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1.
J Immigr Minor Health ; 12(5): 726-36, 2010 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-19728092

RESUMO

To identify barriers to outdoor physical activity in winter among Somali youth in Maine. Despite the many proven health benefits of physical activity among children, such as cardiovascular fitness and health status as an adult, there has been a decrease in physical activity among children in recent years. Specifically, children who are of low socio-economic status or are from communities where many immigrants are at increased risk for developing obesity. Immigrants are also less likely to be physically active. There are many potential barriers to wintertime physical activity among Somali youth in Maine, such as lack of financial resources, transportation, proper winter clothing, and appropriate knowledge of winter safety, and language and cultural barriers. For females, different attire required for outdoor activity may be a barrier. Somali parents and children were recruited from Portland, Maine to participate in focus groups led by a trained facilitator with a Somali translator and cultural broker. Transcripts were coded using NVIVO software to identify barriers to physical activity among Somali youth outside in winter. Eight focus groups were conducted. Sixty-one Somali community members were recruited. Participants felt outdoor physical activity is important, but note that it is decreased in winter. Barriers to outdoor activity in winter cited by focus group participants were lack of resources, health concerns, gender barriers for females, and knowledge barriers. Concern over lack of supervision while children play outside was also cited. This study revealed many of the underlying beliefs, barriers and cultural issues that impact Somali families' intention to be active and ability to be active outdoors in winter. These findings can be used to generate research hypotheses and public health interventions regarding outdoor physical activity among Somali youth.


Assuntos
Exercício Físico , Comportamentos Relacionados com a Saúde/etnologia , Adolescente , Adulto , Criança , Características Culturais , Feminino , Grupos Focais , Humanos , Maine , Masculino , Estações do Ano , Classe Social , Somália/etnologia
2.
Violence Vict ; 24(2): 193-203, 2009.
Artigo em Inglês | MEDLINE | ID: mdl-19459399

RESUMO

Health professionals from two different clinical settings were asked about their comfort level in dealing with intimate partner violence (IPV). Focus groups and semistructured interviews were used to gather information. Staff in an obstetrics and gynecology setting relatively rich in IPV resources described feeling capable dealing with IPV. The staff in a general medicine setting dedicated to women's health but without a focus on IPV and with fewer supports described discomfort and difficulty dealing with IPV. Presence of systemic prioritization of and resources for IPV were described as contributing to the confidence in addressing the issue. Other necessary elements identified included (a) on-site resources, (b) adequate time, (c) focused IPV training, and (d) a team or systemic approach.


Assuntos
Atitude do Pessoal de Saúde , Vítimas de Crime/reabilitação , Comportamento de Ajuda , Relações Profissional-Paciente , Maus-Tratos Conjugais/reabilitação , Adulto , Mulheres Maltratadas , Vítimas de Crime/psicologia , Feminino , Grupos Focais , Humanos , Masculino , Pessoa de Meia-Idade , Avaliação das Necessidades , Maus-Tratos Conjugais/prevenção & controle
3.
Nat Neurosci ; 5(10): 963-70, 2002 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-12219096

RESUMO

Surface expression of the nicotinic acetylcholine receptor (AChR) requires the assembly of multiple subunits in the endoplasmic reticulum (ER). Little is known, however, about the mechanism by which assembled receptor pentamers are transported to the cell membrane while unassembled subunits are retained in the ER. Here we report that a motif conserved in the transmembrane domain of AChR subunits is critically involved in this process. In COS cells, mutation within this signal allowed surface expression of unassembled subunits. Conversely, insertion of the sequence to unrelated proteins that are normally transported to the surface resulted in ER retention. The signal is buried in AChR pentamers, but is exposed on unassembled subunits in the ER, where it promotes protein degradation. We therefore conclude that this signal ensures surface trafficking of only functional AChRs.


Assuntos
Receptores Nicotínicos/fisiologia , Motivos de Aminoácidos/fisiologia , Sequência de Aminoácidos , Animais , Células COS , Membrana Celular/metabolismo , Membrana Celular/fisiologia , Retículo Endoplasmático/metabolismo , Camundongos , Dados de Sequência Molecular , Subunidades Proteicas , Transporte Proteico/fisiologia , Receptores Nicotínicos/química
4.
Am J Physiol Regul Integr Comp Physiol ; 283(1): R99-106, 2002 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-12069935

RESUMO

The present study examined possible interactions between central glucagon-like peptide-1 (GLP-1) and oxytocin (OT) neural systems by determining whether blockade of GLP-1 receptors attenuates OT-induced anorexia and vice versa. Male rats were acclimated to daily 4-h food access. In the first experiment, rats were infused centrally with GLP-1 receptor antagonist or vehicle, followed by an anorexigenic dose of synthetic OT. Access to food began 20 min later. Cumulative food intake was measured every 30 min for 4 h. In the second experiment, rats were infused with OT receptor blocker or vehicle, followed by synthetic GLP-1 [(7-36) amide]. Subsequent food intake was monitored as before. The anorexigenic effect of OT was eliminated in rats pretreated with the GLP-1 receptor antagonist. Conversely, GLP-1-induced anorexia was not affected by blockade of OT receptors. In a separate immunocytochemical study, OT-positive terminals were found closely apposed to GLP-1-positive perikarya, and central infusion of OT activated c-Fos expression in GLP-1 neurons. These findings implicate endogenous GLP-1 receptor signaling as an important downstream mediator of anorexia in rats after activation of central OT neural pathways.


Assuntos
Anorexia/induzido quimicamente , Ocitocina/administração & dosagem , Receptores de Glucagon/fisiologia , Transdução de Sinais/fisiologia , Animais , Ingestão de Alimentos/efeitos dos fármacos , Glucagon/farmacologia , Peptídeo 1 Semelhante ao Glucagon , Receptor do Peptídeo Semelhante ao Glucagon 1 , Peptídeos Semelhantes ao Glucagon , Injeções Intraventriculares , Masculino , Neurônios/metabolismo , Neurotransmissores/farmacologia , Ocitocina/metabolismo , Fragmentos de Peptídeos/farmacologia , Precursores de Proteínas/farmacologia , Proteínas Proto-Oncogênicas c-fos/metabolismo , Ratos , Ratos Sprague-Dawley , Receptores de Ocitocina/fisiologia
5.
J Biol Chem ; 277(15): 12613-21, 2002 Apr 12.
Artigo em Inglês | MEDLINE | ID: mdl-11812776

RESUMO

The alpha subunit of the nicotinic acetylcholine receptor (AChR) from Torpedo electric organ and mammalian muscle contains high affinity binding sites for alpha-bungarotoxin and for autoimmune antibodies in sera of patients with myasthenia gravis. To obtain sufficient materials for structural studies of the receptor-ligand complexes, we have expressed part of the mouse muscle alpha subunit as a soluble, secretory protein using the yeast Pichia pastoris. By testing a series of truncated fragments of the receptor protein, we show that alpha211, the entire amino-terminal extracellular domain of AChR alpha subunit (amino acids 1-211), is the minimal segment that could fold properly in yeast. The alpha211 protein was secreted into the culture medium at a concentration of >3 mg/liter. It migrated as a 31-kDa polypeptide with N-linked glycosylation on SDS-polyacrylamide gel. The protein was purified to homogeneity by isoelectric focusing electrophoresis (pI 5.8), and it appeared as a 4.5 S monomer on sucrose gradient at concentrations up to 1 mm ( approximately 30 mg/ml). The receptor domain bound monoclonal antibody mAb35, a conformation-specific antibody against the main immunogenic region of the AChR. In addition, it formed a high affinity complex with alpha-bungarotoxin (k(D) 0.2 nm) but showed relatively low affinity to the small cholinergic ligand acetylcholine. Circular dichroism spectroscopy of alpha211 revealed a composition of secondary structure corresponding to a folded protein. Furthermore, the receptor fragment was efficiently (15)N-labeled in P. pastoris, and proton cross-peaks were well dispersed in nuclear Overhauser effect and heteronuclear single quantum coherence spectra as measured by NMR spectroscopy. We conclude that the soluble AChR protein is useful for high resolution structural studies.


Assuntos
Músculos/metabolismo , Pichia/genética , Receptores Nicotínicos/genética , Sequência de Aminoácidos , Animais , Células COS , DNA Complementar , Cinética , Ligantes , Ressonância Magnética Nuclear Biomolecular , Receptores Nicotínicos/química , Receptores Nicotínicos/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Torpedo , Difração de Raios X
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