RESUMO
In facial plastic surgery, attaining hemostasis may require adjuncts to traditional surgical techniques. Fibrin tissue adhesives have broad applications in surgery and are particularly useful when addressing the soft tissue encountered in facial plastic surgery. Beyond hemostasis, tissue adhesion and enhanced wound healing are reported benefits associated with a decrease in operating time, necessity for drains and pressure dressings, and incidence of wound healing complications. These products are clinically accessible to most physicians who perform facial plastic surgery, including skin grafts, flaps, rhytidectomy, and endoscopic forehead lift.
Assuntos
Perda Sanguínea Cirúrgica/prevenção & controle , Adesivo Tecidual de Fibrina/farmacologia , Hemostasia Cirúrgica , Ritidoplastia , Cirurgia Plástica/métodos , Hemostasia Cirúrgica/instrumentação , Hemostasia Cirúrgica/métodos , Ritidoplastia/efeitos adversos , Ritidoplastia/métodos , Cicatrização/efeitos dos fármacosRESUMO
A human cDNA phage display library screen, using a phosphopeptide designed to mimic the activation loop phosphotyrosine of the Src tyrosine kinase, has identified the N-terminal SH2 domain of the p85 regulatory subunit of phosphatidyl inositol-3 kinase (PI3K) as an interacting recognition domain. Activation loop phosphorylation is known to play a conformational role in kinase activation, but is largely not thought to play a role in protein/protein recognition. Affinity chromatography and biochemical evaluation in mouse fibroblast cells has confirmed the dependence of this interaction on both the Src activation loop phosphotyrosine and the N-terminal SH2 domain of PI3K.
Assuntos
Fosfotirosina/metabolismo , Quinases da Família src/metabolismo , Animais , Biotina/análogos & derivados , Biotina/metabolismo , Ativação Enzimática , Humanos , Camundongos , Células NIH 3T3 , Fosfatidilinositol 3-Quinases/química , Fosfatidilinositol 3-Quinases/metabolismo , Fosfopeptídeos/química , Fosfopeptídeos/metabolismo , Fosfotirosina/análogos & derivados , Domínios de Homologia de src , Quinases da Família src/químicaRESUMO
A random phosphopeptide probe (bio-pYZZZ) has been used for the isolation and identification of multiple SH2 domains from human cDNA-displaying phage libraries. In addition, on-phage analysis and quantification of binding affinities for these phage-displayed proteins has shown them to be functional domains, retaining the same characteristics as in their native state.