Health-promoting factors in higher education for a sustainable working life - protocol for a multicenter longitudinal study.

BACKGROUND: The World Health Organization has highlighted the importance of health promotion for health service providers in order to ensure sustainable working life for individuals involved in providing health services. Such sustainability begins when students are preparing to manage their own future health and welfare in working life. It has been suggested that universities, employees and trainee health professionals should adopt or follow a salutogenic approach that not only complements the providing of information on known health risks but also favors health promotion strategies. This paper describes the study design and data collection methods in a planned study aiming to explore health-promoting factors for a sustainable working life among students in higher education within healthcare and social work. METHODS: This protocol describes a multicenter longitudinal study involving Swedish students on higher education programs in the healthcare and social work sectors. In 2018, the study invited students on seven education programs at six universities to participate. These programs were for qualification as: biomedical laboratory scientists (n = 121); dental hygienists (n = 87); nurses (n = 1411); occupational therapists (n = 111); physiotherapists (n = 48); radiographers (n = 60); and, social workers (n = 443). In total, 2283 students were invited to participate. Participants completed a baseline, a self-reported questionnaire including six validated instruments measuring health-promoting factors and processes. There are to be five follow-up questionnaires. Three while the students are studying, one a year after graduating, and one three years after graduating. Each questionnaire captures different health-promoting dimensions, namely: health-promoting resources (i.e. sense of coherence); occupational balance; emotional intelligence; health and welfare; social interaction; and work and workplace experiences/perceptions. DISCUSSION: This study focuses on the vastly important aspect of promoting a sustainable working life for healthcare and social work employees. In contrast to previous studies in this area, the present study uses different, validated instruments in health promotion, taking a salutogenic approach. It is hoped that, by stimulating the implementation of new strategies, the study's findings will lead to education programs that prepare students better for a sustainable working life in healthcare and social work.

The relationship between fear and pain levels during needle procedures in children from the parents' perspective.

BACKGROUND: The primary objective was to determine the levels of and potential relationships between procedure-related fear and pain in children. Secondary objectives were to determine if there are associations between the child's age and sex, diagnostic group, time since diagnosis, time since last needle insertion, cortisol levels and the parent's fear level in relation to fear and pain. METHODS: The child's level of pain and fear was reported by parents on 0-100 mm visual analogue scales (VAS). One hundred and fifty-one children were included consecutively when undergoing routine needle insertion into a subcutaneously implanted intravenous port. All children were subjected to one needle insertion following topical anaesthesia (EMLA) application. The effect of the child's age and sex, diagnostic group, time since diagnosis, time since last needle insertion, cortisol change levels and the parent's fear level, on fear and pain levels was investigated with multiple regression analysis. RESULTS: The needle-related fear level (VAS mean 28 mm) was higher than the needle-related pain level (VAS mean 17 mm) when topical anaesthesia is used according to parents' reports (n = 151, p < 0.001). With fear as the dependent variable, age and pain were significantly associated and explained 33% of the variance, and with pain as the dependent variable, fear, parents' fear and change in cortisol level were significantly associated and explained 38% of the variance. CONCLUSIONS: According to parents, children experienced more fear than pain during needle insertion when topical anaesthesia is used. Therefore, in addition to pain management, an extended focus on fear-reducing interventions is suggested for needle procedures.

Effect of high-dose paracetamol on needle procedures in children with cancer--an RCT.

AIM: The aim was to investigate whether children experience less pain, fear and/or distress when they receive high-dose paracetamol compared with placebo, using a needle insertion in a subcutaneously implanted intravenous port as a model. METHODS: Fifty-one children ranging from 1 to 18 years of age being treated in a paediatric oncology setting were included consecutively when undergoing routine needle insertion into a subcutaneously implanted intravenous port. All children were subjected to one needle insertion following topical anaesthetic (EMLA) application in this double-blind, placebo-controlled RCT, comparing orally administered paracetamol (n = 24) 40 mg/kg body weight (max 2000 mg) with placebo (n = 27). The patients' pain, fear and distress were reported by parents, nurses and children (≥7 years of age) using 0- to 100-mm visual analogue scales (VAS). In addition, pain observation, procedure time and cortisol reduction were assessed. RESULTS: No differences between the paracetamol and the placebo group were found with respect to demographic characteristics. According to VAS reports, paracetamol did not reduce pain, fear and distress compared with placebo. Pain observation, cortisol reduction and procedure time did not differ between the study groups. CONCLUSION: Paracetamol provides no additive effect in reducing pain, fear and distress when combined with topical anaesthesia in children undergoing port needle insertion.

Randomized interventions for needle procedures in children with cancer.

The aim of this study was to examine whether children experience less fear, distress and pain connected to a routine needle insertion in an intravenous port when subjected to an intervention: blowing soap bubbles or having a heated pillow vs. standard care. Twenty-eight children, 2-7 years, cared for at a paediatric oncology unit, undergoing a routine needle insertion in an intravenous port were included consecutively. All children were subjected to two needle insertions; at the first they received standard care, and at the second standard care + a randomized intervention. Parents and nurses assessed children's fear, distress and pain on 0-100 mm visual analogue scales. According to parents' report, children experienced less fear when subjected to intervention vs. standard care reported by parents (P < 0.001). Children also experienced less fear (P < 0.05) and distress (P < 0.05) when subjected to standard care + blowing soap bubbles vs. standard care (n = 14), and less fear when subjected to standard care + heated pillow vs. standard care (P < 0.05). Nurses' reports did not show any differences for standard care + intervention vs. standard care. Blowing soap bubbles or having a heated pillow is more effective than standard care in reducing children's fear and distress in needle procedures, according to parents' report.

Efeito de diferentes níveis de vitamina e sobre a ocorrência de Ectoparasitas em larvas de Tilápia do Nilo (Oreochromis niloticus) no processo de reversão sexual / The effect of different levels of vitamin e on the occurrence of Ectoparasites on Nile Tilapia (Oreochromis niloticus) larvae during sexual reversion

De dezembro de 1999 a janeiro de 2000, foi avaliado o efeito de diferentes níveis de vitamina E na ração de larvas de O. niloticus durante o processo de reversão sexual, observando-se a ocorrência de ectoparasitas, sobrevivência, peso médio, comprimento total médio e biomassa total das larvas. O experimento foi conduzido no distrito de Floriano, na Estação de Piscicultura da Universidade Estadual de Maringá, UEM-CODAPAR. As unidades experimentais eram compostas de caixas de cimento amianto de 250 litros, sendo que cada uma iniciou o experimento com 200 larvas em um volume de 100 litros. Estas caixas estavam localizadas em uma estufa revestida lateralmente por lona plástica e com cobertura de sombrite (50 por cento de luminosidade). As larvas foram submetidas a quatro tratamentos: T1 (25), T2 (250), T3 (500) e T4 (750) mg de vitamina E/kg de ração com 60mg de 17a-metiltestosterona/kg de ração. Cada tratamento tinha quatro repetições. Semanalmente foram aferidos os parâmetros físicos e químicos da água. No início do experimento, foi estimada a ocorrência de ectoparasitas de 50 larvas, naturalmente infectadas e posteriormente, a cada semana, foi estimada a ocorrência em 20 larvas por tratamento. Ao final do experimento foram medidos e pesados 100 peixes e contados todos os peixes por unidade experimental. No inicio as larvas apresentavam 9,8 mm de comprimento total e 0,02 g de peso médio, sendo que a ocorrência de ectoparasitas foi de 100,0 por cento. Ao final do experimento não foi encontrarada diferença significativa entre os tratamentos, quanto à ocorrência de ectoparasitas. Em relação aos grupos de ectoparasitas, houve diferença significativa para os monogenéticos, entre T2 (43,8 por cento) e T3 (21,3 por cento). Não foi encontrado diferença significativa para biomassa total e sobrevivência dos peixes.

A highly variable region in members of the streptococcal M protein family binds the human complement regulator C4BP.

Strains of Streptococcus pyogenes express one or more molecules that are members of the M protein family, a group of surface proteins implicated in virulence. A characteristic property of the molecules in this family is the presence of a highly variable N-terminal region, whose function is unknown. Here we show that human C4b-binding protein (C4BP), a regulatory component of the complement system, binds to the highly variable region of many members of the M protein family. Chimeric molecules, in which the N-terminal regions of four different C4BP-binding proteins were combined with the C-terminal part of the non-binding M5 protein, had intact C4BP-binding ability, as judged by binding assays and Scatchard analysis with highly purified molecules. Moreover, work with the C4BP-binding Arp4 protein showed that an N-terminal 52-residue fragment retained binding ability, and that a 21-residue synthetic peptide derived from the variable region completely inhibited the binding of C4BP. Computer-assisted analysis of the four C4BP-binding regions studied here (45-66 amino acid residues) indicated that they lack residue identities that could explain their ability to bind the same ligand, but differ from the nonbinding M5 protein in their lower propensity to form a coiled-coil. Thus, the variable C4BP-binding regions have an extraordinary capacity for sequence variation, while retaining the ability to bind C4BP. These data indicate that an important function of the variable region in members of the M protein family is to bind a host protein that down-regulates the complement system.

Complementation of divergent mga genes in group A Streptococcus.

The gene (mga4) encoding the positive regulatory protein, Mga4, was cloned and sequenced from an M type 4 strain (AP4) of Streptococcus pyogenes. The deduced amino acid (aa) sequence of this "divergent Mga' shows 88% identity to the prototype Mga1 in its N-terminal half, which contains all three of the predicted helix-turn-helix domains. However, one of the predicted receiver domains of Mga1, which is at its C terminus, is not conserved in the Mga4 aa sequence. Nevertheless, a mutation in mga1 was found to be complemented for activation of the gene encoding M protein (emm) by mga4 in trans. This suggests that the aa residues of the C-terminal predicted receiver domain are not critical for activation of emm transcription.

Molecular characterization of a saline-soluble lectin from a parasitic fungus. Extensive sequence similarities between fungal lectins.

It has been proposed that the interactions between several parasitic and pathogenic fungi and their hosts are mediated by soluble lectins present in the fungus. We have cloned and analyzed a gene encoding such a lectin (AOL) from the nematophagous fungus Arthrobotrys oligospora (deuteromycete). The deduced primary structure of the AOL gene displayed an extensive similarity (identity 46.3%) to that of a gene encoding a lectin (ABL) recently isolated from the mushroom Agaricus bisporus (basidiomycete), but not to any other fungal, microbial, plant or animal lectins. The similarities between AOL and ABL were further demonstrated by the observation that an antibody specific for AOL cross-reacted with ABL. Together with data showing that AOL has a binding specificity that is similar to that of ABL [Rosen, S., Bergström, J., Karlsson, K.-A. & Tunlid, A. (1996) Eur. J. Biochem. 238, 830-837], these results indicate that AOL and ABL are members of a novel family of saline soluble lectins present in fungi. Southern blots indicated that there is only one AOL gene in the genome encoding a subunit (monomer) of the lectin. The primary structure of AOL did not show the presence of a typical N-terminal signal sequence. Comparison of the deduced primary structure with the molecular mass of AOL as determined by electrospray mass spectrometry (16153 Da), indicated that AOL has an acetylated N-terminal but no other post-translational modifications, and that a minor isoform is formed by deamidation. Circular dichroism (CD) spectroscopy suggested that the secondary structure of AOL contains 34% beta-sheets, 21% alpha-helix, and 45% turns and coils.

Identification of the IgA-binding region in streptococcal protein Arp.

Cell surface proteins that bind to the Fc part of human IgA are expressed by different species of pathogenic streptococci. The most extensively characterized streptococcal IgA-binding protein is the Streptococcus pyogenes protein Arp4, a member of the M protein family. Here we describe work that identifies the IgA-binding region in this streptococcal protein. A comparison of the amino acid sequences of protein Arp4 and four other IgA-binding proteins of S. pyogenes first made possible the identification of a putative IgA-binding region. Site-specific mutagenesis and generation of deletions were then used to show that Arp4 derivatives lacking different parts of the putative IgA-binding region had lost the ability to bind IgA. Conclusive evidence for the localization of the IgA-binding region was obtained through the characterization of a chimeric protein, in which the putative IgA-binding region of Arp4 had been introduced into another S. pyogenes cell surface protein that does not bind IgA. Our data show that a region comprising 29-amino acid residues in the N-terminal part of Arp4 is necessary and sufficient for IgA-binding capacity. Competitive inhibition experiments with synthetic peptides indicated that the C-terminal half of this 29 residue region may be most important for the IgA-binding property of Arp4. These results identify, for the first time, the ligand-binding region in an Fc alpha binding protein.

Conserved and variable regions in protein Arp, the IgA receptor of Streptococcus pyogenes.

The streptococcal M protein family, a number of cell surface molecules that interact with the human immune system, can be divided into two major classes, A and C, characterized by different types of repeats in the central part of the molecule. Class A and class C molecules are known to have a variable N-terminal region and a more conserved C-terminal region, but little is known about the mechanisms that give rise to this structural variation. In this report, we show that two variants of protein Arp, an IgA receptor in class C of the M protein family, have virtually identical signal sequences and C-terminal halves, but unrelated N-terminal sequences. Comparison of the sequences of the two genes and their flanking regions also demonstrates the presence of well-defined variable and conserved regions. Our results strongly suggest that the N-terminal sequence variation between the two variants of protein Arp was generated through an intergenic recombination event, rather than through intragenic recombination or accumulation of mutations.

Protein D, the immunoglobulin D-binding protein of Haemophilus influenzae, is a lipoprotein.

Protein D is an immunoglobulin D-binding membrane protein exposed on the surface of the gram-negative bacterium Haemophilus influenzae. Results reported here indicate that protein D is a lipoprotein. The protein is apparently synthesized as a precursor with an 18-residue-long signal sequence modified by the covalent attachment of both ester-linked and amide-linked palmitate to the cysteine residue, which becomes the amino terminus after cleavage of the signal sequence. Globomycin inhibited maturation of protein D in H. influenzae, implying that protein D is exported through the lipoprotein export pathway. A mutant expressing a protein D lacking the cysteine residue was constructed by oligonucleotide site-directed mutagenesis. The mutated protein D molecule was not acylated and partitioned in the aqueous phase after Triton X-114 extraction of intact bacteria, unlike native and recombinant protein D, which partitioned in the detergent phase. The nonacylated protein D molecule was localized to the periplasmic space of Escherichia coli. The hydrophilic protein D molecule will be used in investigations concerning its ability to function as a vaccine component.

Duplication of a DNA sequence homologous to genes for immunoglobulin receptors and M proteins in Streptococcus pyogenes.

The nucleotide sequence of an open reading frame of 355 amino acids downstream of the IgA-binding protein gene arp4 in Streptococcus pyogenes M-type 4 has been determined. Analysis of the deduced amino acid sequence for the open reading frame shows an extensive homology to streptococcal M proteins and immunoglobulin binding proteins. Expression of the open reading frame has not been detected and the function may be as a genetic reservoir in the generation of new immunoglobulin receptors and antigenic variants of M proteins.

Molecular characterization of an IgA receptor from group B streptococci: sequence of the gene, identification of a proline-rich region with unique structure and isolation of N-terminal fragments with IgA-binding capacity.

Certain strains of group B streptococci express a cell surface protein that binds IgA and acts as a virulence factor. This IgA receptor is referred to here as protein Bac. The gene for protein Bac was cloned and expressed in Escherichia coli, and the complete nucleotide sequence was determined. The deduced amino acid sequence of 1134 residues includes a signal sequence of 37 amino acids and a putative membrane anchor region at the C-terminal end. The processed form of the receptor, 1097 residues, has a calculated molecular weight of 123,786. There are no cysteines in protein Bac, suggesting a fibrillar structure. The C-terminal half of the protein includes a 90 residues long region with a novel type of periodic structure, the "XPZ motif", in which every third amino acid is proline. Unlike other bacterial immunoglobulin-binding proteins, there are no long repeats in protein Bac. Clones which express only part of the protein Bac gene were used to show that IgA-binding takes place in the N-terminal part of the molecule. Protein Bac was originally described as an antigen called beta, but N-terminal fragments that bind IgA do not react with a reference serum against the beta antigen. These and other data indicate that protein Bac can be divided into two regions with different functions: an N-terminal IgA-binding region and a C-terminal region corresponding to the beta antigen. The IgA-binding region of protein Bac does not show any homology to protein Arp, the IgA receptor from group A streptococci, although these receptors have similar binding properties. This indicates that convergent evolution has favored the appearance of these two structurally different streptococcal IgA receptors.

Protein D, an immunoglobulin D-binding protein of Haemophilus influenzae: cloning, nucleotide sequence, and expression in Escherichia coli.

The gene for protein D, a membrane-associated protein with specific affinity for human immunoglobulin D, was cloned from a nontypeable strain of Haemophilus influenzae. The gene was expressed in Escherichia coli from an endogenous promoter, and the gene product has an apparent molecular weight equal to that of H. influenzae protein D (42,000). The complete nucleotide sequence of the gene for protein D was determined, and the deduced amino acid sequence of 364 residues includes a putative signal sequence of 18 amino acids containing a consensus sequence, Leu-Ala-Gly-Cys, for bacterial lipoproteins. The sequence of protein D shows no similarity to those of other immunoglobulin-binding proteins. Protein D is the first example of immunoglobulin receptors from gram-negative bacteria that has been cloned and sequenced.

Extensive sequence homology between IgA receptor and M proteins in Streptococcus pyogenes.

Many strains of Streptococcus pyogenes are known to express a receptor for IgA. The complete nucleotide sequence of the gene for such a receptor, protein Arp4, has been determined. The deduced amino acid sequence of 386 residues includes a signal sequence of 41 amino acids and a putative membrane anchor region, both of which are homologous to similar regions in other streptococcal surface proteins. The processed form of the IgA receptor has a length of 345 amino acids and a calculated molecular weight of 39544. The N-terminal sequence of the processed form is different from that previously found for a similar IgA receptor isolated from a S. pyogenes strain of type M60. The sequence of protein Arp4 shows extensive homology to the C-terminal half of streptococcal M proteins, but not to the streptococcal IgG receptor protein G or staphlyococcal protein A. Apart from the membrane anchor, this homology includes a sequence of 119 amino acid residues containing three repeated units and a 54-residue sequence without repeats. The protein expressed in Escherichia coli is found in the periplasmic space, in which it constitutes the major protein. Protein Arp4 is the first example of a surface protein that has both immunoglobulin-binding capacity and structural features characteristic of M proteins.

Cervical score and onset of spontaneous labor in prolonged pregnancy dated by second-trimester ultrasonic scan.

The interval from expected day of delivery to spontaneous onset of labor was correlated with parity and cervical score in 103 women with uncomplicated prolonged pregnancy (greater than 294 days). All women had a routine ultrasonic scan in weeks 16-18 for the purpose of dating. The mean (+/- SD) modified Bishop score on entry to the study was 4.15 +/- 2.0 for nulliparas and 4.90 +/- 2.1 for multiparas. The duration beyond 294 days to spontaneous onset of labor varied little (mean 3.5-4.5 days) for nulliparas with scores greater than 2 and for multiparas regardless of score. Nulliparous women with a poor score (less than 3) had spontaneous onset of labor and delivery within a mean of 9.8 days. Half of the multiparas (50.0%) and 43.9% of the nulliparas gave birth within 3 days. About 90% of all women gave birth within 7 days. All but three had a vaginal delivery; the instrumental vaginal delivery rate was 16.3%. The results suggest that in postterm women dated with a second-trimester ultrasonic scan, the cervical scores are in general more favorable than previously reported in series not dated with early scans. The postterm group is also much smaller, and the time interval from entry into the postterm period to spontaneous onset of labor is shorter.

New properties of Bacillus subtilis succinate dehydrogenase altered at the active site. The apparent active site thiol of succinate oxidoreductases is dispensable for succinate oxidation.

Mammalian and Escherichia coli succinate dehydrogenase (SDH) and E. coli fumarate reductase apparently contain an essential cysteine residue at the active site, as shown by substrate-protectable inactivation with thiol-specific reagents. Bacillus subtilis SDH was found to be resistant to this type of reagent and contains an alanine residue at the amino acid position equivalent to the only invariant cysteine in the flavoprotein subunit of E. coli succinate oxidoreductases. Substitution of this alanine, at position 252 in the flavoprotein subunit of B. subtilis SDH, by cysteine resulted in an enzyme sensitive to thiol-specific reagents and protectable by substrate. Other biochemical properties of the redesigned SDH were similar to those of the wild-type enzyme. It is concluded that the invariant cysteine in the flavoprotein of E. coli succinate oxidoreductases corresponds to the active site thiol. However, this cysteine is most likely not essential for succinate oxidation and seemingly lacks an assignable specific function. An invariant arginine in juxtaposition to Ala-252 in the flavoprotein of B. subtilis SDH, and to the invariant cysteine in the E. coli homologous enzymes, is probably essential for substrate binding.

Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit.

The class II enzyme of human liver alcohol dehydrogenase was isolated, carboxymethylated, and cleaved with CNBr and proteolytic enzymes. Sequence analysis of peptides established structures corresponding to the pi subunit. Two segments from the C-terminal region unique to pi were selected for synthesis of oligodeoxyribonucleotide probes to screen a human liver cDNA library constructed in plasmid pT4. Sequence analysis of two identical hybridization-positive clones with cDNA inserts of about 2000 nucleotides gave the entire coding region of the pi subunit, a 61-nucleotide 5' noncoding region and a 741-nucleotide 3' noncoding region containing four possible polyadenylation sites. Translation of the coding region yields a 391-residue polypeptide, which in all regions except the C-terminal segment corresponds to the protein structure as determined directly by peptide analysis. With the class I numbering system, the exception concerns a residue exchange at position 368, the actual C-terminus which is Phe-374 by peptide data but a 12-residue extension by cDNA data, and possibly two further residue exchanges at positions 303 and 312. The size difference might indicate the existence of posttranslational modifications of the mature protein or, in combination with the residue exchanges, the existence of polymorphism at the locus for class II subunits. The pi subunit analyzed directly results in a 379-residue polypeptide and is the only class II size thus far known to occur in the mature protein.(ABSTRACT TRUNCATED AT 250 WORDS)