A Large Cross-Sectional Study of Health Attitudes, Knowledge, Behaviour and Risks in the Post-War Croatian Population (The First Croatian Health Project*)

As the liberation of occupied Croatian territories ended the war in the country in 1995, the Ministry of Health and Croatian Health Insurance Institute have agreed to create the new framework for developing a long-term strategy of public health planning, prevention and intervention. They provided financial resources to develop the First Cro-atian Health Project, the rest of the support coming from the World Bank loan and the National Institute of Public Health. A large cross-sectional study was designed aiming to assess health attitudes, knowledge, behaviour and risks in the post-war Croatian population. The large field study was carried out by the Institute for Anthropological Research with technical support from the National Institute of Public Health. The field study was completed between 1995–1997. It included about 10,000 adult volunteers from all 21 Croatian counties. The geographic distribution of the sample covered both coastal and continental areas of Croatia and included rural and urban environments. The specific measurements included antropometry (body mass index and blood pressure). From each examinee a blood sample was collected from which the levels of total plasma cholesterol (TC), triglycerides (TG), HDL-cholesterol (High Density Lipoprotein), LDL-cholesterol (Low Density Lipoprotein), lipoprotein Lp(a), and haemostatic risk factor fibrinogen (F) were determined. The detailed data were collected on the general knowledge and attitudes on health issues, followed by specific investigation of smoking history, alcohol consumption, nutrition habits, physical activity, family history of chronic non-communicable diseases and occupational exposures. From the initial database a targeted sample of 5,840 persons of both sexes, aged 18–65, was created corresponding by age, sex and geographic distribution to the general Croatian population. This paper summarises and discusses the main findings of the project within this representative sample of Croatian population

Elastin is Localised to the Interfascicular Matrix of Energy Storing Tendons and Becomes Increasingly Disorganised With Ageing

Tendon is composed of fascicles bound together by the interfascicular matrix (IFM). Energy storing tendons are more elastic and extensible than positional tendons; behaviour provided by specialisation of the IFM to enable repeated interfascicular sliding and recoil. With ageing, the IFM becomes stiffer and less fatigue resistant, potentially explaining why older tendons become more injury-prone. Recent data indicates enrichment of elastin within the IFM, but this has yet to be quantified. We hypothesised that elastin is more prevalent in energy storing than positional tendons, and is mainly localised to the IFM. Further, we hypothesised that elastin becomes disorganised and fragmented, and decreases in amount with ageing, especially in energy storing tendons. Biochemical analyses and immunohistochemical techniques were used to determine elastin content and organisation, in young and old equine energy storing and positional tendons. Supporting the hypothesis, elastin localises to the IFM of energy storing tendons, reducing in quantity and becoming more disorganised with ageing. These changes may contribute to the increased injury risk in aged energy storing tendons. Full understanding of the processes leading to loss of elastin and its disorganisation with ageing may aid in the development of treatments to prevent age related tendinopathy

Improving Internal Peptide Dynamics in the Coarse-Grained MARTINI Model: Toward Large-Scale Simulations of Amyloid- and Elastin-like Peptides

We present an extension of the coarse-grained MARTINI model for proteins and apply this extension to amyloid- and elastin-like peptides. Atomistic simulations of tetrapeptides, octapeptides, and longer peptides in solution are used as a reference to parametrize a set of pseudodihedral potentials that describe the internal flexibility of MARTINI peptides. We assess the performance of the resulting model in reproducing various structural properties computed from atomistic trajectories of peptides in water. The addition of new dihedral angle potentials improves agreement with the contact maps computed from atomistic simulations significantly. We also address the question of which parameters derived from atomistic trajectories are transferable between different lengths of peptides. The modified coarse-grained model shows reasonable transferability of parameters for the amyloid- and elastin-like peptides. In addition, the improved coarse-grained model is also applied to investigate the self-assembly of β-sheet forming peptides on the microsecond time scale. The octapeptides SNNFGAIL and (GV)4 are used to examine peptide aggregation in different environments, in water, and at the water–octane interface. At the interface, peptide adsorption occurs rapidly, and peptides spontaneously aggregate in favor of stretched conformers resembling β-strands

Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly

The tropoelastin monomer undergoes stages of association by coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers. Tropoelastin consists of an elastic N-terminal coil region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region. The bridge region is conveniently positioned to modulate elastic fiber assembly through association by coacervation and its proximity to dominant cross-linking domains. Tropoelastin constructs that either modify or remove the entire bridge and downstream regions were assessed for elastogenesis. These constructs focused on a single alanine substitution (R515A) and a truncation (M155n) at the highly conserved arginine 515 site that borders the bridge. Each form displayed less efficient coacervation, impaired hydrogel formation, and decreased dermal fibroblast attachment compared to wild-type tropoelastin. The R515A mutant protein additionally showed reduced elastic fiber formation upon addition to human retinal pigmented epithelium cells and dermal fibroblasts. The small-angle X-ray scattering nanostructure of the R515A mutant protein revealed greater conformational flexibility around the bridge and C-terminal regions. This increased flexibility of the R515A mutant suggests that the tropoelastin R515 residue stabilizes the structure of the bridge region, which is critical for elastic fiber assembly