Medical Journal of Australia

ABSTRACT • Despite leadership roles being critical, we persist with outmoded models of organisations and pay inadequate attention to developing individual leaders and new models of leadership within the medical profession. • New forms of leadership are required. Among many important roles, leaders are called on: • to enhance the meaningful identity of a profession; • to create effective linkages with other healthcare professionals and stakeholders, as well as with healthcare system managers; • to interpret complexity so that their institutions and followers can operate successfully in uncertain times ; and MJA 2004; 181: 652-654 • to consistently model ethical behaviour

Imperatives in medical education and training in response to demands for a sustainable workforce

Factors to be considered in planning our medical workforce to meet future needs include: • Need for outcomes-based curricular designs in medical schools and postgraduate training. • Shortening the length of medical training. • Improving career flexibility to permit professional reinvention. • Developing awareness within the profession about how innovation happens.4 page(s

Leadership in medicine : where are the leaders?

• Despite leadership roles being critical, we persist with outmoded models of organisations and pay inadequate attention to developing individual leaders and new models of leadership within the medical profession. • New forms of leadership are required. Among many important roles, leaders are called on: • to enhance the meaningful identity of a profession; • to create effective linkages with other healthcare professionals and stakeholders, as well as with healthcare system managers; • to interpret complexity so that their institutions and followers can operate successfully in uncertain times; and • to consistently model ethical behaviour.3 page(s

Familial polyposis coli associated with familial meningiomas

1 page(s

Aase syndrome : novel radiographic features

We report on a female with hypoplastic anemia and abnormally digitalized thumbs who presented with growth failure and novel osseous radiologic abnormalities. In addition to thumb anomalies, abnormalities of the clavicles, ilia, distal sacrum, and coccyx and described.3 page(s

Serum amyloid A : an acute phase apolipoprotein and precursor of AA amyloid

Serum amyloid A is an acute phase protein complexed to HDL as an apoprotein. The molecular weight is 11.4-12.5 kDa in different species and the protein has from 104 to 112 amino acids, without or with an insertion of eight amino acids at position 72. The protein is very well conserved throughout evolution, indicating an important biological function. The N-terminal part of the molecule is hydrophobic and probably responsible for the lipid binding properties. The most conserved part is from position 38 to 52 and this part is therefore believed to be responsible for the until now unknown biological function. The protein is coded on chromosome 11p in man, and chromosome 7 in mice, and found in all mammals until now investigated, and also in the Peking duck. In the rat a truncated SAA mRNA has been demonstrated, but no equivalent serum protein has been reported. Acute phase SAA is first of all produced in hepatocytes after induction by cytokines, but extrahepatic expression of both acute phase and constitutive SAA proteins have been demonstrated. Several cytokines, first of all IL-1, IL-6 and TNF are involved in the induction of SAA synthesis, but the mutual importance of these cytokines seems to be cell-type specific and to vary in various experimental settings. The role of corticosteroids in SAA induction is somewhat confusing. In most in vitro studies corticosteroids show an enhancing or synergistic effect with cytokines on SAA production in cultured cell. However, in clinical studies and in vivo studies in animals an inhibitory effect of corticosteroids is evident, probably due to the all over anti-inflammatory effect of the drug. Until now no drug has been found that selectively inhibits SAA production by hepatocytes. Effective anti-inflammatory or antibacterial treatment is the only tool for reducing SAA concentration in serum and reducing the risk of developing secondary amyloidosis. The function of SAA is still unclear. Interesting theories, based on current knowledge of the lipid binding properties of the protein and the relation to macrophages, in the transportation of cholesterol from damaged tissues has been advanced. A putative role in cholesterol metabolism is supported by the findings of SAA as an inhibitor of LCAT. The potential that SAA is a modifying protein in inflammation influencing the function of neutrophils and platelets is interesting and more directly related to the inflammatory process itself. SAA is the most sensitive acute phase protein characterized to date. Serum levels of SAA have been used both in diagnosis and monitoring of inflammatory and infectious diseases, and because of its sensitivity it should probably be used more for these purposes. However, fast and reliable commercial assays have not until recently been available. Since SAA is the precursor of protein AA in secondary amyloid monitoring of SAA concentrations in patients threatened by this complication seems important. Even if the role of SAA in amyloidogenesis is unclear, it it obvious that an increased serum level of SAA for a long time is a most important pathogenetic factor. Theories of impaired degradation of SAA and formation of an intermediate product, protein AA, which is incorporated in amyloid fibril is interesting, but partly contradicted by the fact that full length SAA proteins are often found in secondary amyloid. A special 'amyloid prone' isoform of SAA is found in mice, but this is probably not a universal phenomenon, as this is not the case in all species. The ability of fibril formation of SAA and SAA degradation products seems to be connected to the N-terminal hydrophobic portion of the protein, but the interactions between protein AA, amyloid P component and glucosaminoglycans in the tissues which result in fibril formation are still to be elucidated.21 page(s

Editorial : Reinventing ourselves

2 page(s

Training our future rural medical workforce

Comments.1 page(s

Rat serum amyloid P component. Analysis of cDNA sequence and gene expression

cDNA clones for rat serum amyloid P component (SAP) were isolated, and the derived amino acid sequence for pre-SAP was determined from the complete nucleotide sequence. Rat SAP is encoded by ~1 kb of mRNA, and the mature SAP protein is predicted to be 208 amino acids long. An increase in hepatic mRNA levels of rat SAP was found after administration of lipopolysaccharide, and SAP mRNA levels in livers of unstimulated male rats were lower than in hepatic RNA from female rats.4 page(s