ABSTRACT
AIMS: To perform the first psychometric analysis of the Norwegian version of the eHLQ using confirmative factor analysis (CFA) procedures in a population of patients admitted to hospital using a cross-sectional design. The eHLQ consists of 35 items capturing the 7-dimensional eHealth Literacy Framework (eHLF) which describes users' attributes, user's interaction with technologies and user's experience with digital health systems. METHODS: The 7 independent scales of the eHLQ was translated from Danish and culturally adapted into the Norwegian language following a standardised protocol. Assessment of construct validity of the eHLQ was undertaken using data from a cross-sectional survey of 260 patients hospitalized at a Norwegian University Hospital in the Oslo area during a two-week period in June 2021. The analysis included using correlation analysis (Pearsons R), internal consistency (Cronbach's alpha) and confirmatory factor analysis (CFA). RESULTS: All factor loadings were high to acceptable (i.e. > 0.6), except for five items which had somewhat lower loadings. Regarding internal consistency, alpha ranged from 0.73 to 0.90. For optimal CFA fit for the different scale models, correlated residuals were required for five of the seven scales. Overall our analysis shows an intermediate fit of the orginal construct. Scale intercorrelations were all below 0.8, indicating an overall acceptable discriminant validity between the 7 dimensions. CONCLUSIONS: The results from the CFA analysis indicate that for almost all 7 eHLQ scales, an acceptable model fit was achieved. The 260 hospitalized patients included in this study represented a variety of diagnoses, recruited from a geographically limited area. Further studies on psychometric properties of the Norwegian version of eHLQ in larger samples, diverse settings and by using more comprehensive approaches are warranted.
Subject(s)
Literacy , Telemedicine , Humans , Cross-Sectional Studies , Reproducibility of Results , Surveys and Questionnaires , Language , Telemedicine/methods , Norway , Factor Analysis, Statistical , Psychometrics/methodsABSTRACT
BACKGROUND: There are major gaps in the understanding of sexual and reproductive health in female renal transplant recipients. METHODS: In this Norwegian multicenter retrospective observational study, 118 female renal transplant recipients aged 22 to 49 years responded to a questionnaire on fertility, contraceptive use, and pregnancy. RESULTS: More than one-third (37%) of patients reported that they did not receive advice on contraceptive methods from health care personnel in the early post-transplant phase. These women used effective contraceptive methods less often. Nearly half of the patients (45%) reported that they had not received any advice on timing of conception after transplant. From 95 pregnancies after renal transplant, 52 (55%) resulted in live births. CONCLUSION: Counseling on contraceptive methods should be part of standard care in conjunction with transplantation. More than one-third of young female renal transplant recipients of reproductive age could not recall having received advice from health care personnel about contraceptive use, and nearly half of the patients did not receive preconceptional advice after transplant. Although the current study does not discriminate between lack of advice and recall bias, the findings signal the need for improved counseling on female sexual and reproductive health after renal transplant.
Subject(s)
Contraception , Counseling , Fertility , Kidney Transplantation , Transplant Recipients/education , Adult , Female , Humans , Middle Aged , Norway , Pregnancy , Retrospective Studies , Sexual Behavior , Young AdultABSTRACT
The potential benefit of continuous local administration of antiangiogenic proteins to CNS tumors in vivo has recently been demonstrated using endostatin-producing recombinant cells encapsulated in alginate beads. Due to the treatment potential of transplanted alginate-encapsulated cells producing therapeutic proteins, we describe a successful method of cryopreservation (CP) of such beads, in which cellular viability, alginate structure, and protein secretion were maintained. Alginate beads containing human embryonic kidney cells (HEK 293 cells) stably transfected with the gene encoding for endostatin were cryopreserved in dimethyl sulfoxide (DMSO) using a slow freezing procedure. Briefly, the DMSO concentration was gradually increased prior to the freezing procedure. The cryotubes were further supercooled to -7.5 degrees C and nucleated. Thereafter, the samples were cooled at a rate of 0.25 degrees C/min and stored in liquid nitrogen. The viability of the encapsulated cells was assessed using confocal microscopy quantification (CLSM) technique and a MTS assay. The cell cycle distribution inside the beads was assessed by DNA flow cytometry and endostatin production was determined by an endostatin-specific ELISA assay, both prior to and after CP. CLSM measurements showed sustained esterase activity in the beads after thawing, with only a slight transient decrease 24 h after CP. The MTS assay verified these findings by displaying similar variations of intracellular dehydrogenase activity. Flow cytometric analyses revealed no cryorelated disturbances in cellular ploidy. Furthermore, ELISA measurements showed a well-preserved endostatin production after CP. In conclusion, this work describes the successful CP of alginate-encapsulated recombinant cells secreting a therapeutic protein. Together with previous published reports, these results further substantiate the feasibility and potential of cell encapsulation therapy in the treatment of malignant tumors.
Subject(s)
Alginates , Cell Transplantation/methods , Glucuronic Acid , Hexuronic Acids , Angiogenesis Inhibitors , Capsules , Cell Line , Cryopreservation/methods , Dimethyl Sulfoxide , Endostatins/genetics , Humans , Image Processing, Computer-Assisted , Kidney/cytology , Microscopy, Confocal , TransfectionABSTRACT
This study reports on morphological and contractile properties of the bovine central adrenomedullary vein (bCAMV). Up to several layers of circularly orientated smooth muscle cells (SMC) were observed, however, without forming a continuous, closed sheath. Discrete bundles of eccentrically arranged, longitudinal SMC were also conspicuous. Chromaffin cells were in most cases located outside the SMC layers, while sometimes being in close apposition to the endothelium in areas without SMC. Circularly mounted preparations of the endothelium-denuded vessel responded selectively to high K+, endothelins (ETs) and neuropeptide Y (NPY). The threshold for ET-1 was 0.13 nM and the half maximally effective concentration (EC50) was 3 +/- 1 nM (n = 9). The order of potencies was ET-1 > or = ET-2 >> ET-3, suggesting a vascular receptor (ETA). Concentrations at and above EC50 frequently developed long-lasting oscillations during the spontaneous relaxation of the ET-1 evoked tension. This response was partly (21%) independent of extracellular Ca2+. A marked tachyphylaxis developed to ET-1 (3-30 nM), resulting, on the other hand, in facilitation of the subsequent constrictor responses to high K+ and NPY. Propranolol and phentolamine alone, or in combination, were without effects on the basal tension and on the above-mentioned responses to high K+, ET-1 or NPY, making a contribution from adrenoceptor activation unlikely. No response was obtained with exogenous catecholamines, acetylcholine or serotonin, nor with a series of peptides known to occur in the adrenal medulla. This study shows that bCAMV is not a passive capacitance vessel but appears unique among mammalian veins in being selectively regulated by ETs.
Subject(s)
Adrenal Medulla/blood supply , Endothelins/pharmacology , Muscle, Smooth, Vascular/physiology , Adrenal Medulla/cytology , Animals , Calcium/pharmacology , Calcium/physiology , Catecholamines/metabolism , Cattle , Electrophoresis, Polyacrylamide Gel , Immunochemistry , In Vitro Techniques , Isometric Contraction/drug effects , Isometric Contraction/physiology , Muscle Contraction/drug effects , Muscle Contraction/physiology , Muscle Proteins/metabolism , Muscle, Smooth, Vascular/drug effects , Neuropeptide Y/pharmacology , Potassium/pharmacology , Regional Blood Flow/drug effects , Regional Blood Flow/physiology , Veins/drug effects , Veins/physiologyABSTRACT
Synchronous contractions in the intramedullary venous vasculature have been postulated to assist in the discharge of hormones from the stimulated adrenal medulla in a manner analogous to the squeezing of a wet sponge. This study reports on two experimental approaches to support the hypothesis that contractions in the venous vasculature may contribute to the hormonal efflux. Firstly, the bovine adrenal medulla was perfused retrogradely via the bovine central adrenomedullary vein end changes in the vascular volume were assessed as changes in wet weight of the perfused tissue. Stimulation with acetylcholine and carbachol resulted in repetitive, transient weight losses, suggesting cholinergically mediated reductions in the vascular volume. Secondly, the contractile properties of the longitudinal layers of smooth muscle cells in the intramedullary venous system were characterized, using the bovine central adrenomedullary vein as a model. The results showed that the longitudinal layers of this vein were, similarly to the circular layers, selectively contracted by endothelin-1 via an ETA-like receptor, by neuropeptide Y and by membrane depolarization (high K+). However, the vein was insensitive to electrical stimulation acetylcholine and carbacho, as well as to catecholamines. These results suggest neuropeptide Y, released from the cholinergically stimulated chromaffin cells, as the most likely mediator of stimulus-evoked synchronous contractions of the venous vasculature in the bovine adrenal medulla. Together, these experiments provide support for the 'wet sponge' hypothesis for hormonal discharge from the adrenal gland.
Subject(s)
Adrenal Medulla/blood supply , Adrenal Medulla/physiology , Adrenal Medulla/drug effects , Animals , Carbachol/pharmacology , Cattle , Cholinergic Agonists/pharmacology , Electric Stimulation , Endothelins/pharmacology , In Vitro Techniques , Isometric Contraction/drug effects , Isometric Contraction/physiology , Muscle Contraction/drug effects , Muscle Contraction/physiology , Muscle, Smooth, Vascular/cytology , Muscle, Smooth, Vascular/drug effects , Muscle, Smooth, Vascular/physiology , Neuropeptide Y/pharmacology , Vasoconstriction/drug effects , Vasoconstriction/physiologyABSTRACT
The functional properties of the isolated porcine and bovine central adrenomedullary veins were compared, with emphasis on the active tension responses to high K+, endothelin-1 (ET-1) and neuropeptide Y (NPY). In the porcine vein, the contraction evoked by ET-1 was 4--5-fold higher than with high K+, as in the bovine vein. The potencies for ET-1 were similar in ring and strip preparations of the porcine vein, with EC50 values 5--7-fold higher than in the bovine vein. In preparations previously exposed to ET-1 the contractions evoked by high K+ and NPY were potentiated and facilitated, respectively,. However, only in the porcine vein was the ET-1 contraction sustained. This contraction was effectively relaxed by milrinone, indicating a role for cGMP inhibited cyclic nucleotide phosphodiesterase in the sustained contraction. Caffeine and forskolin were also effective relaxants of contractions evoked by ET-1 in both veins, suggesting relaxation by elevated levels of cAMP. The K(+)-contracted porcine, but not bovine, vein was relaxed by acetylcholine (ACh) and vasointestinal polypeptide in a concentration-dependent manner, indicating species differences with respect to signal transduction leading to increases in cyclic nucleotides. In conclusion, these results demonstrate that ET-1 is the main constrictor of the porcine central adrenomedullary vein, with significant species differences in mode of contraction and relaxation. These findings suggest roles for the endogeneously released ET-1 and NPY in regulation of venous contractility within the adrenal gland of mammals.
Subject(s)
Adrenal Medulla/blood supply , Cattle/physiology , Endothelin-1/pharmacology , Swine/physiology , Vasoconstriction/drug effects , Acetylcholine/pharmacology , Adenylyl Cyclases/metabolism , Animals , Caffeine/pharmacology , Colforsin/pharmacology , Cyclic AMP/physiology , Milrinone/pharmacology , Muscle, Smooth, Vascular/drug effects , Neuropeptide Y/pharmacology , Potassium/pharmacology , Propranolol/pharmacology , Receptor, Endothelin A , Receptors, Endothelin/drug effects , Receptors, Endothelin/physiology , Second Messenger Systems/physiology , Species Specificity , Vasoactive Intestinal Peptide/pharmacology , Vasoconstrictor Agents/pharmacology , Vasodilation/drug effects , Vasodilator Agents/pharmacology , Veins/drug effectsABSTRACT
Chromogranins constitute a family of acidic soluble proteins widely distributed in endocrine cells and neurons. Chromogranin A, the major soluble component in bovine adrenal medullary secretory granules in chromaffin cells, has been shown to be actively processed to peptide fragments [Metz-Boutigue, M. H., Garcia-Sablone, P., Hogue-Angeletti, R. & Aunis, D. (1993) Eur. J. Biochem. 217, 247-257]. In the present paper, the structural features of the proteolytic degradation mechanism of chromogranin B/secretogranin I have been characterized with regard to the possible function of this protein as a precursor of biologically active peptides. Chromogranin-B-derived fragments present in bovine chromaffin granules were identified by microsequencing after separation by two-dimensional gel electrophoresis or high-performance liquid chromatography. A similar approach was performed to characterize chromogranin-B-derived fragments released into the extracellular space from depolarized bovine cultured chromaffin cells. In chromogranin B, 18 cleavage sites were identified along the protein chain and chromogranin B/secretogranin I fragments were generated by proteolytic attack at both the N-terminus and C-terminus. A major fragment corresponding to residues 614-626 of the C-terminal sequence, was identified in the extracellular space; this peptide was found to share sequence and structural similarities with the lytic domain of cecropins and, as expected from this similarity, to display potent antibacterial properties. Endogenous and synthetic peptides were active on Micrococus luteus, killing bacteria in the micromolar concentration range. The synthetic peptide slows the growth of Bacillus megaterium and was inactive towards Escherichia coli. In addition, the synthetic peptide was unable to induce hemolytic activity. This antibacterial function might be of biological significance in the neuroendocrine system of living organisms. We propose to name this peptide secretolytin.