‘Here come “Chelsea” of Sweden’:Djurgården football club on tour in apartheid South Africa

In this article we argue that while apartheid, boycotts and South African sport have received significant coverage and focus, this has primarily been restricted to Britain and former white colonies of the Commonwealth such as Australia and New Zealand. In addition, sports such as cricket and rugby receive most attention. We argue that it is useful to consider other countries and sports engaged in apartheid South Africa. We consider Swedish engagement with apartheid South Africa and focus the case study of our analysis on the tour by champions Djurgården to the country in 1955. The tourists received favourable and widespread support in South Africa and Sweden. Yet towards the end of the tour sections of the Swedish press asked critical and probing questions of the club's tour to South Africa. We contend that the tour can be viewed as naïve and apolitical and in a similar vein to the organization of Swedish sports at that time. Only after the intensification of suppression of opposition to apartheid in South Africa from the 1960s onwards do we see a change in stance on the part of Swedish sports authorities. © 2013 © 2013 The British Society of Sports History.

Mechanism of attenuation of angiotensin-II-induced protein degradation by insulin-like growth factor-I (IGF-I)

Insulin-like growth factor-I (IGF-I) has been shown to attenuate protein degradation in murine myotubes induced by angiotensin II through downregulation of the ubiquitin-proteasome pathway, although the mechanism is not known. Angiotensin II is known to upregulate this pathway through a cellular signalling mechanism involving release of arachidonic acid, activation of protein kinase Cα (PKCα), degradation of inhibitor-κB (I-κB) and nuclear migration of nuclear factor-κB (NF-κB), and all of these events were attenuated by IGF-I (13.2 nM). Induction of the ubiquitin-proteasome pathway has been linked to activation of the RNA-activated protein kinase (PKR), since an inhibitor of PKR attenuated proteasome expression and activity in response to angiotensin II and prevented the decrease in the myofibrillar protein myosin. Angiotensin II induced phosphorylation of PKR and of the eukaryotic initiation factor-2 (eIF2) on the α-subunit, and this was attenuated by IGF-I, by induction of the expression of protein phosphatase 1, which dephosphorylates PKR. Release of arachidonic acid and activation of PKCα by angiotensin II were attenuated by an inhibitor of PKR and IGF-I, and the effect was reversed by Salubrinal (15 μM), an inhibitor of eIF2α dephosphorylation, as was activation of PKCα. In addition myotubes transfected with a dominant-negative PKR (PKRΔ6) showed no release of arachidonate in response to Ang II, and no activation of PKCα. These results suggest that phosphorylation of PKR by angiotensin II was responsible for the activation of the PLA2/PKC pathway leading to activation of NF-κB and that IGF-I attenuates protein degradation due to an inhibitory effect on activation of PKR. © 2007 Elsevier Inc. All rights reserved.