Partners in nursing education.

In this article, the authors present the efforts of several hospitals in a large southern city to collaborate on continuing education projects to meet the needs of the nursing staff. In 1985, four hospitals formed a health maintenance organization. An outgrowth was the formation of a critical care consortium whose main objective was to develop an entry level critical care course. The authors discuss the development of this course, the advantages and disadvantages of a partnership, and the results of 7 years of experience.

Delineation of the glucocorticoid-sensitive period of intestinal development in the rat.

Jejunal sucrase has been used as a marker for intestinal development. The effects of sequential adrenalectomy and sequential administration of hydrocortisone have led to the conclusion that the glucocorticoid sensitivity of the jejunum ceases abruptly at a postnatal age of 17--18 days. Adrenalectomy on day 17 or earlier resulted in significant depression of the usual developmental rise of sucrase activity, whereas adrenalectomy on days 18, 21, or 28 or in adults had no effect on sucrase activity. In contrast, the effect of adrenalectomy on body weight was similar to all ages studied. When hydrocortisone (50 microgram/g BW) was administered to intact animals on day 15 or 16, it caused significant elevation of sucrase activity but, when administered on day 17, 18, or 28, there was no difference between control and treated animals. Since adrenalectomy on day 15 delayed weaning, it was possible that the glucocorticoid dependence of the younger animals was mediated by effects on feeding behavior. However, a further study showed that complete prevention of weaning did not depress sucrase activity between days 15--21. Thus, at early ages, when the tissue was sensitive to glucocorticoid, it was independent of dietary regulation. In contrast, at later ages (days 25 and 27), prevention of weaning caused significant depression of jejunal sucrase activity.

The pathways of protein synthesis and degradation in normal heart and during development and regression of cardiac hypertrophy.

The half-life of cardiac myosin heavy chains (HC) was determined, with leucyl-tRNA as precursor, to be 5.4 days. Myosin HC are labeled more rapidly than actin; myosin light chains (LC1 and LC2) are labeled more slowly than HC. The observed differences are attributable to heterogeneity in the half-lives, e.g., actin, and to the effect of dilution by the existing macromolecular precursor pool (LC1 and LC2). Cardiac and skeletal muscle contain a population of filaments that can be released from myofibrils by ATP-relaxing solution. The easily released filaments (ERF) are devoid of alpha-actinin and M-protein. Labeling of ERF is more rapid than that of residual myofibrils. Cardiac and skeletal muscle contains calcium-activated neutral protease, which selectively removes alpha-actinin when incubated with isolated myofibrils. During development of pressure-induced cardiac hypertrophy, the labeling of LC2 is increased. In regressing cardiac hypertrophy the activities of free and total cathepsin D and of acidic RNase are unaltered.