RESUMO
The successful implementation by a large public university health service of a satellite clinic involves a number of processes and funding issues. The authors discuss the development of such a program at a small community college in Appalachia. The first 4 years' experience in operating the satellite clinic created a number of valuable management lessons that they believe could assist others with similar goals for extending their services.
Assuntos
Instituições de Assistência Ambulatorial , Planejamento em Saúde , Saúde da População Rural , Serviços de Saúde para Estudantes/organização & administração , Universidades , Adulto , Feminino , Humanos , Kentucky , MasculinoRESUMO
The current study explored the impact of varying the order of message components on coping with breast cancer information. In a 2 x 2 x 2 factorial design, threat information, coping information and order of information were manipulated. College students read persuasive essays that varied in emphasis on threat of developing breast cancer and effectiveness of breast self-examination (BSE) in averting the threat of cancer. Participants who read the high-threat message reported higher intentions to perform BSE, more rational problem solving and more hopelessness than did those who read a low-threat message. The coping information messages produced a similar pattern of results. In addition, those who read the high-coping message reported less fatalism than did participants who read the low-coping message. When threat information was presented first, the high-threat message led to less hopelessness and reliance on religious faith than when the coping information was presented first. These results demonstrate the threatening health information energizes one to act in both adaptive and maladaptive ways, and that coping information decreases the tendency to respond maladaptively to the health threat. They also suggest that the order of presentation of the information may affect the extent to which people respond adaptively.
Assuntos
Adaptação Psicológica , Neoplasias da Mama/prevenção & controle , Neoplasias da Mama/psicologia , Educação em Saúde/métodos , Comunicação Persuasiva , Autoexame de Mama , Feminino , Humanos , Serviços de Informação , Mamografia , Análise MultivariadaRESUMO
Malic enzymes are widely distributed in nature and have many biological functions. The crystal structure of human mitochondrial NAD(P)+-dependent malic enzyme in a quaternary complex with NAD+, Mn++ and oxalate has been determined at 2.2 A resolution. The structures of the quaternary complex with NAD+, Mg++, tartronate or ketomalonate have been determined at 2.6 A resolution. The structures show the enzyme in a closed form in these complexes and reveal the binding modes of the cation and the inhibitors. The divalent cation is coordinated in an octahedral fashion by six ligating oxygens, two from the substrate/inhibitor, three from Glu 255, Asp 256 and Asp 279 of the enzyme, and one from a water molecule. The structural information has significant implications for the catalytic mechanism of malic enzymes and identifies Tyr 112 and Lys 183 as possible catalytic residues. Changes in tetramer organization of the enzyme are also observed in these complexes, which might be relevant for its cooperative behavior and allosteric control.
Assuntos
Malato Desidrogenase/química , Malato Desidrogenase/metabolismo , Modelos Químicos , Regulação Alostérica , Sítios de Ligação , Catálise , Cristalografia por Raios X , Humanos , Ligação de Hidrogênio , Magnésio/metabolismo , Malato Desidrogenase/antagonistas & inibidores , Malonatos/química , Malonatos/metabolismo , Malonatos/farmacologia , Manganês/metabolismo , Modelos Moleculares , Dados de Sequência Molecular , NAD/metabolismo , Ácido Oxálico/química , Ácido Oxálico/metabolismo , Ácido Oxálico/farmacologia , Oxigênio/metabolismo , Estrutura Quaternária de Proteína , Relação Estrutura-Atividade , Tartronatos/química , Tartronatos/metabolismo , Tartronatos/farmacologia , Água/metabolismoRESUMO
A description is given of a technique that provides a relatively simple means by which O2 consumption and hemodynamic variables can be measured in exercising dogs. We used a multistage submaximal treadmill test to study the responses of 10 foxhounds to dynamic exercise. They were also studied during maximal treadmill exercise. O2 consumption increased from 16.3 +/- 1.7 ml O2 X min-1 X kg-1 at rest to 92.9 +/- 9.7 ml O2 X min-1 X kg-1 at a work load of 6.4 km/h, 20% grade and to 111.9 +/- 9.6 ml O2 X min-1 X kg-1 during maximal exercise. Cardiac output (CO) increased from 6.11 +/- 0.45 l/min at rest to 16.91 +/- 1.46 and 17.66 +/- 0.60 l/min at 6.4 km/h, 20% grade and maximal exercise, respectively. Arteriovenous O2 difference increased from 5.8 +/- 0.3 vol% at rest to 12.0 +/- 0.4 and 13.2 +/- 0.7 vol% at 6.4 km/h, 20% grade and maximal exercise, respectively. Heart rate (HR) increased from 116 +/- 7 beats/min at rest to 250 +/- 8 beats/min at 6.4 km/h, 20% grade and to 278 +/- 6 beats/min during maximal exercise. O2 uptake, CO, and arteriovenous O2 difference increased with the onset of exercise, appeared to level at lower work intensities (6.4 km/h, 4 and 8% grade), and increased significantly at each of the higher work intensities (6.4 km/h, 12, 16, and 20% grade). Additionally, we observed linear relationships between O2 consumption and HR (HR = 1.35 X VO2 + 120.5; r = 0.87; P less than 0.001) and between O2 consumption and CO (CO = 5.91 X VO2 + 216.6; r = 0.96; P less than 0.001). Further, the linear relationship between O2 consumption and CO demonstrated in the present study is similar to that observed in humans.
Assuntos
Hemodinâmica , Consumo de Oxigênio , Esforço Físico , Animais , Pressão Sanguínea , Débito Cardíaco , Cães , Feminino , Frequência Cardíaca , Métodos , Volume SistólicoRESUMO
The catalytic activity of malic enzyme (ME), a member of a new class of oxidative decarboxylases, requires the presence of divalent cations (Mn(2+), Mg(2+), and others). The crystal structure at 2.9 A resolution of human mitochondrial NAD(+)-dependent malic enzyme in a ternary complex with NAD(+) and the lanthanide ion Lu(3+), which has similar radius as Mn(2+), reveals a new conformation of the enzyme. The active site in this ternary complex is in an open form, while the organization of the tetramer of the enzyme actually resembles that with a closed active site. The Lu(3+) ion is bound to the enzyme at the same site as Mn(2+). Kinetic studies showed that Lu(3+) is a potent inhibitor of both the human NAD(P)(+)-dependent ME and the NADP(+)-dependent ME from pigeon liver, and is competitive with respect to the divalent cation, consistent with the structural information.