How does the alcohol industry attempt to influence marketing regulations? A systematic review

Aim: To systematically review, using a qualitative, narrative synthesis approach, papers examining alcohol industry efforts to influence alcohol marketing policy, and compare with those used by the tobacco industry. Methods: Literature searches were conducted between April and July 2011, and updated in March 2013. Papers were included if they: made reference to alcohol industry efforts to influence (a) policy debates concerning marketing regulations, (b) new specific marketing policies or (c) broad alcohol policy which included marketing regulations; were written in English; and concerned the period 1990-2013. Alcohol industry political activity was categorized into strategies/tactics and frames/arguments. Data extraction was undertaken by the lead author and 100% of the papers were fully second-reviewed. Seventeen papers met the review criteria. Results: Five main political strategies and five main frames were identified. The alcohol industry argues against marketing regulation by emphasizing industry responsibility and the effectiveness of self-regulation, questioning the effectiveness of statutory regulation and by focusing on individual responsibility. Arguments relating to industry responsibility are often reinforced through corporate social responsibility activities. The industry primarily conveys its arguments through manipulating the evidence base and by promoting ineffective voluntary codes and non-regulatory initiatives. Conclusions: The alcohol industry's political activity is more varied than existing models of corporate political activity suggest. The industry's opposition to marketing regulation centres on claims that the industry is responsible and that self regulation is effective. There are considerable commonalities between tobacco and alcohol industry political activity, with differences due potentially to differences in policy contexts and perceived industry legitimacy.

Mutations of beta-arrestin 2 that limit self-association also interfere with interactions with the beta2-adrenoceptor and the ERK1/2 MAPKs:implications for beta2-adrenoceptor signalling via the ERK1/2 MAPKs

FRET (fluorescence resonance energy transfer) and co-immunoprecipitation studies confirmed the capacity of beta-arrestin 2 to self-associate. Amino acids potentially involved in direct protein-protein interaction were identified via combinations of spot-immobilized peptide arrays and mapping of surface exposure. Among potential key amino acids, Lys(285), Arg(286) and Lys(295) are part of a continuous surface epitope located in the polar core between the N- and C-terminal domains. Introduction of K285A/R286A mutations into beta-arrestin 2-eCFP (where eCFP is enhanced cyan fluorescent protein) and beta-arrestin 2-eYFP (where eYFP is enhanced yellow fluorescent protein) constructs substantially reduced FRET, whereas introduction of a K295A mutation had a more limited effect. Neither of these mutants was able to promote beta2-adrenoceptor-mediated phosphorylation of the ERK1/2 (extracellular-signal-regulated kinase 1/2) MAPKs (mitogen-activated protein kinases). Both beta-arrestin 2 mutants displayed limited capacity to co-immunoprecipitate ERK1/2 and further spot-immobilized peptide arrays indicated each of Lys(285), Arg(286) and particularly Lys(295) to be important for this interaction. Direct interactions between beta-arrestin 2 and the beta2-adrenoceptor were also compromised by both K285A/R286A and K295A mutations of beta-arrestin 2. These were not non-specific effects linked to improper folding of beta-arrestin 2 as limited proteolysis was unable to distinguish the K285A/R286A or K295A mutants from wild-type beta-arrestin 2, and the interaction of beta-arrestin 2 with JNK3 (c-Jun N-terminal kinase 3) was unaffected by the K285A/R286A or L295A mutations. These results suggest that amino acids important for self-association of beta-arrestin 2 also play an important role in the interaction with both the beta2-adrenoceptor and the ERK1/2 MAPKs. Regulation of beta-arrestin 2 self-association may therefore control beta-arrestin 2-mediated beta2-adrenoceptor-ERK1/2 MAPK signalling.