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1.
Fam Process ; 40(4): 401-12, 2001.
Artigo em Inglês | MEDLINE | ID: mdl-11802487

RESUMO

Although the end of history has often been announced, human thought continues to renew itself, always incorporating, in each of its stages, important aspects of what has come before. In this sense, neither family therapy in general, nor its more particular postmodern orientations, have led to a radical break with the past. Neither can they claim to have reached a comfortable, definitive position. The subjectivist turn that introduced postmodernism into the systemic model has enriched it with important theoretical and practical elements, such as the critique of a therapist's supposed objectivity, circular and reflexive questioning, or the technique of externalization. This article proposes to take the renewal of systemic family therapy farther by addressing still unresolved issues, such as the role of the individual in relational systems, the place of emotions, or the construction of a relational psychopathology. The term "ultramodern family therapy" is proposed until such time as there is agreement upon a better one.


Assuntos
Filosofia Médica , Psicoterapia/tendências , Terapia Familiar/métodos , Terapia Familiar/tendências , Humanos
2.
FEBS Lett ; 480(2-3): 249-54, 2000 Sep 01.
Artigo em Inglês | MEDLINE | ID: mdl-11034339

RESUMO

C2PA is a novel protein that contains a C2 membrane binding domain, a PDZ protein/protein interaction domain, and an ATP/GTP binding domain. C2PA is expressed during embryogenesis from 8.5 days post-coitum (dpc) until birth. After birth, C2PA expression is mainly observed in the post-natal and adult testis. During spermatogenesis, C2PA transcripts are specifically observed in the spermatocytes, whereas spermatogonia and spermatids are negative. Taken together, these results suggest that C2PA might be involved in cell signaling pathways occurring during spermatogenesis.


Assuntos
Proteínas de Ligação ao GTP/genética , Proteínas Ativadoras de GTPase , Espermatogênese/fisiologia , Testículo/metabolismo , Sequência de Aminoácidos , Animais , Sequência de Bases , DNA Complementar , Proteínas de Ligação ao GTP/classificação , Proteínas de Ligação ao GTP/metabolismo , Expressão Gênica , Humanos , Masculino , Camundongos , Dados de Sequência Molecular , Proteínas RGS , Homologia de Sequência de Aminoácidos , Testículo/embriologia , Testículo/crescimento & desenvolvimento
3.
Gastroenterology ; 118(1): 70-80, 2000 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-10611155

RESUMO

BACKGROUND & AIMS: Trefoil factors (TFFs) are secreted gastrointestinal proteins that have been shown to protect and promote healing of the gastrointestinal tract. Moreover, pS2/TFF1 is essential for normal differentiation of the gastric mucosa because deficient mice develop antropyloric adenomas. To date, it is unclear how TFFs mediate their functions. METHODS: Using the yeast 2-hybrid system, we attempted to identify murine TFF1 interacting proteins by screening a stomach and duodenum complementary DNA (cDNA) expression library. RESULTS: Four positive clones were isolated. Sequence and expression studies showed that they corresponded to the murine counterpart of human cDNA sequences encoding carboxy-terminal fragments of mMuc2 (489 residues) and mMuc5AC (427, 430, and 894 residues) mucin proteins. Mutagenesis experiments showed that TFF1 interacts with the 2 mucins through binding with their VWFC1 and VWFC2 (von Willebrand factor C) cysteine-rich domains. CONCLUSIONS: These results show that the gastrointestinal protective effect of TFF1, and presumably of the other TFFs, is caused at least partially by their participation, via mucin binding, in the correct organization of the mucous layer that protects the apical side of the mucosa from deleterious luminal agents.


Assuntos
Duodeno/metabolismo , Mucosa Gástrica/metabolismo , Substâncias de Crescimento/metabolismo , Mucinas/metabolismo , Proteínas Musculares , Neuropeptídeos , Peptídeos/metabolismo , Fator de von Willebrand/metabolismo , Sequência de Aminoácidos , Animais , Sequência de Bases , Células Clonais , Cisteína , Células Híbridas , Camundongos , Dados de Sequência Molecular , Mucinas/química , Mucinas/genética , Estrutura Terciária de Proteína , RNA Mensageiro/metabolismo , Homologia de Sequência de Aminoácidos , Fator Trefoil-2 , Fator Trefoil-3 , Leveduras , Fator de von Willebrand/genética
6.
Gene ; 207(2): 171-5, 1998 Jan 30.
Artigo em Inglês | MEDLINE | ID: mdl-9511759

RESUMO

The human Lasp-1 (LIM and SH3 protein) gene was previously identified by differential screening of a breast cancer-derived metastatic lymph node cDNA library. It was located on the q12-q21 region of human chromosome 17 and was shown to be amplified and overexpressed in 12% of breast tumors. Lasp-1 defines a new LIM-protein subfamily, as it associates a C-terminal Src homology 3 (SH3) domain to a N-terminal LIM motif. In this study, the isolation and characterization of the cDNA encoding the mouse Lasp-1 protein are described, and it is shown to be highly conserved with its human counterpart. In addition to the LIM and SH3 domains, both human and mouse Lasp-1 contain an actin-binding domain. The mouse gene was mapped by in situ hybridization to the 11C-11D region of chromosome 11. Northern blot analysis shows that this gene is expressed from 7.5 to 17.5 days post-coitum of mouse embryogenesis and in almost all adult tissues.


Assuntos
Mapeamento Cromossômico , Proteínas de Homeodomínio/genética , Proteínas de Neoplasias , Proteínas Adaptadoras de Transdução de Sinal , Envelhecimento/metabolismo , Sequência de Aminoácidos , Animais , Células Cultivadas , Proteínas do Citoesqueleto , DNA Complementar , Desenvolvimento Embrionário e Fetal , Expressão Gênica , Humanos , Proteínas com Domínio LIM , Masculino , Camundongos , Dados de Sequência Molecular , Especificidade de Órgãos , Mapeamento por Restrição , Domínios de Homologia de src
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