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1.
Sex Transm Infect ; 84(5): 393-4, 2008 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-18550694

RESUMO

OBJECTIVES: To examine the characteristics and work attitudes of female sex workers working in licensed brothels in Victoria, Australia. METHODS: This was a cross-sectional study of sex workers working at 38 of the 92 licensed brothels operating in Victoria during 2006. RESULTS: Of the 108 women approached, 97 (90%) completed the questionnaire. Women working in the legal sex industry in Victoria were generally aged between 23 and 35 years (51%), had completed high school (26%) and had worked in the industry for more than 5 years (43%). Half had dependent children and one third were in a relationship. Women's primary motivation for working in the sex industry was financial, whether this was the reason for their starting (56%), or the barrier to their leaving (61%). Although women valued the higher income and flexibility of this work, many were concerned about sexually transmitted infections (STI) (55%), community attitudes towards the industry (47%), their physical safety (38%) and maintaining their anonymity (37%). Over half of the women would like to leave the industry. The majority (95%) supported the monthly STI checks that are part of the Victorian regulations, with only one fifth reporting that the cost of these tests was prohibitive. CONCLUSIONS: The findings of this study indicate that women working in licensed Victorian brothels come from a diverse range of backgrounds and circumstances and hold varying attitudes towards working in the sex industry. It is hoped that these findings go some way to redressing the assumptions commonly made about women working in the sex industry and reducing the stigma associated with this occupation.


Assuntos
Atitude Frente a Saúde , Trabalho Sexual/psicologia , Adulto , Estudos Transversais , Escolaridade , Feminino , Humanos , Trabalho Sexual/estatística & dados numéricos , Vitória/epidemiologia
3.
J Intellect Disabil Res ; 50(Pt 4): 239-47, 2006 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-16507028

RESUMO

BACKGROUND: The current study describes the development and evaluation of group treatment programme for people with mild/moderate intellectual disability (ID). METHODS: A total of 34 participants (16 males, 18 females) completed the treatment programme and 15 participants (six males, nine females) comprised a control group. RESULTS: Compared to the control group, the intervention group showed an improvement in levels of depression, positive feelings about the self, and lower levels of automatic negative thoughts after the intervention. These changes were maintained at 3-month follow-up. CONCLUSIONS: These results demonstrate that intervention programmes are effective for the treatment of depression among people with ID.


Assuntos
Terapia Cognitivo-Comportamental , Transtorno Depressivo/terapia , Inteligência , Pessoas com Deficiência Mental/psicologia , Adulto , Afeto , Automatismo/psicologia , Transtorno Depressivo/psicologia , Feminino , Seguimentos , Humanos , Masculino , Pessoa de Meia-Idade , Inventário de Personalidade , Autoimagem , Percepção Social , Pensamento , Resultado do Tratamento
4.
Proc Natl Acad Sci U S A ; 96(21): 12150-5, 1999 Oct 12.
Artigo em Inglês | MEDLINE | ID: mdl-10518591

RESUMO

A comprehensive analysis of the structure of neuronal nitric oxide synthase (nNOS; EC 1.14.13.39) mRNA species revealed NOS1 to be the most structurally diverse human gene described to date in terms of promoter usage. Nine unique exon 1 variants are variously used for transcript initiation in diverse tissues, and each is expressed from a unique 5'-flanking region. The dependence on unique genomic regions to control transcription initiation in a cell-specific fashion burdens the transcripts with complex 5'-mRNA leader sequences. Elaborate splicing patterns that involve alternatively spliced leader exons and exon skipping have been superimposed on this diversity. Highly structured nNOS mRNA 5'-untranslated regions, which have profound effects on translation both in vitro and in cells, contain cis RNA elements that modulate translational efficiency in response to changes in cellular phenotype.


Assuntos
Neurônios/enzimologia , Óxido Nítrico Sintase/genética , RNA/fisiologia , Regiões 5' não Traduzidas/genética , Processamento Alternativo , Sequência de Bases , Éxons , Variação Genética , Humanos , Hibridização In Situ , Modelos Genéticos , Dados de Sequência Molecular , Fenótipo , Biossíntese de Proteínas , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Deleção de Sequência , Distribuição Tecidual
5.
Crit Rev Neurobiol ; 13(1): 21-43, 1999.
Artigo em Inglês | MEDLINE | ID: mdl-10223522

RESUMO

Neuronal nitric oxide synthase (nNOS) has been implicated in a wide variety of physiological and pathological processes. These include neurotransmission, neurotoxicity, skeletal muscle contraction, sexual function, body fluid homeostasis and atherosclerosis, among others. Consistent with the involvement of nNOS in such varied aspects of cellular biology, nNOS mRNA and protein are expressed in numerous tissues. Both its gene structure and expressional regulation are exceedingly complex. Characterization of the genomic organization of the human nNOS has revealed that the transcription unit of 29 exons spans a region greater than 240 kb at 12q24.2. The gene produces multiple mRNA transcripts via a variety of intriguing mechanisms: alternate promoter usage, alternative splicing, cassette insertions/deletions, and varied sites for 3'-UTR cleavage and polyadenylation. Allelic diversity in mRNA structure also exists. Some, but not all, of these various transcripts affect the encoded amino acid sequence and translate into nNOS protein isoforms with altered structural and functional properties. Interestingly, much of this diversity is restricted to the untranslated regions of the mRNA transcript and may affect its translation or stability. Taken together, these properties present nNOS as one of the most complex human genes described to date. Given the importance of nNOS in human health and disease, understanding this intricate genetic regulation has been a major focus in nNOS research. This review addresses the structure of the nNOS gene, its mRNA diversity, and overall genetic regulation with an emphasis on their biological implications.


Assuntos
Regulação Enzimológica da Expressão Gênica/fisiologia , Neurônios/enzimologia , Óxido Nítrico Sintase/genética , Óxido Nítrico Sintase/metabolismo , Animais , Humanos , Óxido Nítrico Sintase Tipo I , Regiões Promotoras Genéticas/fisiologia , RNA Mensageiro/genética
6.
Arch Biochem Biophys ; 359(2): 249-57, 1998 Nov 15.
Artigo em Inglês | MEDLINE | ID: mdl-9808767

RESUMO

Nitric oxide synthases (NOSs) are composed of a flavin-containing reductase domain and a heme-containing oxygenase domain. Each NOS enzyme also contains a calmodulin (CaM) binding domain and requires bound calmodulin for enzymatic activity. The CaM binding properties of the different NOS isozymes differ in the need for free calcium ions (Ca2+). We investigated CaM binding using reductase domains from the human and mouse inducible as well as the rat neuronal isoforms of NOS. An Escherichia coli expression system was designed to generate truncated recombinant NOS proteins for each isoform in which an extended CaM binding domain was either included or deleted. The reductase domains with the extended N-terminal CaM binding domains of human iNOS (residues 480-1153) and mouse iNOS (residues 474-1144) show Ca2+ binding properties that are similar to their respective holoenzymes. In addition, the iNOS reductases were active in the presence or absence of CaM. Thus, CaM does not stimulate NADPH utilization of the reductase domain in iNOS enzymes. In contrast, the rat nNOS reductase enzymes showed Ca2+-dependent CaM binding and activation.


Assuntos
Calmodulina/metabolismo , Óxido Nítrico Sintase/metabolismo , Oxirredutases/metabolismo , Fragmentos de Peptídeos/metabolismo , Animais , Proteínas de Ligação a Calmodulina/metabolismo , Catálise , Ativação Enzimática/genética , Ativação Enzimática/fisiologia , Humanos , Isoenzimas/química , Isoenzimas/genética , Isoenzimas/metabolismo , Camundongos , Mutagênese Sítio-Dirigida , Óxido Nítrico Sintase/química , Óxido Nítrico Sintase/genética , Óxido Nítrico Sintase Tipo I , Óxido Nítrico Sintase Tipo II , Oxirredução , Oxirredutases/biossíntese , Oxirredutases/genética , Fragmentos de Peptídeos/biossíntese , Estrutura Terciária de Proteína , Ratos , Deleção de Sequência , Espectrofotometria
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