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- Kihlbom, Ulrik, 1961-, et al.
(author)
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Healthcare Decisions
- 2019
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In: What About the Family?. - Oxford : Oxford University Press. - 9780190624880
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Book chapter (other academic/artistic)abstract
- The aim of this collection is to develop new theoretical and practical approaches to address the responsibilities created by new forms of healthcare practice. In particular, the authors examine the significance of people’s key relationships, such as family and community, and how they deliberate and make decisions about their responsibilities. Each chapter of the collection works through a set of questions that provide a framework for understanding the problematic behind the book and the broader debates it is part of: why families matter, what counts as family, how families track responsibilities, how treatment decisions ought to work in families, and what justice requires of families.
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- Knutsson, Simon, et al.
(author)
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A Virtue of Precaution Regarding the Moral Status of Animals with Uncertain Sentience
- 2017
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In: Journal of Agricultural and Environmental Ethics. - : Springer Science and Business Media LLC. - 1187-7863 .- 1573-322X. ; 30:2, s. 213-224
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Journal article (peer-reviewed)abstract
- We address the moral importance of fish, invertebrates such as crustaceans, snails and insects, and other animals about which there is qualified scientific uncertainty about their sentience. We argue that, on a sentientist basis, one can at least say that how such animals fare make ethically significant claims on our character. It is a requirement of a morally decent (or virtuous) person that she at least pays attention to and is cautious regarding the possibly morally relevant aspects of such animals. This involves having a moral stance, in the sense of patterns of perception, such that one notices such animals as being morally relevant in various situations. For the person who does not already consider these animals in this way, this could be a big change in moral psychology, and can be assumed to have behavioural consequences, albeit indeterminate. Character has been largely neglected in the literature, which focuses on act-centred approaches (i.e. that the evidence on sentience supports, or does not support, taking some specific action). We see our character-centred approach as complementary to, not superior to, act-centred approaches. Our approach has the advantage of allowing us to make ethically interesting and practically relevant claims about a wider range of cases, but it has the drawback of providing less specific action guidance.
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- Kozarcanin, Huda, et al.
(author)
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The lectin complement pathway serine proteases (MASPs) represent a possible crossroad between the coagulation and complement systems in thromboinflammation
- 2016
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In: Journal of Thrombosis and Haemostasis. - : Elsevier BV. - 1538-7933 .- 1538-7836. ; 14:3, s. 531-545
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Journal article (peer-reviewed)abstract
- The lectin pathway's MASP-1/2 activates coagulation factors but the trigger of the activation is unknown. MASP-1/2 activation was assessed by quantifying complexes between MASPs and antithrombin/C1-inhibitor. Activated platelets and fibrin were demonstrated to activate MASP-1 and MASP-2 both invitro and invivo. These findings may represent a crossroad between the complement and the coagulation systems. Summary Background The activated forms of the complement lectin pathway (LP) proteases MASP-1 and MASP-2 are able to cleave the coagulation factors prothrombin, fibrinogen, factor XIII and thrombin-activatable fibrinolysis inhibitor invitro. In vivo studies also show that MASP-1 is involved in thrombogenesis. Objectives To clarify the not yet identified mechanisms involved in triggering activation of the LP during thrombotic reactions. Methods Novel sandwich-ELISAs for detection of complexes between MASP-1 or MASP-2 and the serpins C1 inhibitor (C1-INH) or antithrombin (AT), were used to specifically detect and quantify the activated forms of MASP-1 and MASP-2. Results Activated platelets were shown by flow cytometry to bind Ficolin-1, -2 and -3 but not MBL, which was associated with activation of MASP-1 and MASP-2. We also demonstrated that fibrin and the plasmin-generated fibrin fragment DD in plasma, bind and activate MASP-1 and MASP-2. As demonstrated by the ELISA and SDS-PAGE/Western blotting, the fibrin-associated activation was reflected in a specific inactivation by AT during clotting without the assistance of heparin. In all other cases the MASPs were, as previously reported, inactivated by C1-INH. In systemic lupus erythematosus patients with thrombotic disease and in polytrauma patients, the levels of activated MASP-1 and MASP-2 in complex with both AT and C1-INH were associated with markers of thrombotic disease and contact/coagulation system activation. Conclusions MASP-1 and MASP-2 are activated during blood clotting. This activation is triggered by activated platelets and by the generation of fibrin during thrombotic reactions invitro and invivo, and may represent a novel activation/amplification mechanism in thromboinflammation.
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