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Nutrition has traditionally involved in supplying energy and hydration. An emerging concept developed by the authors is the concept of using omega-3 fatty acids (n-3 FAs) to increase the resilience of the brain. The n-3 FAs have numerous proven benefits including support of cardiovascular and psychiatric health. Docosahexaenoic acid in particular, is found in high concentrations in the brain. N-3 FAs provide benefits by exerting a protective mechanism at the cellular and neuronal levels including the modulation of inflammatory cascade following traumatic brain injury. Promising research and evolving clinical experience now indicate that n-3 FA is useful and effective for recovery following traumatic brain injury. More exciting is that new laboratory research shows the beneficial effects extend to when n-3 FA is given before injury. Given the safety profile, availability, and affordability of n-3 FA, Generally Recognized As Safe amounts of eicosapentaenoic acid and docosahexaenoic acid (up to 3,000 mg daily) should be considered for the athlete and soldier, not only for its general health benefits, but particularly also for those at risk or high exposure to brain impacts. A comprehensive, coordinated research program to evaluate the multiple uses of n-3 FA should be a high priority for the Department of Defense. [ABSTRACT FROM AUTHOR]

Fifty-three patients with atopic eczema took part in a double blind controlled cross-over trial of an egg and cow's milk exclusion diet. Response to the diet was assessed in terms of areas affected, day and night time itch, and topical steroid usage. Twenty-five percent of the patients failed to comply adequately with the trial regime and were excluded from the analysis. Of the remaining 40 patients, ten appeared to benefit from the diet and were advised to continue egg and milk avoidance. This response rate to the diet was not statistically significant. [ABSTRACT FROM AUTHOR]

The article presents a study that deals with twofold improved tumor-to-brain contrast using a novel T1 relaxation-enhanced steady-state (T1RESS) MRI technique. It mentions the T1RESS, a novel magnetic resonance imaging (MRI) pulse sequence that enables the flexible modulation of T1 weighting and provides the unique feature that intravascular signals can be toggled on and off in contrast-enhanced scans.

We have used in situ hybridization and computer-aided reconstruction to study the spatial distribution of expression of the mammary tumor proto-oncogene int-1 during mouse embryogenesis. int-1 RNA accumulation is restricted to specific regions of the neural plate and its derivatives between 9 and 14.5 days of development. int-1 RNA accumulates throughout the neural plate at the anterior head folds of the 9 day embryo but only at its lateral tips in more posterior regions. Following neural tube closure, int-1 expression is restricted to specific regions of the dorsal wall of the brain ventricles and spinal cord, the ventral wall of the midbrain and the diencephalon, and the lateral walls of the neuroepithelium at the midbrain-hindbrain junction. These data suggest that int-1 has a role in the early stages of central nervous system development in the mouse embryo.

Several overlapping cDNA clones encompassing 2760 nucleotides of the alpha-subunit of a human non-erythroid spectrin (termed fodrin) were isolated from a human lung fibroblast cDNA library. DNA and RNA blot analyses indicated that a single copy alpha-fodrin gene encodes a 9-kb transcript. The cDNA clones were sequenced, and all were found to contain long open reading frames. The overlapping regions were identical except for a 60-nucleotide inframe insertion at position 1133 in the composite sequence. This result suggests that at least two distinct transcripts exist in fibroblast cells. The chromosomal location of human alpha-fodrin was assigned to 1p34-1p36.1 by hybridization to somatic cell hybrids, and it is thus distinct from that of human alpha-spectrin which has been mapped to 1q22-1q25. Alignment of the composite 919 amino acids of the predicted protein sequence of human alpha-fodrin with that of human alpha-spectrin indicated that alpha-fodrin has a similar 106-amino-acid repeating structure, which is homologous with alpha-spectrin repeats 7-15. Repeats 10 and 11 are anomalous in sequence and structure from other repeats. A comparison of nucleic acid and amino acid homologies between alpha-spectrin and the alpha-fodrin of several vertebrates indicated that human non-erythroid alpha-fodrin and the common alpha-subunit of erythroid and non-erythroid cells of non-mammalian vertebrates are closely related (90%-96% amino acid homology), whereas alpha-fodrin is only distantly related to the erythroid-specific alpha-spectrin subunit of mammals (55%-59% amino acid homology). These data suggest that mammalian erythroid alpha-spectrin evolved by duplication and rapid divergence from an ancestral alpha-fodrin-like gene.

The pattern of protein synthesis in 8-, 9- and 10-day post coitum (p.c.) mouse embryos was examined by 2-D gel electrophoresis of [35S]methionine-labelled proteins. Of the 600-800 polypeptides detected only one, a 14 X 10(3) Mr (14K) protein, was found to accumulate over this period. To isolate cDNA clones that potentially encode this protein, 32P-labelled cDNA was synthesized from 9 and 10 days p.c. embryo poly(A) +RNA, and used for the differential screening of an 8.5-day p.c. mouse embryo cDNA library cloned in lambda gt10. Six clones that hybridized strongly to the 10-day probe were purified and their inserts subcloned into plasmid vectors. Cross hybridization and restriction mapping of these inserts indicate that they fall into four distinct groups. Each of these hybridize with transcripts of approximately 600 nucleotides, which accumulate in the embryo from 9 to 10 days p.c. Expression was barely detectable in adult tissues and restricted to liver and spleen. Expression of one of these clones, 10.1, was examined by in situ hybridization of 35S-labelled RNA probes to 8.5-12.5 day p.c. embryo sections. Strong hybridization was observed in yolk sac blood islands, fetal liver and embryonic erythrocytes, suggesting that 10.1A encodes an erythrocyte-specific protein. DNA sequence analysis indicates that the four classes of cDNA were derived from transcripts of the alpha 1, zeta, beta h1 and epsilon globin genes. Labelling of 10-day p.c. erythrocyte proteins with [35S]methionine, followed by 2-D gel electrophoresis, clearly demonstrates that the most abundant polypeptide migrates to the same position as the 14K protein which accumulates from 8 to 10 days p.c. Thus the only abundant transcripts and corresponding proteins that change over a period of profound morphogenetic change correspond to globins of the newly established blood system.