Bielefeld University

About: Bielefeld University is a education organization based out in Bielefeld, Nordrhein-Westfalen, Germany. It is known for research contribution in the topics: Population & Quantum chromodynamics. The organization has 10123 authors who have published 26576 publications receiving 728250 citations. The organization is also known as: University of Bielefeld & UNIVERSITAET BIELEFELD.

Health literacy among different age groups in Germany: results of a cross-sectional survey

Abstract: Health literacy is of increasing importance in public health research. It is a necessary pre-condition for the involvement in decisions about health and health care and related to health outcomes. Knowledge about limited health literacy in different age groups is crucial to better target public health interventions for subgroups of the population. However, little is known about health literacy in Germany. The study therefore assesses the prevalence of limited health literacy and associated factors among different age groups. The Health Literacy Survey Germany is a cross-sectional study with 2,000 participants aged 15 years or older in private households. Perceived health literacy was assessed via computer-assisted personal interviews using the HLS-EU-Q-47 questionnaire. Descriptive analyses, chi-square tests and odds ratios were performed stratified for different age groups. The population affected by limited perceived health literacy increases by age. Of the respondents aged 15–29 years, 47.3 % had limited perceived health literacy and 47.2 % of those aged 30–45 years, whereas 55.2 % of the respondents aged 46–64 years and 66.4 % aged 65 years and older showed limited perceived health literacy. In all age groups, limited perceived health literacy was associated with limited functional health literacy, low social status, and a high frequency of doctor visits. The results suggest a need to further investigate perceived health literacy in all phases of the life-course. Particular attention should be devoted to persons with lower social status, limited functional health literacy and/or a high number of doctor visits in all age groups.

On Chemical Equilibrium in Nuclear Collisions

Abstract: The data on average hadron multiplicities in central A+A collisions measured at CERN SPS are analysed with the ideal hadron gas model. It is shown that the full chemical equilibrium version of the model fails to describe the experimental results. The agreement of the data with the off-equilibrium version allowing for partial strangeness saturation is significantly better. The chemical freeze-out temperature of about 180 MeV seems to be independent of the system size (from S+S to Pb+Pb) and in agreement with that extracted in e+ + e−, p + p and $$p + \bar p$$ collisions. The strangeness suppression is discussed at both hadron and valence quark level. It is found that the hadronic strangeness saturation factor γs increases from about 0.45 for p + p interactions to about 0.7 for central A+A collisions with no significant change from S+S to Pb+Pb collisions indicating that the strangeness enhancement in heavy ion collisions cannot be fully attributed to the increased system size. The quark strangeness suppression factor As is found to be about 0.2 for elementary collisions and about 0.4 for heavy ion collisions independently of collision energy and type of colliding system.

Neutrophil collagenase (MMP-8) cleaves at the aggrecanase site E373-A374 in the interglobular domain of cartilage aggrecan

Abstract: Native and recombinant neutrophil collagenase (MMP-8) was shown to cleave at the E373-A374 'aggrecanase' site in the interglobular domain of aggrecan. The time course of digestion in vitro showed that MMP-8 cleaved initially at N341-F342, the predominant metalloproteinase site, before cleaving at the E373-A374 site. A synthetic peptide, IPENFFG, inhibited cleavage at E373-A374 but not N341-F342 in vitro, indicating that the E373-A374 sequence was a less preferred site for MMP-8 cleavage than N341-F342. IPENFFG also inhibited release of A374 RGSVI fragments from cartilage in explant culture, suggesting that a metalloproteinase cleaved at the aggrecanase site in situ. The possibility remains that 'aggrecanase' may be a metalloproteinase in cartilage.