Corneal asphericity in eye bank eyes implanted with the intrastromal corneal ring

The endogenous circadian rhythm of melatonin in humans provides information regarding the resetting response of the human circadian timing system to changes in the light-dark (LD) cycle. Alterations in the LD cycle have both acute and chronic effects on the observed melatonin rhythm. Investigations to date have firmly established that the melatonin rhythm can be reentrained following an inversion of the LD cycle. Exposure to bright light and darkness given over a series of days can rapidly induce large-magnitude phase shifts of the melatonin rhythm. Even single pulses of bright light can shift the timing of the melatonin rhythm. Recent data have demonstrated that lower light intensities than originally believed are capable of resetting the melatonin rhythm and that stimulation of photopically sensitive photoreceptors (i.e., cones) is sufficient to reset the endogenous circadian melatonin rhythm. In addition to phase resetting, exposure to light of critical timing, strength, and duration can attenuate the amplitude of the endogenous circadian rhythm of melatonin. Measurement of melatonin throughout resetting trials provides a dynamic view of the resetting response of the human circadian pacemaker to light. Future studies of the melatonin rhythm in humans may further characterize the resetting response of the human circadian timing system to light.     

Athlete''s heart in elite disabled athletes

Nineteen children with congenital upper alimentary tract malformation were studied prospectively at the Department of Paediatrics, University College Hospital (UCH), Ibadan, over a period of 12 months. There were 20 cases, grouped into six types comprising congenital hypertrophic pyloric stenosis, seven; cleft lip and/or cleft palate, five; oesophagal atresia with or without tracheo-oesophageal fistula, four; jejunal atresia two and a case each of achalasia and annular pancreas. One patient had oesophageal atresia and congenital hypertrophic pyloric stenosis. The mortality rate was 31.51% (six out of nineteen). Low mortality was recorded in cases of cleft lip and/or palate, while mortalities of over 70% were recorded among cases of jejunal atresia, and oesophageal atresia with or without tracheo-oesophageal fistul. The common causes of death were milk feed aspiration (28.6%-two cases), purulent peritonitis (14.3%-one case), and probable septicaemia (14.3%-one case). The cause of death in two cases could not be determined.     

Comparison of professional judgment versus an algorithm for nutrition status classification

OBJECTIVES: The classification of a patient's nutrition status is important for identifying patients who require nutrition care, for designing effective nutrition interventions, and for measuring severity of illness. The objective of this study was to evaluate the reliability and validity of two variants of the Department of Veterans Affairs' nutrition status classification: professional judgment versus an algorithm. METHODS: The study consisted of two phases, both of which included providing a sample of approximately 60 registered dietitians and 60 clinical dietetic technicians with data on 16 (phase I) and 20 (phase II) patients, to which they assigned nutrition statuses using both professional judgment and the algorithm. Improvements in instructions and training were implemented between the two phases. Interrater reliability of the responses was calculated, and content validity was measured by comparing the staff's responses with those of an expert panel. RESULTS: Reliability improved significantly between phases for both professional judgment and the algorithm. Greater reliability and validity were observed with use of the algorithm, by both dietitians and technicians, during both phases. CONCLUSION: Classification of a patient's nutrition status is important in the delivery of cost-effective health care. The Department of Veterans Affairs' nutrition status classification is a good one for assessing nutrition status quickly and reliably, especially when an algorithm is used. The results underscore the advantages of a classification system based on an algorithm when the system is designed to be used by many different staff across multiple facilities.     

Involvement of amino acid residues 423-429 of human protein S in binding to C4b-binding protein

Human protein S binds to C4b-binding protein (C4BP) both in plasma and in a system using purified proteins. Amino acid residues 420-434 of the first disulfide loop of the sex hormone binding globulinlike domain of protein S are involved in the interaction of protein S with C4BP. To define the involvement of specific polar amino acids within residues 420-434, we studied in parallel synthetic protein S peptides and recombinant protein S variants containing the same amino acid replacements, K423E, E424K, Q427E and K429E. Synthetic peptide analogs of peptide PSP-420 (residues 420-434) were assayed for binding C4BP and as inhibitors of complex formation. The PSP-420 peptide and the analogous peptide with the substitution E424K, but not the peptides containing the substitutions K423E and K429E, were able to bind C4BP. Recombinant proteins with mutations of K423E, Q427E and K429E showed reduced affinity for C4BP compared to plasma protein S, recombinant wild type protein S, or E424K-protein S. These results suggest that Lys-423, Gln-427 and Lys-429 of protein S are important for normal binding to C4BP. The anti-protein S monoclonal antibody LJ-56, raised against peptide PSP-420, recognizes only free protein S and inhibits complex formation with C4BP. Antibody LJ-56 recognized the E424K and Q427E peptides but not the K423E or K429E peptides. Similarly, the E424K and Q427E protein S mutants were recognized by LJ-56, whereas the K423E and K429E protein S mutants were not recognized. This suggests that both in the peptide PSP-420 and in protein S, Lys-423 and Lys-429 significantly contribute to binding to antibody LJ-56. These results demonstrate that protein S residues 423, 427 and 429, but not residue 424, are involved in binding to both the antibody LJ-56 and to C4BP. When peptides PSP 420 and SL-6 (residues 447-460) with carboxyterminal amide or carboxylate moieties were compared to their ability to inhibit C4BP-protein S complexation, PSP-420-amide was the most potent. This finding together with the other results described here supports the hypothesis that the residues 420 and 434 in protein S provides a major binding site for C4BP.