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- Andersen, Paul Krüger, et al.
(författare)
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Response to the Proposal for a Directive on Corporate Sustainability Due Diligence by Nordic and Baltic Company Law Scholars
- 2022
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Annan publikation (övrigt vetenskapligt/konstnärligt)abstract
- On February 23, 2022, The EU Commission published its Proposal for a Directive of the European Parliament and of the Council on Corporate Sustainability Due Diligence and amending Directive (EU) 2019/1937 (“CSDDD” or “the Proposal”). The purpose of the Proposal, to further the “Union’s transition to a climate-neutral and green economy in line with the European Green Deal and in delivering on the UN Sustainable Development Goals”, is of great importance, and the Commission’s initiative is therefore commendable. However, it is our firm opinion that the Proposal should not be enacted in its present form, and that if it were to be, it would not only damage European businesses but also run the risk of having an adverse effect on both the transition to a climate-neutral economy as well as the goal of delivering on the UN Sustainable Development Goals. This is to a large extent because many of the Proposal’s provisions are excessive, unfounded and disproportionate and as such in violation of the fundamental principles of subsidiarity and proportionality safeguarded by Art. 5 TEU as well as having a questionable basis in Art. 50 TFEU. Furthermore and in regard of procedure, we find that the presentation of the Proposal by the Commission represents a disregard for the principles of better regulation that should not pass unnoticed and must be observed in the future to maintain trust in the legislative process of the Union.In this response to the consultation, we have presented an analysis of the key issues of the Proposal from a corporate governance perspective. We have divided the response into two parts: one on the pure corporate governance parts of the Proposal (article 15, 25 and 26) and one of the due diligence parts of the Proposal. With regards to the corporate governance parts of the Proposal, our conclusion is that they, by and large, should not be included in the proposed directive at all. Including them would in several ways be in breach of the EU principles on subsidiarity and proportionality, but perhaps more importantly, they are not only unsubstantiated by available empirical evidence on corporate behaviour, but also refuted by what we know. There is also good reason to believe that the proposed rules on director’s duties and environmental remuneration would risk decreasing the effectiveness of the stock markets within the EU contrary to the goal of a Capital Market Union, which also risk slowing down the necessary transition to a green economy and the goals of the EU Green Deal. The regulation necessary for the Capital Market Union and the EU Green Deal should complement each other, not collide as would be the outcome if the Proposal is adopted in its present form.With regards to the due diligence parts of the Proposal, our criticism is limited to corporate governance aspects and far less fundamental. We primarily believe that grounds for harmonisation needs further consideration in the present very challenging times, that Article 22 on Civil Liability might in several ways be counter-productive to the goals of the Proposal, that the effects on SMEs as well as for the financial companies included covered by the Proposal warrants further analysis, that the choice to focus the Proposal on individual companies instead of company groups needs to be reviewed, and that a risk based approach should be taken rather than an approach were companies are unable to focus their efforts to where they can be most effective. Overall, these issues can be worked out, but if they are not, then the proposed directive would not only have a severe adverse impact on EU companies and possibly capital markets, but might actually hinder EU companies from acting in the way that the Proposal aims for them to do.This joint response to the public consultation is made by a group of Nordic and Baltic company law scholars who, although we may not agree on every detail, do share the main arguments and grave concerns expressed here.
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| 3. |
- Yamada, Takashi, et al.
(författare)
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Impaired Myofibrillar Function in the Soleus Muscle of Mice With Collagen-Induced Arthritis
- 2009
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Ingår i: Arthritis and Rheumatism. - : Wiley. - 0004-3591 .- 1529-0131. ; 60:11, s. 3280-3289
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Tidskriftsartikel (refereegranskat)abstract
- Objective. Progressive muscle weakness is a common feature in patients with rheumatoid arthritis (RA). However, little is known about whether the intrinsic contractile properties of muscle fibers are affected in RA. This study was undertaken to investigate muscle contractility and the myoplasmic free Ca2+ concentration ([Ca2+](i)) in the soleus, a major postural muscle, in mice with collagen-induced arthritis (CIA). Methods. Muscle contractility and [Ca2+](i) were assessed in whole muscle and intact single-fiber preparations, respectively. The underlying mechanisms of contractile dysfunction were assessed by investigating redox modifications using Western blotting and antibodies against nitric oxide synthase (NOS), superoxide dismutase (SOD), 3-nitrotyrosine (3-NT), carbonyl, malondialdehyde (MDA), and S-nitrosocysteine (SNO-Cys). Results. The tetanic force per cross-sectional area was markedly decreased in the soleus muscle of mice with CIA, and the change was not due to a decrease in the amplitude of [Ca2+](i) transients. The reduction in force production was accompanied by slowing of the twitch contraction and relaxation and a decrease in the maximum shortening velocity. Immunoblot analyses showed a marked increase in neuronal NOS expression but not in inducible or endothelial NOS expression, which, together with the observed decrease in SOD2 expression, favors peroxynitrite formation. These changes were accompanied by increased 3-NT, carbonyl, and MDA adducts content in myofibrillar proteins from the muscles of mice with CIA. Moreover, there was a significant increase in SNO-Cys content in myosin heavy-chain and troponin I myofibrillar proteins from the soleus muscle of mice with CIA. Conclusion. These findings show impaired contractile function in the soleus muscle of mice with CIA and suggest that this abnormality is due to peroxynitrite-induced modifications in myofibrillar proteins.
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| 4. |
- Östberg, Therese
(författare)
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Characterisation of HMGB1 in inflammation
- 2008
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Doktorsavhandling (övrigt vetenskapligt/konstnärligt)abstract
- High mobility group box chromosomal protein 1 (HMGB1) was discovered over three decades ago as a nuclear protein which is present in all mammalian nucleated cells. Subsequent studies have revealed additional properties of HMGB1 besides its originally described nuclear functions. Extracellular HMGB1 induces cellular migration, recruits stem cells, possesses antibacterial functions and somewhat surprisingly is involved in proinflammatory responses. HMGB1 can be released from certain cells in two distinct ways, either passively by dying cells or through active release from multiple cell types such as myeloid cells. The active secretion of HMGB1 is mediated via a non-classical pathway involving secretory lysosomes, a route sharing many features with the IL-1β secretion pathway. My studies of macrophages from RAGE gene-deficient mice indicate that RAGE is the major functional receptor for HMGB1 on these cells. The results also show that HMGB1 interacts with additional receptor(s), since the absence of RAGE molecules did not completely abolish HMGB1-induced cytokine production. HMGB1 needed to form complexes with selected endogenous and exogenous danger signals in order to promote inflammation, as highly purified HMGB1 on its own did not induce cytokine production. I have demonstrated the potential involvement of HMGB1 in the pathogenesis of a novel spontaneous experimental arthritis model, DNase II x Interferon type I receptor double gene-deficient mice. Marked, aberrant cytoplasmic and extracellular HMGB1 expression was evident in joint tissues from arthritic mice. HMGB1 and anti-HMGB1 antibodies could be detected in serum long before established disease, suggesting a role for HMGB1 in the initiation phase of the disease. Finally, I have used a novel approach to inhibit extracellular HMGB1 release by inducing its nuclear retention. Chromatin sequestration of HMGB1 by oxaliplatin ameliorated collagen-induced arthritis in mice. Nuclear retention of HMGB1 was also demonstrated to be a potential mechanism for the therapeutic effects of gold salts which are commonly used in rheumatic diseases. In conclusion, these studies demonstrate that HMGB1 when complexed with distinct molecules potentiates inflammation, provide further evidence of a role of extracellular HMGB1 in inflammatory arthritis, and that targeting HMGB1 is therapeutically beneficial.
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