Dependentes de AMP Cíclico/biossíntese , Primers do DNA , Regulação Enzimológica da Expressão Gênica , Manosidases/biossíntese , Proteína Oncogênica p21(ras)/biossíntese , Reação em Cadeia da Polimerase , Biossíntese de Proteínas , Proteínas/metabolismo , Ratos , Receptores da Tireotropina/biossíntese , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/metabolismo , Deleção de Sequência , Tireoglobulina/biossíntese , Transfecção , alfa-ManosidaseRESUMO
TSH receptor mRNA levels in FRTL-5 thyroid cells are autoregulated at a transcriptional level by the same hormones required for the growth and function of the cells: TSH, insulin, and insulin-like growth factor-I (IGF-I). Thus, the ability of TSH, via its cAMP signal, to down-regulate steady state receptor mRNA levels is preceded by the action of TSH to decrease pre-mRNA levels in nuclear run-on assays to the same quantitative level as evident in Northern analyses. In contrast, the receptor mRNA half-life is shown not to change when down-regulation is reversed by withdrawing TSH in the presence or absence of actinomycin-D. Evidence is additionally provided that TSH receptor mRNA levels are increased by insulin, IGF-I, or calf serum in both Northern and run-on assays. This action cannot be duplicated by hydrocortisone and is evident at more than 20-fold lower concentrations of IGF-I than insulin. Moreover, insulin, IGF-I, and/or calf serum are required for the autoregulatory negative transcriptional regulation of the TSH receptor by TSH/cAMP, as is the case for thyroglobulin. This occurs despite the opposite actions of TSH/cAMP on the two genes, positive in the case of thyroglobulin and negative with TSH receptor. The positive and negative regulatory actions, respectively, of insulin/IGF-I and TSH on receptor gene expression are associated with coincident increases or decreases in cell surface receptors measured by [125I]TSH binding. The autoregulation additionally involves the interplay of a second cAMP-modulated regulatory factor, one which up-regulates TSH receptor mRNA levels rather than causing down-regulation. Thus, cycloheximide inhibits the transcriptional action of both TSH/cAMP and insulin/IGF-I/serum within 4 h, i.e. a rapidly synthesized protein is an intermediate in both cases. The presence of cycloheximide for as little as 1 h, however, uncovers the ability of TSH/cAMP to increase TSH receptor mRNA levels. This activity is the result of the action of a stable cAMP-induced activator which can be detected physiologically, i.e. in the absence of cycloheximide. For example, low levels of a cAMP analog (0.2 mM), as opposed to high levels (greater than 1 mM), can increase TSH receptor RNA levels. Low levels also accelerate the insulin/IGF-I-dependent return of receptor mRNA to normal levels after TSH withdrawal.(ABSTRACT TRUNCATED AT 400 WORDS)
Assuntos
Regulação da Expressão Gênica , Receptores da Tireotropina/genética , Glândula Tireoide/metabolismo , Animais , Fenômenos Fisiológicos Sanguíneos , Células Cultivadas , AMP Cíclico/farmacologia , Cicloeximida/farmacologia , Regulação para Baixo , Insulina/farmacologia , Fator de Crescimento Insulin-Like I/farmacologia , Biossíntese de Proteínas , RNA Mensageiro/análise , Ratos , Tireotropina/metabolismo , Tireotropina/farmacologia , Transcrição Gênica , Regulação para CimaRESUMO
In thyroid cells, iodide is accumulated intracellularly via a Na+-I-cotransporter. In this report we show that it is possible to detect diffusible 125I-concentrated in thyroid cell colonies that have been replicated onto nylon filters. Using the replica filter assay, we demonstrate that the iodide transport 1) is restricted to thyroid cells, 2) is Na+ dependent and electrogenic, 3) is inhibited by ClO4- and SCN-, and 4) is adenosine 3',5'-cyclic monophosphate dependent. These are all characteristics of thyroidal iodide transport. This technique can, in principle, detect the expression of any transport system that results in the intracellular accumulation of a diffusible molecule. Moreover, the filter assay can be used to screen for colonies carrying structural or functional mutations affecting such transport systems.
Assuntos
Filtração/métodos , Iodetos/farmacocinética , Técnicas de Réplica , Glândula Tireoide/metabolismo , Animais , Transporte Biológico , Linhagem Celular , Sensibilidade e Especificidade , Glândula Tireoide/citologiaRESUMO
The biologic effects of IFN-gamma are mediated through a receptor that is expressed in relatively low abundance on normal mammalian cells. As a consequence, investigations of the physicochemical and ligand-binding properties of the purified receptor have been limited. The work reported here characterizes a secreted form of the receptor for mouse IFN-gamma, made by deletion of the nucleotides that code for the anchoring domain from a cDNA that encodes the receptor binding protein and its related signal peptide. When transfected into rat XC cells, this construct produced up to approximately 1 mg/liter of a secreted protein that had the characteristics of the native receptor. Both the secreted protein and its mRNA were of sizes that were consistent with loss of the transmembrane region. The protein was detectable by a mAb that is specific for an epitope that is found in the ligand binding site of the receptor for mouse IFN-gamma, as well as by a goat polyclonal IgG that is monospecific for the mouse IFN-gamma R. Supernates that contained the secreted protein blocked binding of IFN-gamma to mouse IFN-gamma R and inhibited in a dose-dependent manner the IFN-gamma-mediated priming of mouse bone marrow culture-derived macrophages for tumor cell killing. Availability of relatively large amounts of a secreted protein that retains ligand-binding activity should facilitate purification and basic studies of the receptor binding protein and could provide new approaches to the treatment/prevention of diseases that arise due to inappropriate response of cells to IFN-gamma. In addition, because this secreted receptor, unlike others, consists of both the extracellular and intracellular domains, it is likely that it will be useful in determining how the cytoplasmic portion of the receptor is involved in receptor function.
Assuntos
Interferon gama/metabolismo , Receptores Imunológicos/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Sítios de Ligação , Northern Blotting , Clonagem Molecular , Expressão Gênica , Camundongos , Dados de Sequência Molecular , Peso Molecular , RNA Mensageiro/genética , Ratos , Receptores Imunológicos/química , Receptores Imunológicos/metabolismo , Receptores de Interferon , Relação Estrutura-Atividade , TransfecçãoRESUMO
Exposure of rat thyroid cells for 1 week to a temperature-sensitive variant of Kirsten murine sarcoma virus (KiMSV) Ras inactivated the thyroglobulin promoter (pTg). Cellular dedifferentiation was paralleled by the loss of the thyroid-specific trans-acting factor, TgTF1, which binds to pTg. When Ras was denatured by shifting cells to 39 degrees C, TgTF1 binding and pTg function recovered rapidly without the synthesis of new protein. TgTF1 could be reactivated in vitro by treating nuclear extracts with protein kinase A. After 4 weeks of exposure to the oncogene, denaturation of Ras no longer restored TgTF1 binding or reactivated pTg. Incubation of nuclear extracts with protein kinase A likewise did not reactivate TgTF1. Cells chronically exposed to Ras did, however, yield differentiated clones after treatment with 5-azacytidine. We suggest that Ras induces dedifferentiation in two sequential steps: (1) Ras reduces PKA activity; TgTF1 (or an auxiliary protein) becomes dephosphorylated, and binding to pTg is abolished. (2) The effects of Ras become imprinted by methylation, possibly of the TgTF1 gene.
Assuntos
Genes ras , Tireoglobulina/genética , Glândula Tireoide/metabolismo , Transativadores/antagonistas & inibidores , Animais , Sequência de Bases , Transformação Celular Viral/genética , DNA/metabolismo , Vírus do Sarcoma Murino de Kirsten/genética , Metilação , Dados de Sequência Molecular , Sondas de Oligonucleotídeos , Regiões Promotoras Genéticas , Ratos , Transcrição GênicaRESUMO
Madin-Darby canine kidney cells (MDCK II) have been cotransfected with plasmids expressing the human CD8 alpha glycoprotein and the bacterial gene which confers resistance to neomycin. Stable transformants have been isolated in the presence of G-418 in the culture medium and screened for CD8 alpha expression by immunofluorescence. The three clones we have characterized showed: 1) high level of synthesis and efficient surface expression of glycosylated, homodimeric CD8 alpha and 2) preferential apical deposition of CD8 alpha in confluent monolayers. This polar distribution has been measured in cells grown on a plastic substratum as well as on nitrocellulose filter by means of EM immunocytochemistry and surface radioimmunoassay. CD8 alpha was 6 to 11-fold enriched on the apical membrane whereas the 58 kDa protein, a basolateral marker in MDCK II cells, resulted about 9-fold enriched on the basolateral membrane of the three clones. We believe these permanently transformed clones could prove to be a useful tool with which to study cell polarity.
Assuntos
Antígenos de Diferenciação de Linfócitos T/biossíntese , Linhagem Celular Transformada/metabolismo , Glicoproteínas de Membrana/biossíntese , Animais , Antígenos CD8 , Linhagem Celular Transformada/ultraestrutura , Membrana Celular/metabolismo , Membrana Celular/ultraestrutura , Células Clonais , Cães , Vírus da Leucemia Murina de Friend/genética , Humanos , Microscopia de Fluorescência , Microscopia Imunoeletrônica , Plásticos , Radioimunoensaio , Radioisótopos de Enxofre , Fatores de Tempo , Transfecção/genéticaRESUMO
Thyroglobulin gene expression was repressed in a rat thyroid cell line transformed with Kirsten murine sarcoma virus. Expression of a dominant selectable marker driven by the thyroglobulin promoter was also inhibited. Somatic cell hybridization of transformed and differentiated thyroid cells resulted in extinction of thyroglobulin gene expression. When transformed cells carrying a dominant selectable marker driven by the thyroglobulin promoter were fused to differentiated cells and expression of this marker was selected, we obtained stable hybrid cell lines expressing both the endogenous and the exogenous thyroglobulin promoters. Although the expression of v-ras remained unchanged compared with expression in the parental transformed cells, transformation was suppressed in the hybrid cell lines. The other thyroid differentiation markers, iodide uptake and thyroid-stimulating hormone-dependent growth, were inhibited in all the hybrids tested. We show that activity of the thyroglobulin promoter correlates with the presence of a thyroid nuclear factor that binds the promoter at position -60 from the transcription start site. Loss of this factor accompanies the extinction of thyroglobulin gene expression in hybrids selected for expression of a non-thyroid-specific promoter.
Assuntos
Células Híbridas/fisiologia , Tireoglobulina/genética , Glândula Tireoide/fisiologia , Fatores de Transcrição/fisiologia , Animais , Diferenciação Celular , Regulação da Expressão Gênica , Genes ras , Técnicas In Vitro , RNA Mensageiro/genética , Ratos , Seleção Genética , Glândula Tireoide/citologia , TransfecçãoRESUMO
Transformed rat thyroid cells fail to express thyroglobulin. Cells transformed with a Kirsten murine sarcoma virus carrying a temperature-sensitive ras allele lose their transformation phenotype when shifted to the nonpermissive (39 degrees C) temperature. The thyroglobulin promoter, however, remains inactive. Similarly, transfection of these cells with a thyroglobulin promoter fused to a neomycin resistance reporter gene does not produce clones resistant to G418. Treatment of the transfected cells with the DNA demethylating agent 5-azacytidine reactivates the thyroglobulin promoter and yields stable G418-resistant clones. We show that thyroglobulin promoter activity is correlated with the presence of a thyroid-specific nuclear factor, TgTF1. TgTF1 cannot be detected in transformed cells but reappears after treatment with 5-azacytidine at 39 degrees C. Restoration of Ras activity at 33 degrees C leads to the rapid loss of TgTF1 and G418 resistance.
Assuntos
Azacitidina/farmacologia , Transformação Celular Neoplásica , Regulação da Expressão Gênica/efeitos dos fármacos , Genes/efeitos dos fármacos , Tireoglobulina/genética , Transcrição Gênica , Animais , Sequência de Bases , Linhagem Celular , Núcleo Celular/metabolismo , Clonagem Molecular , Vírus do Sarcoma Murino de Kirsten/genética , Dados de Sequência Molecular , Sondas de Oligonucleotídeos , Regiões Promotoras Genéticas , Ratos , Glândula Tireoide , TransfecçãoRESUMO
A novel human gene, encoding a 188 amino acid polypeptide that contains a region similar to that of the epidermal growth factor, has been isolated. The gene, expressed in undifferentiated human and mouse teratocarcinoma cells, is shut off after inducing the cells to differentiate by treatment with retinoic acid. Introduction of the cDNA under the control of a viral LTR induces transformation of NIH3T3 cells.
Assuntos
Fator de Crescimento Epidérmico/genética , Genes , Família Multigênica , Teratoma/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Northern Blotting , Diferenciação Celular/efeitos dos fármacos , Linhagem Celular , Células Cultivadas , DNA de Neoplasias/genética , DNA de Neoplasias/isolamento & purificação , Humanos , Camundongos , Dados de Sequência Molecular , Homologia de Sequência do Ácido Nucleico , Transcrição Gênica , Tretinoína/farmacologiaRESUMO
We have introduced the beta 2-adrenergic receptor into the unnatural environment of a thyroid cell to demonstrate that the activation of this receptor initiates diverse cellular programs in different cell types. The thyroid-stimulating hormone (TSH) receptor and the beta 2-adrenergic receptor stimulate a common signaling pathway in distinct populations of cells. In this study, we demonstrate that the activation of the beta 2-adrenergic receptor, transfected into a thyroid epithelial cell, elicits a program of growth and differentiation normally observed with TSH. In thyroid cells expressing beta 2 receptors, the beta 2 agonist isoproterenol activates adenylate cyclase, induces the expression of a thyroid-specific iodide carrier system, and can substitute for TSH to promote growth. Thus, in thyroid cells expressing beta 2-adrenergic receptors, isoproterenol elicits the entire array of thyroid-specific functions normally activated by TSH.
Assuntos
Receptores Adrenérgicos beta/fisiologia , Glândula Tireoide/citologia , 1-Metil-3-Isobutilxantina/farmacologia , Animais , Diferenciação Celular/efeitos dos fármacos , Divisão Celular/efeitos dos fármacos , Linhagem Celular , Colforsina/farmacologia , AMP Cíclico/metabolismo , Replicação do DNA , Humanos , Iodetos/metabolismo , Isoproterenol/farmacologia , Ratos , Receptores Adrenérgicos beta/genética , Glândula Tireoide/metabolismo , Tireotropina/farmacologia , TransfecçãoRESUMO
Type III collagen is often found in the same tissues as type I collagen, yet the function and nature of the fibrils formed by the two collagens differ markedly. To understand the evolutionary history of the collagen gene family in more detail, we isolated the gene for type III collagen and compared its structure with that of the gene for alpha 2(I) collagen. This comparison points to a remarkable conservation in the size distribution of the exons coding for the helical part of these two collagen polypeptides: equivalent amino acid segments in the helical domain of each polypeptide are encoded by exons of equal sizes in each gene. This suggests that after the interstitial collagen genes had been duplicated from a common ancestor about 2-5 X 10(8) years ago, no recombinations between these exons were tolerated, although the same recombinational phenomena must have played an important part in shaping the structure of the progenitor for these genes. This fixation of the size distribution of the exons which code for the interstitial collagen helical domains is found despite the persistence in these exons of sequence elements that should have favoured recombinational rearrangements, and contrasts with the variations in the pattern of sizes of some exons coding for the amino and carboxyl propeptides of these collagens.