The influence of the ACTH-derived short regulatory peptide on the rabbit behaviour.
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Biomedical subjects
Publications and source records attributed to M Teter.
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During an 8-week period in the winter of 1986-87, there were 11 deaths from an adenovirus infection (case fatality rate = 39%, 11/28) in a long-term care paediatric facility in southern New Jersey. Among the 61 resident children, all with severe congenital and/or acquired disabilities, 28 developed a febrile respiratory illness compatible with adenovirus infection [attack rate (AR) = 46%]. Patients with tracheostomies were three times as likely to become ill [relative risk (RR) = 3.2, 95% confidence intervals (CI) = 1.8-5.6]. Twenty-three members of the staff had a similar febrile illness (AR = 22%, 23/106); nurses were more likely to be ill than other staff (RR = 3.0, 95% CI = 1.1-11.4). Adenovirus 7 was isolated from four of the case patients and adenovirus 1 from one. The findings suggest prolonged transmission between patients and nursing staff with lack of cohorting of ill patients probably contributing to the prolongation of the outbreak. This investigation indicates that adenoviral outbreaks, although rare, can have a high mortality in severely disabled children, and that future outbreak investigations should examine the use of vaccines or antiviral agents to reduce mortality and for outbreak control.
Human skin fibroblasts secrete collagenase as two proenzyme forms (57 and 52 kDa). The minor (57-kDa) proenzyme form is the result of a partial posttranslational modification of the major (52-kDa) proenzyme through the addition of N-linked complex oligosaccharides. Human endothelial cells as well as fibroblasts from human colon, cornea, gingiva, and lung also secrete collagenase in two forms indistinguishable from those of the skin fibroblast enzyme. In vitro tissue culture studies have shown that the level of constitutive synthesis of this fibroblast-type interstitial collagenase is tissue specific, varies widely, and correlates with the steady-state level of a single collagenase-specific mRNA of 2.5 kilobases. The tumor promoter, phorbol 12-myristate 13-acetate, apparently blocks the control of collagenase synthesis resulting in a similarly high level of collagenase expression (approximately equal to 3-7 micrograms of collagenase per 10(6) cells per 24 hr) in all examined cells. The constitutive level of synthesis of a 28-kDa collagenase inhibitor does not correlate with that of the enzyme. Phorbol 12-myristate 13-acetate stimulates the production of this inhibitor that in turn modulates the activity of collagenase in the conditioned media. As a result, the apparent activity of the enzyme present in the medium does not accurately reflect the rate of its synthesis and secretion.
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