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1.
Acta Paediatr ; 98(12): 1977-81, 2009 Dec.
Article in English | MEDLINE | ID: mdl-19814751

ABSTRACT

AIM: To investigate whether severe loss of activities of daily living (ADL) in asylum-seeking children is associated with physical disease or toxic influences and to describe the clinical course during the recovery process. METHODS: A total of 29 asylum-seeking children with severe loss of ADL were regularly assessed by physical examinations, laboratory tests and a structured evaluation of their ADL status during rehabilitation. RESULTS: A total of 12 children had previously recorded suicide attempts and 21 were recorded to have experienced traumatic events in their country of origin. The mean time from turning point to recovery was 6 months. Of the study participants, 22 needed enteral feeding and 18 gained weight during recovery. All children had a pulse rate and systolic blood pressure within the normal range. No sign of intoxication or physical disease was identified in laboratory tests or clinical examinations, with the exception of one case of epilepsy. CONCLUSION: Physical disease, pharmacological sedation or anorexia nervosa was not considered to be a probable cause of the loss of ADL in these children. The high rate of psychosocial risk factors and the stressful event of being in an asylum-seeking process call for further investigation of psychosomatic mechanisms.


Subject(s)
Activities of Daily Living , Refugees , Rehabilitation , Adolescent , Anorexia Nervosa/diagnosis , Child , Enteral Nutrition/statistics & numerical data , Female , Health Status , Humans , Hypnotics and Sedatives/blood , Hypnotics and Sedatives/urine , Interviews as Topic , Length of Stay/statistics & numerical data , Male , Refugees/psychology , Refugees/statistics & numerical data , Risk Factors , Severity of Illness Index , Sweden , Young Adult
2.
J Biol Chem ; 276(22): 18947-52, 2001 Jun 01.
Article in English | MEDLINE | ID: mdl-11259413

ABSTRACT

The binding of native biglycan and decorin to pepsin-extracted collagen VI from human placenta was examined by solid phase assay and by measurement of surface plasmon resonance in the BIAcore(TM)2000 system. Both proteoglycans exhibited a strong affinity for collagen VI with dissociation constants (K(D)) of approximately 30 nm. Removal of the glycosaminoglycan chains by chondroitinase ABC digestion did not significantly affect binding. In coprecipitation experiments, biglycan and decorin bound to collagen VI and equally competed with the other, suggesting that biglycan and decorin bind to the same binding site on collagen VI. This was confirmed by electron microscopy after negative staining of complexes between gold-labeled proteoglycans and collagen VI, demonstrating that both biglycan and decorin bound exclusively to a domain close to the interface between the N terminus of the triple helical region and the following globular domain. In solid phase assay using recombinant collagen VI fragments, it was shown that the alpha2(VI) chain probably plays a role in the interaction.


Subject(s)
Collagen/chemistry , Collagen/metabolism , Proteoglycans/metabolism , Animals , Biglycan , Binding, Competitive , CHO Cells , Cattle , Chondroitin ABC Lyase/pharmacology , Cricetinae , Decorin , Dose-Response Relationship, Drug , Extracellular Matrix Proteins , Glycosaminoglycans/metabolism , HeLa Cells , Humans , Kinetics , Microscopy, Electron , Placenta/metabolism , Precipitin Tests , Protein Binding , Protein Conformation , Protein Structure, Tertiary , Recombinant Proteins/metabolism , Surface Plasmon Resonance
3.
J Biol Chem ; 276(1): 187-93, 2001 Jan 05.
Article in English | MEDLINE | ID: mdl-11027693

ABSTRACT

Collagen VI assembly is unique within the collagen superfamily in that the alpha 1(VI), alpha 2(VI), and alpha 3(VI) chains associate intracellularly to form triple helical monomers, and then dimers and tetramers, which are secreted from the cell. Secreted tetramers associate end-to-end to form the distinctive extracellular microfibrils that are found in virtually all connective tissues. Although the precise protein interactions involved in this process are unknown, the N-terminal globular regions, which are composed of multiple copies of von Willebrand factor type A-like domains, are likely to play a critical role in microfibril formation, because they are exposed at both ends of the tetramers. To explore the role of these subdomains in collagen VI intracellular and extracellular assembly, alpha 3(VI) cDNA expression constructs with sequential N-terminal deletions were stably transfected into SaOS-2 cells, producing cell lines that express alpha 3(VI) chains with N-terminal globular domains containing modules N9-N1, N6-N1, N5-N1, N4-N1, N3-N1, or N1, as well as the complete triple helix and C-terminal globular domain (C1-C5). All of these transfected alpha 3(VI) chains were able to associate with endogenous alpha 1(VI) and alpha 2(VI) to form collagen VI monomers, dimers, and tetramers, which were secreted. Importantly, cells that expressed alpha 3(VI) chains containing the N5 subdomain, alpha 3(VI) N9-C5, N6-C5, and N5-C5, formed microfibrils and deposited a collagen VI matrix. In contrast, cells that expressed the shorter alpha 3(VI) chains, N4-C5, N3-C5, and N1-C5, were severely compromised in their ability to form end-to-end tetramer assemblies and failed to deposit a collagen VI matrix. These data demonstrate that the alpha 3(VI) N5 module is critical for microfibril formation, thus identifying a functional role for a specific type A subdomain in collagen VI assembly.


Subject(s)
Collagen/chemistry , Collagen/metabolism , Microfibrils/metabolism , Microfibrils/ultrastructure , Collagen/genetics , Collagen/ultrastructure , Electrophoresis, Polyacrylamide Gel , Fluorescent Antibody Technique, Indirect , Humans , Macromolecular Substances , Microfibrils/genetics , Microscopy, Electron , Protein Structure, Quaternary , Protein Structure, Tertiary , RNA, Messenger/genetics , RNA, Messenger/metabolism , Sequence Deletion , Transfection , Tumor Cells, Cultured
4.
Int J Food Microbiol ; 29(2-3): 353-60, 1996 Apr.
Article in English | MEDLINE | ID: mdl-8796434

ABSTRACT

Motility enrichment on modified semisolid Rappaport-Vassiliadis (MSRV) medium was evaluated for a rapid Salmonella detection in naturally contaminated food- and feed samples. The results of this procedure were compared with a conventional cultural procedure using Rappaport-Vassiliadis (RV) broth as selective enrichment and modified brilliant green-, xylose lysine desoxycholate- and mannitol lysine crystal violet brilliant green agar for selective plating. The productivity of motility enrichment was 87% compared to a productivity of 99% for the cultural procedure. Statistical analysis showed that there was a significant difference at the 5% level. The present study shows that a combination of direct motility enrichment with the cultural procedure could be used as a very rapid and highly cost-efficient method for Salmonella detection.


Subject(s)
Bacteriological Techniques , Culture Media/chemistry , Food Microbiology , Salmonella/isolation & purification
5.
J Appl Bacteriol ; 66(6): 523-8, 1989 Jun.
Article in English | MEDLINE | ID: mdl-2753844

ABSTRACT

Growth rate of salmonellas in Rappaport-Vassiliadis broth (RV) decreased with higher temperature when incubated at 40, 42 and 43 degrees C. Home-made RV and RV-Merck were less inhibitory than RV-Oxoid and RV-lab m. At 43 degrees C growth of all strains of Salmonella dublin were almost completely inhibited in all types of RV. In home-made RV and RV-Merck incubated at 42 degrees C, Salm. dublin was not inhibited any more than other serotypes tested. Variations in growth rate between different types of RV could be explained by differences in concentration of MgCl2. RV with higher MgCl2-concentration were most inhibitory. It is proposed that RV should be incubated at 41.5 +/- 0.5 degrees C (42.0 +/- 0.1 degrees C in a waterbath) and that the amount of MgCl2.6H2O should be approximately 28.6 g/l of the ready-to-use medium, which corresponds to the formula in the original description.


Subject(s)
Culture Media , Magnesium , Salmonella/growth & development , Temperature , Magnesium Chloride , Osmolar Concentration
7.
J Food Prot ; 46(5): 391-399, 1983 May.
Article in English | MEDLINE | ID: mdl-30913656

ABSTRACT

Twelve laboratories from 7 countries compared the productivity of refrigerated (72 h at 5 to 10°C) preenrichment and enrichment broth cultures with a standard cultural procedure for detection of Salmonella in 466 naturally contaminated low and high moisture foods. Refrigerated preenrichment and enrichment cultures identified 92.5 and 94.2% of contaminated samples, respectively. Variations in the ability of laboratories to successfully recover salmonellae under refrigeration test conditions were notable. Three laboratories found complete agreement between results by the standard and refrigeration test procedures and 5 additional laboratories reported >90% accuracy; lowest recovery rate for combined refrigeration results was 77%. Sensitivity of the refrigeration techniques was markedly greater with low than high moisture foods where the latter contributed all but two of the 62 false-negative results encountered in this study. Ability of individual laboratories to recover Salmonella from refrigerated preenrichment and enrichment broth cultures was not significantly different for given food categories. Productivity of paired enrichment-plating media differed widely with food type. Selective enrichment in tetrathionate brilliant green and plating on bismuth sulfite agar showed greatest sensitivity for isolation of Salmonella in high but not in low moisture foods where productivity of the 4 enrichment-plating conditions used in this study was comparable. Results on recoverability of Salmonella from refrigerated broth cultures concur with findings of an earlier comparative study and strongly support incorporation of this novel approach in standard cultural methods for detection of Salmonella in foods.

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