Hoe actief zijn aandeelhouders in Nederland?

In deze bijdrage analyseren wij het gedrag van aandeelhouders bij Nederlandse beursgenoteerde ondernemingen. Het onderzoek bevat unieke data over opkomst en stemgedrag van aandeelhouders voor 54 beursgenoteerde ondernemingen over de periode 1998-2002. De data zijn gebaseerd op een analyse van de notulen van 245 aandeelhoudersvergaderingen en de statuten van de onderzochte ondernemingen. In totaal werden 1.583 onderwerpen in stemming gebracht. De empirische analyse richt zich onder meer op de verklaring van stemgedrag, aard van het voorstel en type aandeelhouder

Some aspects of rat platelet and serum phospholipase A2 activities

Rat platelet lysate contained appreciable phospholipase A2 activity. In agreement with literature data this enzymatic activity eluted in the void volume of a Sephadex G-100 column. When the void volume peak was chromatographed over a Matrex gel blue A column, part of the phospholipase A2 activity ran through, whereas the remainder was bound to the gel. The latter activity could be eluted with buffers containing a high salt concentration. In contrast, phospholipase A2 activity solubilized from rat platelet lysates by treatment with high salt eluted from Sephadex G-100 columns with an apparent molecular weight of 10–15 kDa. This solubilized enzyme completely bound to Matrex gel blue A and, in the presence of Ca2+ also to an alkylphosphocholine-AH Sepharose affinity column. No indications were obtained for the presence of inactive phospholipase A2 and activator proteins in rat platelet lysates as described by Etienne, J., Grüber, A. and Polonovski, J. ((1980) Biochim. Biophys. Acta 619, 693–698; (1982) Biochemie 64, 377–380). Phospholipase A2 activity, both the associated form in platelet lysate and the monomeric form as eluted from Sephadex G-100 was slightly inhibited by trifluoperazine but calmodulin exerted no stimulation. Likewise, phospholipase A2 activity from rat serum eluted in the void volume of a Sephadex G-100 column. Rather than indicating the presence of high molecular weight forms of the enzyme, this is apparently caused by association with lipids or other proteins, in that chromatography in the presence of high salt revealed a molecular weight similar to that found for solubilized platelet phospholipase A2 activity

Clinical outcomes of home parenteral nutrition patients using taurolidine as catheter lock: A long-term cohort study

Item does not contain fulltextBACKGROUND & AIMS: Central venous access device (CVAD)-related complications, such as central-line associated bloodstream infections (CLABSIs), CVAD-related venous thromboses (CRVTs) and -occlusions frequently occur in home parenteral nutrition (HPN) patients. A preventive strategy to decrease the incidence of CLABSIs is the use of CVAD lock solutions, such as 2% taurolidine. The aim of this study was to evaluate long-term clinical outcomes of our HPN cohort while using taurolidine as lock solution. In addition, we explored risk factors associated with CVAD-related complications. METHODS: We conducted a retrospective analysis of complications (CLABSIs, CRVTs and CVAD occlusions) and adverse events in adult HPN patients while using taurolidine as lock solution. Patients with a benign underlying disease leading to intestinal failure were included between 2006 and 2017 at our tertiary referral centre for intestinal failure. Primary outcome was the effectiveness of taurolidine, as described by complication incidence rates. Secondary objectives were to assess adverse events of taurolidine, complication rates of patients who subsequently discontinued taurolidine and started using 0.9% saline alternatively, and risk factors associated with complications. RESULTS: In total, 270 HPN patients used taurolidine during 338521 catheter days. CLABSIs, CRVTs and CVAD occlusions occurred at a rate of 0.60 (CI95% 0.52-0.69), 0.28 (CI95% 0.23-0.34), and 0.12 (CI95% 0.08-0.16) events per 1000 catheter days, respectively. In 24 (9%) patients, mild to moderate adverse events resulted in discontinuation of 2% taurolidine. A subsequent switch to 0.9% saline resulted in an increased CLABSI rate (adjusted rate ratio 4.01 (95%CI 1.23-13.04), P = 0.02). Several risk factors were identified for CLABSIs (a lower age, nontunneled catheters, infusion frequency), CRVTs (site of vein insertion), and CVAD occlusions (type of CVAD). CONCLUSION: Complication rates remained low in the long-term, and use of taurolidine was generally safe. The identified risk factors may help to create new strategies to further prevent CVAD-related complications and improve HPN care in the future

Facial Characteristics and Olfactory Dysfunction: Two Endophenotypes Related to Nonsyndromic Cleft Lip and/or Palate

Roosenboom J., Saey I., Peeters H., Devriendt K., Claes P., Hens G., ''Facial characteristics and olfactory dysfunction: two endophenotypes related to nonsyndromic cleft lip and/or palate'', Biomed research international, vol. 2015, Article ID 863429, 8 pp., 2015.Evidence exists for the presence of a specific facial phenotype in nonaffected first-degree relatives of persons with CL/P. An increased risk for olfactory dysfunction has also been reported in CL/P-relatives. These phenotypic features can probably be explained via the presence of CL/P-related susceptibility genes. We aimed at confirming the occurrence of these endophenotypic traits in first-degree CL/P-relatives, and we investigated the link between the facial phenotype and the smell capacity in this group. We studied the facial morphology of 88 nonaffected first-degree relatives of patients with CL/P and 33 control subjects without family history of facial clefting by 3D surface imaging and a spatially dense analysis of the images. Smell testing was performed in 30 relatives and compared with 23 control subjects. Nonaffected relatives showed midface retrusion, hypertelorism, and olfactory dysfunction, compared to controls. In addition, we show for the first time that olfactory dysfunction in relatives is correlated to a smaller upper nasal region. This might be explained by a smaller central olfactory system. The different facial morphology in the relatives with olfactory impairment as compared to the total group may be an illustration of the contribution of different genetic backgrounds to the occurrence of CL/P via different biological pathways.status: publishe

Alkyl dihydroxyacetone phosphate synthase in human fibroblasts and its deficiency in Zellweger syndrome

The cerebro-hepato-renal (Zellweger) syndrome is an autosomal recessive disorder biochemically characterized by the absence of morphologically distinguishable peroxisomes. Key enzymes involved in the biosynthesis of ether phospholipids, i.e., dihydroxyacetone phosphate acyltransferase and alkyl dihydroxyacetone phosphate synthase, are located in mammalian (micro)peroxisomes. We have previously shown a strikingly reduced activity of dihydroxyacetone phosphate acyltransferase in liver, brain, and cultured skin fibroblasts from Zellweger patients (Schutgens et al. 1984. Biochim. Biophys. Res. Commun. 120: 179-184). We have now extended these investigations by studying alkyl dihydroxyacetone phosphate synthase in cultured human skin fibroblasts. Enzymatic activity was determined by measuring the formation of radioactive alkyl dihydroxyacetone phosphate from palmitoyl dihydroxyacetone phosphate and [1-14C]hexadecanol as substrates. The enzyme was optimally active at pH 8.5 and was stimulated (about 2-3-fold) by the presence of 0.05% (v/v) Triton X-100. The apparent KM values for the enzyme in control fibroblasts amounted to 35 microM for palmitoyl dihydroxyacetone phosphate and 90 microM for hexadecanol. The reaction became inhibited at higher concentrations of both Triton X-100 and palmitoyl dihydroxyacetone phosphate. Control skin fibroblasts showed alkyl dihydroxyacetone phosphate synthase activity of 69 +/- 28 pmol X min-1 X mg-1 (n = 7), while fibroblasts from patients had an activity of only 6.3 +/- 1.7 pmol X min-1 X mg-1 (n = 7). Alkyl dihydroxyacetone phosphate synthase was also found to be deficient in tissue homogenates of Zellweger patients. The specific activity of this enzyme in liver, kidney, and brain homogenates from Zellweger patients was less than 15% of that in the corresponding tissues from control