Familial ring (19) chromosome mosaicism: case report and review

Ring (19) chromosomal mosaicism has been identified in a 14-month-old girl referred for cytogenetic evaluation due to microcephaly and developmental delay with autistic-like mannerisms. An analysis of her peripheral blood lymphocytes showed a 46,XX,r(19) cell line in 119/121 of cells examined. Of the two remaining cells, one had a normal female chromosome complement and the other showed loss of one of the chromosome 19 homologs. Further analysis by fluorescence in situ hybridization using an all human telomere probe showed the presence of a single hybridization signal on the r(19) chromosome. Subsequent cytogenetic characterization of cells derived from the patient's phenotypically normal mother also demonstrated the presence of a ring 19 chromosome in 4/100 cells. The remaining cells had a normal female chromosome complement. These findings represent the first reported case of familial ring 19 mosaicism. The cytogenetic and clinical findings in these two individuals are discussed in relation to six previously reported cases of de novo ring chromosome 19 mosaicism.     

Religion's role in adjustment to a negative life event: Coping with the loss of a child.

Parents (N?=?124) who had lost an infant to sudden infant death syndrome were interviewed 3 wks and 18 mo postloss. Two components of religion (religious participation and religious importance) were assessed, and their relations with 3 coping-process variables (perceived social support, cognitive processing of the loss, and finding meaning in the death) were examined. Greater religious participation was related to increased perception of social support and greater meaning found in the loss. Importance of religion was positively related to cognitive processing and finding meaning in the death. Furthermore, through these coping-process variables, religious participation and importance were indirectly related to greater well-being and less distress among parents 18 mo after their infants' deaths. Results suggest that further study of the social and cognitive aspects of religion would be profitable. (PsycINFO Database Record (c) 2010 APA, all rights reserved)     

Tripe palms: a cutaneous paraneoplastic syndrome

Tripe palms is a cutaneous paraneoplastic syndrome. We report a case of tripe palms in a 71-year-old man with non-small cell lung cancer. Approximately 90% of patients with tripe palms have an associated cancer, most commonly involving the lung or the stomach. Any patient with tripe palms must have a complete cancer workup, especially for lung and stomach cancer.     

Explosion risks during the confined storage of bituminous coals : Calculation of gaseous hydrogen accumulation in ship holds

Bituminous coal piles stored in the open air can undergo autocatalytic heating accompanied by the emission of small but appreciable amounts of molecular hydrogen. When the coal is contained in a confined space and the temperature reaches 40°C, accumulation of hydrogen is expected. This process has been observed for a wide variety of bituminous coals. The amount of hydrogen gas expected to accumulate in the air pocket above the coal cargo in ship holds (assuming that the coal's temperature approaches 40°C during the voyage) has been calculated. The results clearly indicate that in most cases the hydrogen concentration will be appreciably above the lower explosion limit in air. Hence when bituminous coals are stored in a confined space (e.g. a ship hold), the explosive risk of hydrogen should be taken into account.     

Electron transfer by domain movement in cytochrome bc1

The cytochrome bc1 is one of the three major respiratory enzyme complexes residing in the inner mitochondrial membrane. Cytochrome bc1 transfers electrons from ubiquinol to cytochrome c and uses the energy thus released to form an electrochemical gradient across the inner membrane. Our X-ray crystal structures of the complex from chicken, cow and rabbit in both the presence and absence of inhibitors of quinone oxidation, reveal two different locations for the extrinsic domain of one component of the enzyme, an iron-sulphur protein. One location is close enough to the supposed quinol oxidation site to allow reduction of the Fe-S protein by ubiquinol. The other site is close enough to cytochrome c1 to allow oxidation of the Fe-S protein by the cytochrome. As neither location will allow both reactions to proceed at a suitable rate, the reaction mechanism must involve movement of the extrinsic domain of the Fe-S component in order to shuttle electrons from ubiquinol to cytochrome c1. Such a mechanism has not previously been observed in redox protein complexes.