How does globalisation interact with higher education? The continuing lack of consensus:The continuing lack of consensus

This essay attempts to ascertain whether a particular meaning of globalisation, and view on its effects and the appropriate response to it, are becoming standardised across academia. To do so, it content-analyses a representative sample of new scholarship, mapping the various approaches of current researchers towards globalisation. The essay shows how globalisation remains a contested concept within studies of higher education, as in many other fields. Rather than globalisation being taken to refer unambiguously to global flows, pressures or trends, its meaning continues to depend on the particular perspective adopted by contemporary researchers. The same conflict is apparent concerning the impacts which are reputed to globalisation and with regard to the appropriate response to globalisation amongst academics and higher education institutions (HEIs) more generally. Perhaps the only apparent point of consensus amongst contemporary researchers is the claim that globalisation affects HEIs, rather than HEIs themselves being implicated in the promotion of globalisation. This position underplays the often important role of HEIs in encouraging cross-border flows and pressures, and global trends such as marketisation.

Receptor Activity Modifying Proteins (RAMPs) interact with the VPAC2 Receptor and CRF1 receptors and modulate their function

Background and Purpose Although it is established that the receptor activity modifying proteins (RAMPs) can interact with a number of GPCRs, little is known about the consequences of these interactions. Here the interaction of RAMPs with the glucagon-like peptide 1 receptor (GLP-1 receptor), the human vasoactive intestinal polypeptide/pituitary AC-Activating peptide 2 receptor (VPAC) and the type 1 corticotrophin releasing factor receptor (CRF) has been examined. Experimental Approach GPCRs were co-transfected with RAMPs in HEK 293S and CHO-K1 cells. Cell surface expression of RAMPs and GPCRs was examined by elisa. Where there was evidence for interactions, agonist-stimulated cAMP production, Ca mobilization and GTPγS binding to G, G, G and G were examined. The ability of CRF to stimulate adrenal corticotrophic hormone release in Ramp2 mice was assessed. Key Results The GLP-1 receptor failed to enhance the cell surface expression of any RAMP. VPAC enhanced the cell surface expression of all three RAMPs. CRF enhanced the cell surface expression of RAMP2; the cell surface expression of CRF was also increased. There was no effect on agonist-stimulated cAMP production. However, there was enhanced G-protein coupling in a receptor and agonist-dependent manner. The CRF: RAMP2 complex resulted in enhanced elevation of intracellular calcium to CRF and urocortin 1 but not sauvagine. In Ramp2 mice, there was a loss of responsiveness to CRF. Conclusions and Implications The VPAC and CRF receptors interact with RAMPs. This modulates G-protein coupling in an agonist-specific manner. For CRF, coupling to RAMP2 may be of physiological significance. © 2012 The Authors. British Journal of Pharmacology © 2012 The British Pharmacological Society.

Non-peptidic antagonists of the CGRP receptor, BIBN4096BS and MK-0974, interact with the calcitonin receptor-like receptor via methionine-42 and RAMP1 via tryptophan-74

The receptor for calcitonin gene-related peptide (CGRP) has been the target for the development of novel small molecule antagonists for the treatment of migraine. Two such antagonists, BIBN4096BS and MK-0974, have shown great promise in clinical trials and hence a deeper understanding of the mechanism of their interaction with the receptor is now required. The structure of the CGRP receptor is unusual since it is comprised of a hetero-oligomeric complex between the calcitonin receptor-like receptor (CRL) and an accessory protein (RAMP1). Both the CLR and RAMP1 components have extracellular domains which interact with each other and together form part of the peptide-binding site. It seems likely that the antagonist binding site will also be located on the extracellular domains and indeed Trp-74 of RAMP1 has been shown to form part of the binding site for BIBN4096BS. However, despite a chimeric study demonstrating the role of the N-terminal domain of CLR in antagonist binding, no specific residues have been identified. Here we carry out a mutagenic screen of the extreme N-terminal domain of CLR (residues 23-63) and identify a mutant, Met-42-Ala, which displays 48-fold lower affinity for BIBN4096BS and almost 900-fold lower affinity for MK-0974. In addition, we confirm that the Trp-74-Lys mutation at human RAMP1 reduces BIBN4096BS affinity by over 300-fold and show for the first time a similar effect for MK-0974 affinity. The data suggest that the non-peptide antagonists occupy a binding site close to the interface of the N-terminal domains of CLR and RAMP1.

Do left and right asymmetries of hemispheric preference interact with attention to predict local and global performance in applied tasks?

Many cognitive neuroscience studies show that the ability to attend to and identify global or local information is lateralised between the two hemispheres in the human brain; the left hemisphere is biased towards the local level, whereas the right hemisphere is biased towards the global level. Results of two studies show attention-focused people with a right ear preference (biased towards the left hemisphere) are better at local tasks, whereas people with a left ear preference (biased towards the right hemisphere) are better at more global tasks. In a third study we determined if right hemisphere-biased followers who attend to global stimuli are likely to have a stronger relationship between attention and globally based supervisor ratings of performance. Results provide evidence in support of this hypothesis. Our research supports our model and suggests that the interaction between attention and lateral preference is an important and novel predictor of work-related outcomes. © 2012 Copyright Psychology Press Ltd.