RESUMO
Assessment is the undergirding of palliative care and of geriatrics care. Both disciplines insist on a comprehensive assessment that includes personal and social aspects of the patient's illness experience. At the same time, both face challenges due to the amount of time and skill needed to encompass such a broad scope and the often heavy illness burden of the patients, which makes interaction stressful or difficult. This article examines question-based assessment instruments in palliative care for elders. Important in all aspects of medicine, reliance on verbal assessments is of special importance in palliative care.
Assuntos
Avaliação Geriátrica , Indicadores Básicos de Saúde , Cuidados Paliativos , Idoso , Humanos , Medição da Dor , Qualidade da Assistência à Saúde , Perfil de Impacto da Doença , Apoio Social , Inquéritos e QuestionáriosRESUMO
Caspases are critical proapoptotic proteases that execute cell death signals by selectively cleaving proteins at Asp residues to alter their function. Caspases trigger apoptotic chromatin degradation by activating caspase-activated DNase and by inactivating a number of enzymes that sense or repair DNA damage. We have identified the mismatch repair protein MLH1 as a novel caspase-3 substrate by screening small pools of a human prostate adenocarcinoma cDNA library for cDNAs encoding caspase substrates. In this report, we demonstrate that human MLH1 is specifically cleaved by caspase-3 at Asp(418) in vitro. Furthermore, MLH1 is rapidly proteolyzed by caspase-3 in cancer cells induced to undergo apoptosis by treatment with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) or the topoisomerase II inhibitor etoposide, which damages DNA. Importantly, proteolysis of MLH1 by caspase-3 triggers its partial redistribution from the nucleus to the cytoplasm and generates a proapoptotic carboxyl-terminal product. In addition, we demonstrate that a caspase-3 cleavage-resistant D418E MLH1 mutant inhibits etoposide-induced apoptosis but has little effect on TRAIL-induced apoptosis. These results indicate that the proteolysis of MLH1 by caspase-3 plays a functionally important and previously unrecognized role in the execution of DNA damage-induced apoptosis.