Baden Rumble - Academia.edu (original) (raw)

Papers by Baden Rumble

University teaching of Biochemistry has traditionally been based on delivery of the curriculum in... more University teaching of Biochemistry has traditionally been based on delivery of the curriculum in lectures and practical classes. In this paper we describe the design and implementation of a new teaching and learning program in which student-centred learning activities in Peer Groups formed a central element of the teaching of Biochemistry. Through structured discussions, problem-solving exercises, concept mapping and a

Proceedings of The Australian Conference on Science and Mathematics Education (formerly UniServe Science Conference), Nov 13, 2012

Traditional university teaching of undergraduate biochemistry is generally delivered in lectures ... more Traditional university teaching of undergraduate biochemistry is generally delivered in lectures and laboratory classes. Online teaching environments have recently enabled different approaches to content delivery and assessment. By developing an online repository of content (lecture notes, exercises, formative and summative assessment), the academic can now construct new teaching and learning methodologies and experiences for the student, since formal lecture time can be reduced and replaced by other learning ...

Cornerstones: What do we value in higher education? Proceedings, July 12-15, Melbourne, Jul 1, 1999

Drug Development Research, Sep 1, 1995

The triterpenes lupeol (L), lupeol-3-palmitate (LP), and lupeol-3-linoleate (LL) have previously ... more The triterpenes lupeol (L), lupeol-3-palmitate (LP), and lupeol-3-linoleate (LL) have previously been shown to reduce joint destruction in adjuvant arthritic rats. In order to explain the relative antiarthritic effectiveness (LL>LP>L), the triterpenes were tested on the release of collagenase by rat osteosarcoma (bone tumor) cells, on the release of 5 Iipoxygenase inflammatory products by human neutrophils, and on CCI,-induced hepatotoxicity in rats. The rat osteosarcoma cells released collagenase which digested type I (bone) native collagen. The collagenase release, unaffected by 50 FM lupeol, decreased in the presence of lupeol linoleate and lupeol palmitate by 97% and 78%, respectively. The 30% inhibitory concentrations (lC3,J of lupeol linoleate, lupeol palmitate, and lupeol on LTB, release by the neutrophils were 27 pM, 94 FM, and >I00 p, M, respectively. All the triterpenes equally reduced hepatic fatty degeneration in CCI, rats, but only the triterpene esters significantly reduced LDH release (34% LL; 25% LP) and accelerated hepatic cell regeneration (LL>LP). The effectiveness of the triterpenes in the models of inflammatory and arthritic processes employed here corresponded with their relative antiarthritic effectiveness in adjuvant arthritic rats. o 1995 WiIey-Liss. Inc.

Annals of the New York Academy of Sciences, 1991

At the cellular level, Alzheimer's disease (AD) must be the result of neuronal dysfunction an... more At the cellular level, Alzheimer's disease (AD) must be the result of neuronal dysfunction and degeneration leading to a reduction in synaptic density. Filamentous deposits of amyloid, which define the disease at the molecular level, occur within perikarya, axons, dendrites, and terminals of neurons as neurofibrillary tangles (NFT), in the extracellular neuropil as amyloid plaques (APC), and around blood vessels as amyloid congophilic angiopathy (ACA). These fibrillar amyloid protein aggregates are also found in the brain of all individuals with Down's syndrome after the age of 30 years. The amyloid deposits apparently occur in the terminal zones of neurons that develop NFT. It is suggested that amyloid deposition is of fundamental significance in AD and that a thorough understanding of amyloid formation will eventually lead to successful therapeutic intervention in AD. As elucidation of the reasons behind amyloid deposition must shed some light on the pathogenesis of AD, we...

New England Journal of Medicine, 1989

In patients with Alzheimer's disease, amyloid fibrils that are aggregates of A4 protein subu... more In patients with Alzheimer's disease, amyloid fibrils that are aggregates of A4 protein subunits are deposited in the brain. A similar process occurs at an earlier age in persons with Down's syndrome. To investigate the deposition of amyloid in these diseases, we used a radioimmunoassay to measure levels of the amyloid precursor (PreA4) in the serum of 17 patients with Down's syndrome, 15 patients with Alzheimer's disease, and 33 normal elderly controls. The mean (+/- SD) concentration of serum PreA4 was increased 1.5-fold in patients with Down's syndrome (2.49 +/- 1.13 nmol per liter) as compared with that in controls (1.68 +/- 0.49 nmol per liter; P less than 0.007); the levels in patients with Alzheimer's disease were similar to those in controls (1.83 +/- 0.78; P less than 0.98). We also found that the concentration of PreA4 in the brain tissue of two adults with Down's syndrome (100 and 190 pmol per gram) was higher than that in the brain tissue of either 26 patients with Alzheimer's disease (64.4 +/- 17.3 pmol per gram) or 17 elderly controls with neurologic disease (68.5 +/- 26.3 pmol per gram). Immunocytochemical studies of brain tissue from 26 patients with Down's syndrome showed that the deposition of A4 protein amyloid began in these patients approximately 50 years earlier than it began in 127 normal aging subjects studied previously, although the rate of deposition was the same. We conclude that, since the gene for PreA4 is on the long arm of chromosome 21, which is present in triplicate in Down's syndrome, overexpression of this gene may lead to increased levels of PreA4 and amyloid deposition in Down's syndrome. However, since increased levels of PreA4 are not present in Alzheimer's disease, additional factors must account for the amyloid deposition in that disorder.

Journal of Neurochemistry, 1992

The major component of the amyloid deposition that characterizes Alzheimer's disease is the 4-kDa... more The major component of the amyloid deposition that characterizes Alzheimer's disease is the 4-kDa PA4 protein, which is derived from a much larjjer amyloid protein precursor (APP). A procedure for the complete purification of APP from human brain is described. Thc same amino terminal sequence of APP was found in two patients with Alzheimer's disease and one control subject. Two major forms of APP were identified in human brain with apparent molecular masses of 100-1 10 kDa and 120-1 30 kDa. Soluble and membrane fractions of brain contained nearly equal amounts of APP in both humans and rats. Immunoprecipitation with carboxyl terminus-directed antibodies indicates that the soluble forms of APP are truncated. Carboxyl ter-APP7,0 (Kitaguchi et al., 1988; Golde et al., 1990; Jacobsen et al., 1991). The isoforms APP,,, and APP7,0 are generated by the inser-iSOfOlTllS APP

Drug Development Research, 1995

Adult male Wistar rats were made arthritic by the subplantar injection of complete Freund's adjuv... more Adult male Wistar rats were made arthritic by the subplantar injection of complete Freund's adjuvant. Oral treatment with the triterpenes lupeol, luepol palmitate, or lupeol linoleate (66 mg/kg BW every 2 days) from days 24 to 32 reduced synovial granulomatous growth (proximal interphalangeal foot joints) and its invasion of the synovial cavity and reduced the destruction of articular cartilage and subchondral bone (lupeol linoleate > lupeol palmitate > lupeol). Rats treated with the lupeol esters showed reduced periosteal bone erosion with bone repair in the form of periosteal new bone formation. Arthritic rat blood lymphocytes and serum levels of the joint degradative product, hyaluronate, which increased by 73% and 51 %, respectively, were reduced by the triterpenes (lupeol linoleate > lupeol palmitate > lupeol) with lupeol linoleate restoring them to normal values. The antiarthritic effectiveness of lupeol was therefore increased by esterification with the long-chain fatty acids. I C 1995 Wiley-Liss, Inc.

Annals of Neurology, 1992

PA4 amyloid deposition in the brain, which is characteristic of Alzheimer's disease (AD), may res... more PA4 amyloid deposition in the brain, which is characteristic of Alzheimer's disease (AD), may result from either overexpression of the amyloid protein precursor (APP) or failure of APP to be correctly processed. A blood marker reflecting this abnormal metabolism would be of diagnostic value and would provide a means of monitoring the efficacy of therapeutic interventions. We analyzed immunoblots of plasma APP enriched by heparin-Sepharose chromatography from patients with moderate to severe AD dementia (n = 34) and control subjects (n = 77) and found an approximately 50% increase in the proportion of 130-kd APP species in patients with AD (p < 0.001), no difference in the 110-kd form, a 15 to 30% decrease in the 65-kd form (p < 0.001), and a 20 to 35% decrease in the proportion of 42-kd APP (p < 0.001). These species of APP were soluble, lacked the carboxyl terminus, and the 110-and 42-kd species were shown to be consistent with degradation products derived from the 130-kd species. A comparison of levels of 130-kd plasma APP from moderately to severely demented patients with AD and control subjects distinguished the two groups with a specificity of 87.0% and a sensitivity of 79.4%.

Brain Research, 1996

We have previously found that the amyloid precursor protein (APP) of Alzheimer's disease ... more We have previously found that the amyloid precursor protein (APP) of Alzheimer's disease is present on the surface of rat cortical neurons in culture, in a segmental pattern which first becomes evident after 24 hours and is fully developed by five days. As APP has previously been reported to have a short half-life in neuronal cell lines, and has been shown to contain binding sites for various extracellular matrix components within its extracellular domain, we hypothesized that APP would be associated with portions of neurites undergoing rapid structural change, such as growth cones. To test this hypothesis, we observed selected neurons by video time-lapse differential interference microscopy on 24-hour-old primary rat neuronal cultures for up to 45 minutes, followed by fixation and immunocytochemistry to ascertain surface APP distribution on those same neurons. In contrast to our predictions, surface APP was not found on active portions of neurites, even if the activity produced no net translational movement. This result indicates that surface APP is actually associated with stable portions of neurites, a conclusion that tallies with other recent results showing that neuronal surface APP has a longer half-life than general cellular APP, and is associated with markers of adhesion patches, which themselves are relatively stable structures.