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- Bondestam, E, et al.
(författare)
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Pain assessment by patient and nurse in the early phase of acute myocardial infarction
- 1987
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Ingår i: Journal of Advanced Nursing. - : Wiley-Blackwell. - 0309-2402 .- 1365-2648. ; 12:6, s. 677-682
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Tidskriftsartikel (refereegranskat)abstract
- In 47 patients admitted to the coronary care unit (CCU) at Sahlgren's Hospital in Göteborg, Sweden, due to acute myocardial infarction (MI) the intensity of pain independently assessed by the patient and by the nurse on duty was evaluated during the first 24 hours in CCU. Pain was assessed according to a modified numerical rating scale graded from 0-10, where 0 meant no pain and 10 meant the most severe pain. A positive correlation between the patients’ and nurses’ assessments was found (r = 0-76; P < 0-001). However, the nurses under-estimated the patients’ pain in 23% of the situations and over-estimated it in 20%. Over-estimation was particularly found when heart rate and blood pressure increased. Many patients scoring their pain to fairly high degrees were not given pain-relieving treatment. Treatment with morphine did not cause substantial pain relief in a substantial number of patients. A significantly positive correlation was found between the patients’ and nurses’ assessments of pain, although underestimation as well as over-estimation occurred. A few patients with severe pain were not treated and when treatment was given it was often ineffective.
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| 7. |
- Johansson, Hugo, et al.
(författare)
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Herpes simplex type 1-induced Fc receptor binds to the Cgamma2-Cgamma3 interface region of IgG in the area that binds staphylococcal protein A
- 1989
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Ingår i: Immunology. - 0019-2805. ; 66:1, s. 8-13
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Tidskriftsartikel (refereegranskat)abstract
- The binding site of immunoglobulin G (IgG) to herpes simplex virus (HSV) type 1-induced Fc receptor was investigated using human IgG Fc intermediate (Fc(i)) fragments, fragment D of staphylococcal protein A (SPA) and chemically modified human IgG. Human IgG Fc(i) fragment composed of one Cgamma2 and two Cgamma3 domains, bound strongly to HSV-1-infected cells. Fragment D, a monovalent subunit of SPA, inhibited the binding of radiolabelled human IgG Fc fragments to the HSV Fc receptor. Reductively methylated human IgG reacted equally well to HSV-infected cells, as did chemically unmodified IgG in contrast to N-acetylimidazole-modified and diethylpyrocarbonate-modifed human IgG, which were unreactive. These results suggest a similar binding site on human IgG for SPA and the HSV-1 Fc receptor with involvement of the amino acid residues Tyr and His but not Lys. The similarities of binding sites on the IgG molecule for the HSV-1 Fc receptor and rheumatoid factors (RF) may be important for understanding the mechanism of RF production in rheumatoid arthritis or other disease states.
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| 8. |
- Johansson, Hugo, et al.
(författare)
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Interaction between herpes simplex type 1-induced Fc receptor and human and rabbit immunoglobulin G (IgG) domains
- 1986
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Ingår i: Immunology. - 0019-2805. ; 58:2, s. 251-255
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Tidskriftsartikel (refereegranskat)abstract
- Cells infected with herpes simplex virus type 1 (HSV-1) express a cell surface receptor able to bind to the Fc region of immunoglobulin G (IgG). The ability of HSV-1-infected cells to bind 125I-labelled human and rabbit IgG and IgG fragments was studied to localize the site of interaction to the C gamma 2 or C gamma 3 domains of IgG. 125I-labelled IgG and IgG Fc fragments consisting of C gamma 2 and C gamma 3 domains bound strongly to HSV-infected cells and did not bind to uninfected cells. In contrast, 125I-labelled F(ab')2, Facb [consisting of F(ab')2 and C gamma 2 domains] and pFc' (consisting of C gamma 3 domains) fragments did not bind to any of these cells. Unlabelled IgG and IgG Fc fragments inhibited the interaction between 125I-labelled rabbit IgG Fc and the HSV Fc receptor, whereas F(ab')2, Facb and pFc' fragments failed to inhibit this interaction. These data indicate that the HSV Fc receptor requires both the C gamma 2 and C gamma 3 domains for interaction with the IgG molecule analogous to the known interaction of protein A of Staphylococcus aureus, the Fc binding proteins of Group A, C and G streptococci, and certain human rheumatoid factors.
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| 10. |
- Nardella, F A, et al.
(författare)
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Fc epitopes for human rheumatoid factors and the relationships of rheumatoid factors to the Fc binding proteins of microorganisms
- 1988
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Ingår i: Scandinavian Journal of Rheumatology. Supplement. - : Informa UK Limited. - 1502-7740 .- 0300-9742 .- 1502-7732. ; 17:Suppl. 75, s. 190-198
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Tidskriftsartikel (refereegranskat)abstract
- Work from our laboratories has shown that the major antigenic determinants for rheumatoid factors (RFs) are in the C gamma 2-C gamma 3 interface region of IgG in the same area that binds staphylococcal protein A (SPA). Furthermore, the Fc binding proteins of groups A, C and G streptococci as well as the Fc binding proteins induced on cell surfaces by herpes simplex virus type I also bind to the same area of IgG. These binding site similarities between RFs and the microbial Fc binding proteins suggested conformational similarities between the RF antigen combining regions and the Fc binding regions of the microbial proteins. This hypothesis was supported by the observation that antibodies to SPA bind to the antigen combining regions of most RFs as well as to the Fc binding region of the T15 group A streptococcal Fc binding protein. These findings indicate that RFs bear the conformational internal image of these microbial proteins and suggest that RFs could arise as antibodies to the idiotypic determinants on antibodies to microbial Fc binding proteins. Alternatively, microbial Fc binding proteins could present IgG to the immune system in a way that renders specific areas of the C gamma 2-C gamma 3 interface region immunogenic. These relationships between RFs and microbial Fc binding proteins may prove to be important for our understanding of the generation of RFs in rheumatoid arthritis.
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