Self-management of oral anticoagulant therapy training program currently used.

<p>Abbreviations: INR: International Normalized ratio.</p><p>Self-management of oral anticoagulant therapy training program currently used.</p

Adverse events in patients on self-managed oral anticoagulant therapy (N = 2068).

<p>*) Includes traumatic and non-traumatic intracranial bleeding.</p><p>Abbreviations:</p><p>N: Number.</p><p>Pt-ys: Patient years.</p><p>CI: Confidence interval.</p><p>Adverse events in patients on self-managed oral anticoagulant therapy (N = 2068).</p

Baseline characteristics of patients performing self-management of oral anticoagulant therapy (N = 2068).

<p>*)Missing information on 163 patients, excluded in calculation.</p><p>^†)Calculated according to the Charlson Comorbidity Index, group: low: 0, med: 1–2, high:>2.</p><p>Abbreviations:</p><p>N: Number.</p><p>SD: Standard deviation.</p><p>VKA: Vitamin K antagonist.</p><p>ARB: Angiotensin II receptor blocker.</p><p>ACE: Angiotensin-converting-enzyme.</p><p>NSAID: Non-steroidal anti-inflammatory drug.</p><p>Baseline characteristics of patients performing self-management of oral anticoagulant therapy (N = 2068).</p

Hazard rate ratio for male sex based on Cox proportional-hazards model for each outcome.

<p>Adjusted hazard ratio optained by adjusting for age, primary indication, type of Vitamin K antagonist treatment, baseline use of ARB or ACE inhibitors, beta-blocker, and statin. The Intracranial bleeding (n = 6) and the systemic embolism (n = 5) has not been included in the analysis due to the low number of cases. Abbreviations: CI: Confidence interval. IC: Intracranial. GI: Gastrointestinal. Sys: Systemic.</p

Therapeutic control of the oral anticoagulant therapy in self-managed patients (N = 2068).

<p>^†98 patients changed target twice, 13 patients changed target three times, 2 changed target four times.</p><p>*70 targets within 1.5 – 2.4 was standardised to 2 – 3.</p><p>**58 targets within 2.5 and 4.2 was standardised to 2.5 – 3.5.</p><p>***Adjusted for evaluating the effect of sex.</p><p>The percentage of time within therapeutic INR target range was calculated according to Rosendaal's method for each patient, and the crude and adjusted mean percentage is presented.</p><p>Abbreviations</p><p>N: Number.</p><p>INR: International Normalized Ratio.</p><p>SD: Standard deviation.</p><p>CI: Confidence Interval.</p><p>Therapeutic control of the oral anticoagulant therapy in self-managed patients (N = 2068).</p

Adsorption of α‑Synuclein to Supported Lipid Bilayers: Positioning and Role of Electrostatics

An amyloid form of the protein α-synuclein is the major component of the intraneuronal inclusions called Lewy bodies, which are the neuropathological hallmark of Parkinson’s disease (PD). α-Synuclein is known to associate with anionic lipid membranes, and interactions between aggregating α-synuclein and cellular membranes are thought to be important for PD pathology. We have studied the molecular determinants for adsorption of monomeric α-synuclein to planar model lipid membranes composed of zwitterionic phosphatidylcholine alone or in a mixture with anionic phosphatidylserine (relevant for plasma membranes) or anionic cardiolipin (relevant for mitochondrial membranes). We studied the adsorption of the protein to supported bilayers, the position of the protein within and outside the bilayer, and structural changes in the model membranes using two complementary techniquesquartz crystal microbalance with dissipation monitoring, and neutron reflectometry. We found that the interaction and adsorbed conformation depend on membrane charge, protein charge, and electrostatic screening. The results imply that α-synuclein adsorbs in the headgroup region of anionic lipid bilayers with extensions into the bulk but does not penetrate deeply into or across the hydrophobic acyl chain region. The adsorption to anionic bilayers leads to a small perturbation of the acyl chain packing that is independent of anionic headgroup identity. We also explored the effect of changing the area per headgroup in the lipid bilayer by comparing model systems with different degrees of acyl chain saturation. An increase in area per lipid headgroup leads to an increase in the level of α-synuclein adsorption with a reduced water content in the acyl chain layer. In conclusion, the association of α-synuclein to membranes and its adsorbed conformation are of electrostatic origin, combined with van der Waals interactions, but with a very weak correlation to the molecular structure of the anionic lipid headgroup. The perturbation of the acyl chain packing upon monomeric protein adsorption favors association with unsaturated phospholipids preferentially found in the neuronal membrane