RESUMO
The presentation of genital injuries and emergencies in pediatric girls can sometimes be misleading. A traumatic injury with excessive bleeding may be a straddle injury that requires only conservative management, while a penetrating injury may have no recognizable signs or symptoms but require extensive surgery. This issue reviews the most common traumatic genital injuries in girls presenting to the emergency department, including straddle injuries, hematomas, and impalement injuries. Nontraumatic emergencies, including hematocolpos and urethral prolapse, are also discussed. Evidence-based recommendations are presented for identifying and managing these common genital injuries and emergencies in pediatric girls.
Assuntos
Doenças dos Genitais Femininos/diagnóstico , Doenças dos Genitais Femininos/terapia , Genitália Feminina/lesões , Ferimentos não Penetrantes/diagnóstico , Ferimentos não Penetrantes/terapia , Ferimentos Penetrantes/diagnóstico , Ferimentos Penetrantes/terapia , Adolescente , Criança , Pré-Escolar , Anormalidades Congênitas , Procedimentos Clínicos , Diagnóstico Diferencial , Feminino , Doenças dos Genitais Femininos/etiologia , Humanos , Pressão Hidrostática/efeitos adversos , Hímen/anormalidades , Lactente , Insuflação , Distúrbios Menstruais/diagnóstico , Distúrbios Menstruais/etiologia , Distúrbios Menstruais/terapia , Prolapso , Doenças Uretrais/diagnóstico , Doenças Uretrais/etiologia , Doenças Uretrais/terapia , Ferimentos não Penetrantes/etiologia , Ferimentos Penetrantes/etiologiaRESUMO
E. coli GMP synthetase (GMPS) catalyzes the conversion of XMP to GMP. Ammonia, generated in the amino-terminal glutamine amidotransferase (GAT) domain, is transferred by an unknown mechanism to the ATP-pyrophosphatase (ATPP) domain, where it attacks a highly reactive adenyl-XMP intermediate, leading to GMP formation. To study the structural requirements for the activity of E. coli GMPS, we used PCR to generate a protein expression construct that contains the ATPP domain as well as the predicted dimerization domain (DD). The ATPP/DD protein is active in solution, utilizing NH (4) (+) as an NH(3) donor. Size-exclusion chromatography demonstrates a dimeric mass for the ATPP/ DD protein, providing the first evidence in solution for the structural organization of the intact GMPS. Kinetic characterization of the ATPP/DD domain protein provides evidence that the presence of the GAT domain can regulate the activity of the ATPP domain.
