Adapting a Curriculum Unit to Facilitate Interaction Between Technology, Mathematics and Science in the Elementary Classroom: Identifying Relevant Criteria

Calls for the integration of subjects continue to emanate from a wide range of professional bodies, including governments and subject associations. Yet as some authors suggest, blurring the boundaries between subjects may be one of the most daunting tasks educators face. The authors have recently begun a research study that will investigate the extent to which (a) relevant mathematics and science can be made explicit in a technology curriculum unit, (b) pupils utilise this mathematics and science learning, and (c) pupils' ability to design is enhanced by making the mathematics and science explicit and useful. This paper reports the results of Phase 1 of the study: an examination of research literature in order to identify criteria to inform the re-writing of an existing technology curriculum (to be used as a research instrument) that previously did not make explicit embedded mathematics and science concepts. Our reading of the literature has identified two essential criteria that must be met during the re-writing: (a) protecting the integrity of the subjects and (b) identifying the nature and purpose of the intended learning

Loss of Metal Ions, Disulfide Reduction and Mutations Related to Familial ALS Promote Formation of Amyloid-Like Aggregates from Superoxide Dismutase

Mutations in the gene encoding Cu-Zn superoxide dismutase (SOD1) are one of the causes of familial amyotrophic lateral sclerosis (FALS). Fibrillar inclusions containing SOD1 and SOD1 inclusions that bind the amyloid-specific dye thioflavin S have been found in neurons of transgenic mice expressing mutant SOD1. Therefore, the formation of amyloid fibrils from human SOD1 was investigated. When agitated at acidic pH in the presence of low concentrations of guanidine or acetonitrile, metalated SOD1 formed fibrillar material which bound both thioflavin T and Congo red and had circular dichroism and infrared spectra characteristic of amyloid. While metalated SOD1 did not form amyloid-like aggregates at neutral pH, either removing metals from SOD1 with its intramolecular disulfide bond intact or reducing the intramolecular disulfide bond of metalated SOD1 was sufficient to promote formation of these aggregates. SOD1 formed amyloid-like aggregates both with and without intermolecular disulfide bonds, depending on the incubation conditions, and a mutant SOD1 lacking free sulfhydryl groups (AS-SOD1) formed amyloid-like aggregates at neutral pH under reducing conditions. ALS mutations enhanced the ability of disulfide-reduced SOD1 to form amyloid-like aggregates, and apo-AS-SOD1 formed amyloid-like aggregates at pH 7 only when an ALS mutation was also present. These results indicate that some mutations related to ALS promote formation of amyloid-like aggregates by facilitating the loss of metals and/or by making the intramolecular disulfide bond more susceptible to reduction, thus allowing the conversion of SOD1 to a form that aggregates to form resembling amyloid. Furthermore, the occurrence of amyloid-like aggregates per se does not depend on forming intermolecular disulfide bonds, and multiple forms of such aggregates can be produced from SOD1