| 1. |
- Hansson, Ulla-Britt, et al.
(author)
-
IgG with a deviant conformation in serum and synovial fluid from rheumatoid arthritis patients
- 1985
-
In: Scandinavian Journal of Immunology. - : Wiley. - 0300-9475 .- 1365-3083. ; 22:1, s. 27-32
-
Journal article (peer-reviewed)abstract
- Specific rabbit antisera were prepared against an IgG with a special conformation (IgG spec.) previously detected in some sera from patients with rheumatoid arthritis. The antibodies had no affinity to normal human IgG and were not anti-idiotypic to human rheumatoid factor. The affinity of IgG spec, to the antibodies could not be explained by an antiglobulin activity to rabbit IgG. The amount of protein with affinity to immobilized specific IgG F(ab′)2 of the antibodies was determined in serum and synovial fluid from patients with various joint diseases. A relationship between the content of IgG spec, and the diagnosis of seropositive rheumatoid arthritis was found on analysis of serum samples. IgG spec, also occurred in synovial fluid from some individuals with seropositive rheumatoid arthritis. Differences in the serum content of IgG spec, could not be explained by differences in the normal IgG content. Circular dichroism analysis of isolated IgG spec, showed that in the region(s) close to tyrosine residue(s) this polyclonal protein had similarities to heat-aggregated IgG.
|
|
| 2. |
- Truedsson, L, et al.
(author)
-
Protein HC-IgA complexes carry antibody activities
- 1988
-
In: Scandinavian Journal of Immunology. - : Wiley. - 0300-9475 .- 1365-3083. ; 27:2, s. 201-208
-
Journal article (peer-reviewed)abstract
- Polyclonal protein HC-IgA complexes (HC-IgA) were isolated from two different serum pools. Their hydrodynamic volumes were found to be slightly greater than that of monomeric IgA but less than that of dimeric IgA. Sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis of reduced and carboxymethylated complexes followed by immunoblotting showed that the complexes contained normal light and heavy Ig chains, and one polypeptide chain with Mr = 90,000, which carried both IgA alpha chain and protein HC epitopes. Enzyme-linked immunosorbent assays (ELISA) demonstrated that the isolated HC-IgA carried about 0.1 and 4%, respectively, of the antibody activities against one carbohydrate antigen (Yersinia enterocolitica serotype 0:3 lipopolysaccharide) and one protein antigen (rabbit IgG, i.e. antigen for rheumatoid factors) of the IgA populations of the two serum pools. HC-IgA with rheumatoid factor activity could also be demonstrated in the unfractionated serum pool. The binding of HC-IgA in the ELISA was not mediated through its protein HC part. The present observations show that HC-IgA carries antibody activities and constitutes a unique class of IgA complexes, since it does not dissociate under denaturating conditions after reduction. It may represent a further biological potential of the humoral immune system.
|
|
| 3. |
- Gustafsson, A, et al.
(author)
-
Similar effects of treatment with alpha interferon on the protein synthesis of human large granular lymphocytes, T cells, and monocytes.
- 1985
-
In: Scandinavian Journal of Immunology. - 0300-9475 .- 1365-3083. ; 22:5, s. 519-28
-
Journal article (peer-reviewed)abstract
- Preparations of human large granular lymphocytes (LGL), T cells, and monocytes (MC) were obtained through centrifugation on Percoll gradients and preparative E-rosetting. The different preparations contained more than 80% of the appropriate cell type, as judged by their ability to lyse 51Cr-labelled K562 cells, cell morphology, and the presence of cell surface structures recognized by the OKT3, OKT10, Leu 7 and OKM1 monoclonal antibodies. The protein synthesis is unstimulated and alpha interferon (IFN-alpha)-treated cells of the different types was studied by subjecting 35S-methionine-labelled cell extracts to two-dimensional gel electrophoresis. The general pattern of protein synthesis in LGL and T cells was virtually identical, whereas at least 7 major proteins were synthesized at a higher rate in monocytes. The effects of IFN-alpha on the protein synthesis of LGL and T cells were identical, IFN-alpha increasing the rate of synthesis of 9 proteins. These proteins were also expressed, but not always IFN-augmentable, in monocytes. No additional, cell-type associated, IFN-inducible proteins were found. This suggests that the augmenting effect of IFN-alpha on the cytotoxic capacity of LGL, T cells, and monocytes may be to affect common steps in their lytic machineries.
|
|
| 4. |
- Nilsson, B, et al.
(author)
-
An assessment of the extent of antigenic analogy between physiologically bound C3 and C3 denatured by sodium dodecyl sulphate.
- 1985
-
In: Scandinavian Journal of Immunology. - 0300-9475 .- 1365-3083. ; 22:6, s. 703-710
-
Journal article (peer-reviewed)abstract
- Three previously defined antigenic subsets of C3 (C3(S), C3(D) alpha and C3(D)beta) clearly distinguish native C3 from C3 that has been denatured in the presence of sodium dodecyl sulphate (C3-SDS): C3-SDS expresses antigens of all 3 subsets, while native C3 only expressed C3(S) antigens. The radioimmunometric assessment performed in this study revealed that 90% of the C3(S) and C3(D)alpha and 70% of the C3(D)beta antigens demonstrable in C3-SDS also was expressed by physiologically bound C3b on sheep erythrocytes. The antigenic properties of bound C3b were not shared by soluble C3b, which (like soluble C3) only expressed C3(S) antigens, nor did soluble C3b 'spontaneously' released from complement-treated target cells express antigens other than C3(S). We therefore conclude that the expression of C3(D) antigens, under physiological conditions of activation, reflects a conformational modification unique for bound C3b and occurring to an extent comparable to that of C3 in the presence of a strong denaturant. Additional studies further revealed that the antigenic profile of bound C3b is determined by a heterogeneous population of molecules differing in their relative expression of the C3(S), C3(D)alpha and C3(D)beta subsets.
|
|
| 5. |
- Nilsson, B, et al.
(author)
-
Antigens of complement factor C3 involved in the interactions with factors I and H.
- 1986
-
In: Scandinavian Journal of Immunology. - 0300-9475 .- 1365-3083. ; 23:3, s. 357-363
-
Journal article (peer-reviewed)abstract
- This study explores the relationship between defined antigens of the C3 molecule and those surface structures that are involved in interaction with factors I and H. Methylamine treatment at pH 11 followed by neutralization converts C3 into a modified state in which the molecule is optimally susceptible to cleavage by factor I in the presence of factor H. The modified C3 is characterized by an antigenic profile with expression of antigens of the C3(N), C3(S), and C3(D) subsets. These antigenic properties closely mirror those of physiologically bound C3b, suggesting that modification of antigenic expression upon denaturation of C3 reflects a regulatory mechanism for I and H function. Immunochemical studies of the alkaline-denatured C3 suggested that factor H interacts with surfaces of C3 that are situated within the C3c fragment and that are defined by C3(SN) antigens, while factor I predominantly interacts with C3(SN) antigens associated with the C3d fragment and with C3(D) antigens hidden in native C3. Therefore the continuing immunochemical study of this and related problems will require polyclonal and monoclonal antibody reagents reactive not only with the C3(S) and C3(N) but also the C3(D) antigenic subsets.
|
|
| 6. |
- Siegbahn, Agneta, et al.
(author)
-
The chemokinetic inhibitory factor derived from chronic lymphocytic leukaemia cells : Partial purification and characterization of a new lymphokine
- 1986
-
In: Scandinavian Journal of Immunology. - 0300-9475 .- 1365-3083. ; 23:1, s. 15-23
-
Journal article (peer-reviewed)abstract
- We have recently described a heat-labile and cell-directed neutrophil migration inhibitory activity that is present in serum from patients with chronic lymphocytic leukaemia (CLL). The inhibitory activity is produced and secreted by CLL cells in vitro. In the present study the inhibitory activity was partially purified from short-term cultures of monoclonal leukaemic B-CLL cells. On gel filtration the calculated molecular weight was apparently 30,000. By anion exchange chromatography, the inhibitory factor was recovered in the fractions that eluted with 0.3 mol/l NaCl. The active material applied to preparative agarose gel electrophoresis migrated towards the anode. The inhibitory factor was totally destroyed by trypsin. In addition it bound to concanavalin A-Sepharose. These properties indicate that the inhibitory factor is a glycoprotein. Antibodies against the isolated inhibitory factor were raised in rabbits. CLL serum was separated by means of gel filtration and the inhibitory activity was recovered in the pool with a molecular weight of approximately 30,000. The activity was completely neutralized by the antibodies raised against the CLL-cell-derived inhibitor, indicating the similarity between this and the serum-derived inhibitor. We have shown the existence of a new lymphokine, derived from B-CLL cells, in serum from patients with CLL.
|
|
| 7. |
- Strigård, Karin, et al.
(author)
-
Elimination of CD8+ T cells in vivo does not break induced immunospecific tolerance to experimental allergic neuritis in rats.
- 1988
-
In: Scandinavian Journal of Immunology. - 0300-9475 .- 1365-3083. ; 28:3, s. 325-330
-
Journal article (peer-reviewed)abstract
- The role of CD8+ T 'cytotoxic/suppressor' T cells in induced immunospecific tolerance and during recovery after actively induced disease was examined by means of elimination of CD8+ cells from Lewis rats using in vivo treatment by Ox8 monoclonal antibodies, in experimental allergic neuritis (EAN). Animals depleted of CD8+ T cells after recovery from EAN did not show any clinical signs of relapse. Other animals were pretreated with the peripheral nerve basic protein P2 and thereby rendered resistant to disease induction with a potentially neuritogenic emulsion. The elimination of CD8+ T cells did not result in EAN here either. Thus, the CD8+ T-cell population does not seem to participate in the suppression of this autoimmune disease under these experimental conditions.
|
|
| 8. |
- Widner, H, et al.
(author)
-
Immune response in deep cervical lymph nodes and spleen in the mouse after antigen deposition in different intracerebral sites
- 1988
-
In: Scandinavian Journal of Immunology. - 0300-9475. ; 28:5, s. 71-563
-
Journal article (peer-reviewed)abstract
- Brain interstitial and cerebrospinal fluid drainage into the lymphatics was studied by injections of 5 microliters of packed sheep red blood cells (SRBC) injected into the caudate nucleus, the occipital lobe, and the lateral ventricle of the brain in mice. The number of plaque-forming cells (PFC) was determined in the deep cervical lymph nodes, the axillary lymph nodes, and the spleen, and the number of PFC was compared with the response in the same tissues after intravenous immunization with 0.1 ml 10% SRBC. The weight of the deep cervical lymph nodes increased 3.0 times on day 3 after injection in the brain parenchyma compared with the weight of these nodes after intravenous immunization. The antigen-specific response peaked on day 5, 392 +/- 37 PFC/10(6) for IgG in the deep cervical lymph nodes after antigen deposition in the caudate nucleus, whereas only a minor peak in the antigen-specific response was obtained after intraventricular antigen deposition, 127 +/- 79 PFC x 10(6) for IgG on day 6. There were no increased PFC in any of the lymph nodes after intravenous immunization. The experiments show an antigen-specific response in the deep cervical lymph nodes after intracerebral antigen deposition, whereas antigens deposited in the lateral ventricles drain preferentially to the blood, with a high response in the spleen.
|
|
