Who lives in care homes in Greenland? A nationwide survey of demographics, functional level, medication use and comorbidities.

BACKGROUND: Greenland is facing an ageing population, and little is known about the characteristics of the elderly population in Greenland. This study offers both a comparison and a description of the demographics, causes of admission, comorbidities and medication of the residents in care homes in the capital, major and minor towns in four of the five administrative regions of Greenland. METHODS: The study was conducted from 2010 to 2016 as a descriptive questionnaire-based cross-sectional study. Data from eligible residents from eight care homes were collected from the regular care staff. Data were categorised into three groups based on town size for analysis. RESULTS: 244 (100 %) of eligible residents participated in the study. Nearly 100 % were of Greenlandic ethnicity based on parents' place of birth, and 62 % were women. The median age at admission/study was 69/71 years for men and 77/79 years for women (both p = 0.001). The median Body Mass Index was 25.6 kg/m2, more than half of the population were previous- or never-smokers and less than ten per cent consumed more than ten drinks of alcohol per week. The most common causes of admission were dementia (25.4 %), stroke (19.3 %) and social causes (11.1 %), while stroke (30.7 %), dementia (29.5 %) and musculoskeletal diseases (25.8 %) were the most common diagnoses at the time of the study. The Barthel Index was used to estimate the residents' level of independence, and residents in smaller towns were found to have a higher level of independence than residents in the capital. The median number of prescribed medications was five, and more residents in the capital were prescribed more than ten medications than elsewhere in Greenland. CONCLUSIONS: This study is the first to describe care home residents in Greenland. We found a population younger than residents in comparable Danish care homes and that women were older than men at admission. In addition, care home residents in the capital had a lower level of independence and a higher number of prescribed medications, which could relate to differences in morbidity, access to health care services and differences in social circumstances influencing the threshold for care home admission.

Effects of diamide and dibucaine on platelet glycoprotein Ib, actin-binding protein and cytoskeleton.

During extraction of platelets by 1% Triton X-100, the actin-binding protein (platelet filamin) and a 230 kDa protein are degraded by a calcium-activated thiol protease. Occurrence of degradation products of Mr 190 000 (HF-1) and 90 000 (HF-2) is a sensitive indicator of this proteolysis, and can be used to decide whether reduced amounts of the actin-binding protein in extracts are due to proteolysis or to incorporation in the Triton-insoluble (cytoskeletal) fraction. Diamide, which is a sulfhydryl-oxidizing protein cross-linker, inhibits the calcium-activated protease, polymerizes the actin-binding protein and the 230 kDa protein, increases the incorporation of glycoprotein Ib into the cytoskeletal fraction, and inhibits platelet agglutination induced by bovine von Willebrand factor. Inhibition of platelet agglutination by pretreatment with diamide is partly reversed by dibucaine which activates the calcium-activated protease. These observations are in accordance with a working hypothesis that interactions of glycoprotein Ib with cytoskeleton affect, and possibly regulate, its receptor function in the intact platelet.

Glycoprotein Ib in the Triton-insoluble (cytoskeletal) fraction of blood platelets.

Glycoprotein Ib could be demonstrated in the Triton-insoluble (cytoskeletal) fraction of platelets prepared with EGTA by SDS-polyacrylamide gel electrophoresis and staining with the periodic acid Schiff's reagent. Crossed immunoelectrophoresis showed that glycoprotein Ib could be extracted from such Triton-insoluble residues when the extraction solution contained 1% Triton X-100 plus 5 mM CaCl2, but not if it also contained leupeptin. This indicates that glycoprotein Ib was associated to structures in the cytoskeletal fraction in such a way that it could be extracted only after activation of a calcium-dependent protease, and degradation of the actin-binding protein was demonstrated. After crossed immunoelectrophoresis of platelet extracts prepared in the presence of leupeptin or EDTA, a glycoprotein Ib-related, rocket-shaped immunoprecipitate was seen originating from the application well. This was interpreted as being related to glycoprotein Ib associated to actin polymers which did not sediment at low-speed centrifugation. Incubation of platelets with 32P as sodium phosphate led to incorporation of phosphatase-sensitive 32P in all of the glycoprotein Ib-related immunoprecipitates except for that of glycocalicin. This supports the idea that glycoprotein Ib traverses the plasma membrane and can be phosphorylated at the inner surface whereas glycocalicin represents the terminal part of the glycoprotein Ib alpha-chain exposed at the outer surface.

Demonstration of a new glycoprotein Ib-related component in platelet extracts prepared in the presence of leupeptin.

The water-soluble protein glycocalicin is generated during platelet lysis by a proteolytic attack on the integral membrane glycoprotein GP Ib. However, only small amounts of glycocalicin are formed when platelets are solubilized by 1% Triton X-100. Crossed immunoelectrophoresis of such extracts using an antiserum to glycocalicin, shows a continuous immunoprecipitate consisting of two peaks, one representing glycocalicin and the other GP Ib. When leupeptin was present during solubilization, subsequent immunoelectrophoresis revealed yet another GP Ib-related component represented by a third, slow-migrating peak of the immunoprecipitate. During incubation of platelets with dibucaine followed by solubilization in the presence of leupeptin, a gradual transformation of this new form of GP Ib into the previously defined one took place prior to the formation of glycocalicin. An increase followed by a decrease in the agglutination response of the platelets to bovine von Willebrand factor occurred concomitant with these transformations. SDS-polyacrylamide gel electrophoresis of Triton X-100 extracts of platelets did not reveal any difference in the size of GP Ib whether or not leupeptin had been present during the solubilization.