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1.
Eur J Neurol ; 29(9): 2559-2566, 2022 09.
Article in English | MEDLINE | ID: mdl-35538709

ABSTRACT

BACKGROUND AND PURPOSE: Brain health is essential for health, well-being, productivity and creativity across the entire life. Its definition goes beyond the absence of disease embracing all cognitive, emotional, behavioural and social functions which are necessary to cope with life situations. METHODS: The European Academy of Neurology (EAN) Brain Health Strategy responds to the high and increasing burden of neurological disorders. It aims to develop a non-disease-, non-age-centred holistic and positive approach ('one brain, one life, one approach') to prevent neurological disorders (e.g., Alzheimer's disease and other dementias, stroke, epilepsy, headache/migraine, Parkinson's disease, multiple sclerosis, sleep disorders, brain cancer) but also to preserve brain health and promote recovery after brain damage. RESULTS: The pillars of the EAN Brain Health Strategy are (1) to contribute to a global and international brain health approach (together with national and subspecialty societies, other medical societies, the World Health Organization, the World Federation of Neurology, patients' organizations, industry and other stakeholders); (2) to support the 47 European national neurological societies, healthcare and policymakers in the implementation of integrated and people-centred campaigns; (3) to foster research (e.g., on prevention of neurological disorders, determinants and assessments of brain health); (4) to promote education of students, neurologists, general practitioners, other medical specialists and health professionals, patients, caregivers and the general public; (5) to raise public awareness of neurological disorders and brain health. CONCLUSIONS: By adopting this 'one brain, one life, one approach' strategy in cooperation with partner societies, international organizations and policymakers, a significant number of neurological disorders may be prevented whilst the overall well-being of individuals is enhanced by maintaining brain health through the life course.


Subject(s)
Nervous System Diseases , Neurology , Brain , Global Health , Humans , Nervous System Diseases/therapy , Neurologists
2.
Am J Obstet Gynecol ; 195(1): 85-91, 2006 Jul.
Article in English | MEDLINE | ID: mdl-16626610

ABSTRACT

OBJECTIVE: The objective of the study was to compare 3 different approaches for increasing clients' understanding of contraceptive effectiveness. STUDY DESIGN: We randomized 900 reproductive-age women in India and Jamaica to 1 of 3 charts presenting pregnancy risk. RESULTS: The most important reason for choosing a contraceptive was how well it prevents pregnancy (54%) followed by few side effects (17%). At baseline, knowledge about contraceptive effectiveness was poor. About half knew oral contraceptive pills are more effective than condoms (46%) and intrauterine devices are more effective than injectables (50%). All 3 charts improved knowledge significantly (P < .01) for these 2 questions. No chart improved knowledge better than any other (P > .05). The chart ranking contraceptive methods on a continuum was judged slightly easier to understand than the other 2 charts. CONCLUSION: Only with accurate understanding of pregnancy risk can clients make informed choices. Our results have already informed a global handbook for family planning providers to use the chart ranking contraceptive methods on a continuum.


Subject(s)
Choice Behavior , Contraception Behavior , Health Education , Teaching Materials , Adolescent , Adult , Communication , Counseling , Family Planning Services , Female , Humans , India , Jamaica , Risk Assessment , Risk Reduction Behavior , World Health Organization
3.
Fish Shellfish Immunol ; 19(1): 53-65, 2005 Jul.
Article in English | MEDLINE | ID: mdl-15722231

ABSTRACT

In mammals, the pro-inflammatory cytokine interleukin-1 signals through a receptor complex containing a type I interleukin-1 receptor (IL-1RI) and a receptor associated protein (IL-1RAcP). Previously, we have described a cDNA from Atlantic salmon encoding a molecule with homology to the mammalian IL-RI. This molecule was named IL-1 receptor like protein (IL-1RLP) in the absence of functional data to support its proposed role as the salmon IL-1RI. Here, we describe the cloning and characterisation of a cDNA encoding salmon IL-1RAcP. Like other members of the IL-1R family, the salmon IL-1RAcP encodes three extracellular immunoglobulin-like domains and a cytoplasmic Toll/Interleukin-1 receptor (TIR) domain involved in signalling. Specific binding of salmon IL-1RAcP to IL-1RLP was shown by co-immunoprecipitation studies.


Subject(s)
Membrane Proteins/metabolism , Phylogeny , Receptors, Interleukin-1/metabolism , Salmo salar/genetics , Amino Acid Sequence , Animals , Base Sequence , COS Cells , Chlorocebus aethiops , Cloning, Molecular , Cluster Analysis , DNA Primers , Gene Library , Immunoprecipitation , Membrane Proteins/genetics , Molecular Sequence Data , Protein Structure, Tertiary , Receptors, Interleukin-1/genetics , Sequence Alignment , Sequence Analysis, DNA , Signal Transduction/immunology
4.
Dev Comp Immunol ; 28(5): 415-28, 2004 May 03.
Article in English | MEDLINE | ID: mdl-15062641

ABSTRACT

Interleukin-1 is a key inflammatory cytokine that mediates its effects through a type I receptor and a receptor accessory protein. These two molecules are members of a wider family of proteins that have in common the presence of immunoglobulin domains in the extracellular region of the protein and a TIR domain in the cytoplasmic region. The nature of this family of proteins and their signal transduction pathway is discussed in this review.


Subject(s)
Receptors, Interleukin-1/genetics , Receptors, Interleukin-1/physiology , Amino Acid Sequence , Animals , Evolution, Molecular , Humans , Interleukin-1 Receptor Accessory Protein , Interleukin-1 Receptor-Like 1 Protein , Interleukin-18 Receptor alpha Subunit , Membrane Glycoproteins/classification , Membrane Glycoproteins/genetics , Membrane Glycoproteins/physiology , Membrane Proteins/genetics , Membrane Proteins/physiology , Models, Immunological , Molecular Sequence Data , Multigene Family , Phylogeny , Proteins/classification , Proteins/genetics , Proteins/physiology , Receptors, Cell Surface/classification , Receptors, Cell Surface/genetics , Receptors, Cell Surface/physiology , Receptors, Interleukin/genetics , Receptors, Interleukin/physiology , Receptors, Interleukin-1/classification , Receptors, Interleukin-18 , Sequence Homology, Amino Acid , Signal Transduction , Toll-Like Receptors
5.
Fish Shellfish Immunol ; 15(3): 211-24, 2003 Sep.
Article in English | MEDLINE | ID: mdl-12892743

ABSTRACT

The ST2L receptor is a member of the interleukin-1 (IL-1) receptor family and has previously been cloned from human, mouse, rat and chicken. This orphan receptor has no known physiological role but has been implicated in T helper cell type 2 effector function. We describe in this report the cloning and characterisation of a cDNA encoding a homologue of ST2L in Atlantic salmon (Salmo salar). The salmon ST2L cDNA is 2364bp in length and has an open reading frame encoding a polypeptide of 582 amino acids. Similar to other members of the IL-1 receptor (IL-1R) family, the predicted protein has a potential signal peptide, extracellular immunoglobulin-like domains, a short transmembrane region and a characteristic cytoplasmic Toll-IL-1R domain. The predicted protein shows 33% identity and 44% similarity to the chicken ST2L homologue. Phylogenetic analyses cluster the putative salmon ST2L with the chicken and the mammalian ST2L homologues, away from the other members of the IL-1R family. Salmon ST2L is constitutively expressed in brain, white and red blood cells, head kidney, liver, gills and muscle, with highest level of expression in spleen. In vivo stimulation of salmon with lipopolysaccaride does not appear to have a significant effect on expression of the ST2L homologue.


Subject(s)
Phylogeny , Receptors, Interleukin-1/genetics , Salmo salar/genetics , Animals , Base Sequence , DNA Primers , DNA Probes , Gene Expression , Gene Library , Molecular Sequence Data , Reverse Transcriptase Polymerase Chain Reaction , Salmo salar/immunology
6.
J Bacteriol ; 184(7): 1932-9, 2002 Apr.
Article in English | MEDLINE | ID: mdl-11889100

ABSTRACT

Riemerella anatipestifer is responsible for exudative septicemia in ducks. The genetic determinant of the CAMP cohemolysin, cam, from a strain of R. anatipestifer was cloned and expressed in Escherichia coli. Chromosomal DNA from serotype 19 strain 30/90 was used to construct a gene library in pBluescript II SK(-) vector in E. coli XL-1-Blue strain. The clones containing recombinant plasmids were screened for the CAMP reaction with Staphylococcus aureus. Those that showed cohemolysis were chosen for further analysis by sequencing. One of these clones, JFRA8, was subcloned to identify the smallest possible DNA fragment containing the CAMP cohemolysin determinant, which was located on a 3,566-bp BamHI-BstXI fragment which specified a 1,026-bp open reading frame. Clones containing recombinant plasmids carrying cam obtained by PCR cloning into E. coli M15 strain secreted an active CAMP cohemolysin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analyses confirmed that the recombinant strain expressed a protein with a molecular mass of 37 kDa and that strains from serotypes 1, 2, 3, 5, 6, and 19 expressed the cohemolysin. The deduced amino acid sequence showed high homology to those of O-sialoglycoprotein endopeptidases. Hydrolysis of radioiodinated glycophorin A confirmed that Cam is a sialoglycoprotease.


Subject(s)
Bacterial Proteins/genetics , Flavobacterium/genetics , Hemolysin Proteins/genetics , Amino Acid Sequence , Bacterial Proteins/isolation & purification , Cloning, Molecular , DNA, Bacterial/analysis , Endopeptidases/metabolism , Flavobacterium/chemistry , Gene Amplification , Gene Expression , Genome, Bacterial , Hemolysin Proteins/isolation & purification , Immunoassay , Molecular Sequence Data , Sequence Analysis, DNA , Sequence Homology, Amino Acid , Virulence
7.
Dev Comp Immunol ; 26(5): 415-31, 2002 Jun.
Article in English | MEDLINE | ID: mdl-11906722

ABSTRACT

The interleukin-1 receptor/toll-like receptor (IL-1R/TLR) superfamily, defined by a cytosolic Toll/IL-1R (TIR) signalling domain, participates in host responses to injury and infection. We describe in this study the cloning of a cDNA encoding a Salmo salar interleukin-1 receptor-like protein (SalIL-1RLP). SalIL-1RLP comprises a potential signal peptide, three extracellular immunoglobulin domains, a short transmembrane region and an intracellular region that contains the TIR domain. The predicted amino acid sequence of SalIL-1RLP displays 43-44% similarities and 31% identities to chicken and human IL-1RI sequences. Within the intracellular region, SalIL-1RLP displays highest similarity (59%) and identity (46%) to the chicken IL-1RI sequence. Two different 5' distal UTRs were identified among six salmon IL-1RLP clones. The six clones, however, displayed identical 5' proximal UTRs, coding regions and 3' UTRs. SalIL-1RLP expression is induced in liver, head kidney, spleen and gills upon injection of salmon with bacterial lipopolysaccharide. Sequence comparisons, protein domain structures, expression patterns and phylogenetic analyses indicate that SalIL-1RLP is most closely related to type I interleukin-1 receptors and interleukin-1 receptor related proteins.


Subject(s)
DNA, Complementary/genetics , Receptors, Interleukin-1/genetics , Salmo salar/genetics , Amino Acid Sequence , Animals , Base Sequence , Cloning, Molecular , DNA, Complementary/chemistry , Gene Library , Gills/metabolism , Liver/metabolism , Molecular Sequence Data , Phylogeny , Polymerase Chain Reaction , Receptors, Interleukin-1/chemistry , Salmo salar/immunology , Salmo salar/metabolism , Sequence Homology, Nucleic Acid , Spleen/metabolism
8.
Vet Microbiol ; 84(3): 219-30, 2002 Jan 23.
Article in English | MEDLINE | ID: mdl-11731174

ABSTRACT

The generation of protective immunity against Riemerella anatipestifer infection in ducks were investigated by immunizations with recombinant glutathione sulfatransferase (GST) fusion's proteins of OmpA, a 42kDa major outer membrane protein, and P45N', a 41kDa N-terminal fragment of a newly identified 45kDa potential surface protein from R. anatipestifer. The DNA encoding OmpA and P45N' were isolated from R. anatipestifer serotype 15 (field strain 110/89) and serotype 19 (reference strain 30/90), respectively. Immunoblotting and ELISA results showed that the purified recombinant proteins induced the production of antibodies in immunized ducks. However, neither was protective against subsequent challenge with the virulent serotype 15 strain, 34/90. All the five ducks immunized with formalinized R. anatipestifer strain 34/90 survived the challenge with the homologous strain whereas six out of seven ducks in the non-immunized control group died within a week following the challenge.


Subject(s)
Bacterial Outer Membrane Proteins/immunology , Ducks , Gram-Negative Aerobic Rods and Cocci/immunology , Gram-Negative Bacterial Infections/veterinary , Poultry Diseases/prevention & control , Animals , Antibodies, Bacterial/biosynthesis , Bacterial Outer Membrane Proteins/genetics , Base Sequence , DNA, Bacterial/chemistry , DNA, Bacterial/isolation & purification , Enzyme-Linked Immunosorbent Assay/veterinary , Glutathione Transferase/chemistry , Glutathione Transferase/genetics , Gram-Negative Aerobic Rods and Cocci/genetics , Gram-Negative Bacterial Infections/immunology , Gram-Negative Bacterial Infections/prevention & control , Immunoblotting/veterinary , Molecular Sequence Data , Molecular Weight , Polymerase Chain Reaction/veterinary , Poultry Diseases/immunology , Poultry Diseases/microbiology , Recombinant Fusion Proteins/immunology , Serotyping , Specific Pathogen-Free Organisms , Vaccination/veterinary
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