Anti-neuronal antibody in Sydenham's chorea.
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Acute Disease↗
Biomedical subjects
G Husby
Publications and source records attributed to G Husby.
[Genetic aspects of amyloidosis].
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Amyloid↗
Direct immunochemical detection of prostaglandin-E and cyclic nucleotides in human malignant tumors.
Immunofluorescent localization of prostaglandin-E (PGE), cyclic AMP (CAMP), and cyclic GMP (cGMP) was studied in tumor tissues from 40 patients with a variety of solid tumors. Representative normal tissues served as controls. Rabbit antisera specific for PGE or the cyclic nucleotides were used, and the reactions observed were correlated with the degree and type of lymphocytic reaction at the tumor margins. Strong PGE immunofluorescence was detected in tumor cells in 27 of 42 malignancies; by contrast nine of 13 normal tissues showed weak PGE reactions, cAMP was detected in 30 of the 42 malignancies; cGMP was noted in only seven of the 42 malignant tissues and in none of the normal tissues studied. The most common malignant tumor profile (17/42) was that of positive PGE and cAMP and negative cGMP staining. Tumors showing strong staining with anti-PGE or cAMP demonstrated a distinct trend towards heavier lymphocytic infiltration with a predominance of T cells at their margins, although this association did not reach statistical significance in the present material.
B-Lymphocytes↗
Immunohistochemical localization of prostaglandin E in rheumatoid synovial tissues.
Synovial tissues removed at synovectomy from patients with active rheumatoid arthritis (RA) or osteoarthritis (OA) were examined for prostaglandin E (PGE) by immunohistochemical techniques using rabbit antisera specific for PGE. Marked increments of PGE were noted in RA synovia in comparison to OA, with staining concentrated in synovial lining cells, interstitial inflammatory cells, and endothelial cells of blood vessels. A correlation was noted between the degree of synovial lymphocytic infiltrate and the intensity of PGE staining. These studies provide initial cellular localization of PGE in such tissues.
Arthritis, Rheumatoid↗
Identification and characterization of different amyloid fibril proteins in tissue sections.
Antisera specific for 4 different classes of amyloid fibril proteins, amyloid protein AA and the immunoglobulin light-chain amyloid proteins AlambdaI, AlambdaIV, and AlambdaV, were used to identify these proteins directly in tissue sections from 25 patients with amyloidosis. The specificity of these reactions was established by blocking experiments with purified amyloid fibril proteins and Bence Jones proteins of known variable subgroups. Protein AA was detected in 17 patients, including all 13 with secondary amyloidosis, 2 with primary amyloidosis and 2 with Waldenström's macroglobulinemia. Immunoglobulin light-chain proteins AlambdaI, AlambdaIV, and AlambdaV were in 3, 1, and 2 patients, respectively, all of whom had primary or myeloma/macroglobulinemia-associated amyloidosis. Antiserum specific for the amyloid-related serum protein SAA reacted with the same tissues as anti-AA and had the same pattern of staining in tissue sections.
Amyloid↗
Identification in human placentae of antigenic activity related to the amyloid serum protein SAA.
Antigenic activity related to the amyloid serum protein SAA was observed in indirect immunofluorescence studies on human placental tissue. Positive staining with anti-SAA antisera was localized to the cytoplasm of cells scattered within the mesenchymal stroma, thought to be fibroblasts, and to foetal stem vessel endothelium and some individual fibrillar structures in villous stroma and perivascular tissue. This immunofluorescent staining was specifically inhibited by protein SAA. In contrast, no immunofluorescent staining was achieved using antisera to the amyloid protein AA. Absorption and immunodiffusion studies have further suggested that anti-SAA antisera may recognize in human placentae only a very limited number of the antigenic determinants present in protein SAA but not in the smaller protein AA. The results support previous observations that protein SAA-like antigenic material can be found in normal human tissue.
Amyloid↗
Occurrence of amyloid-related serum proteins in patients with benign monoclonal gammopathy.
The serum protein SAA, which is related to the amyloid fibril protein AA, was detected by double immunodiffusion using anti-protein AA antiserum. The SAA level was elevated in 16 to 32 patients with benign monoclonal gammopathy (BMG). In addition, two BMG sera reacted with an antiserum to amyloid fibril protein of immunoglobulin light-chain type, V lambdaI (EF), and one reacted with antiamyloid protein VlambdaV (AR). The reactivity of the BMG sera with antisera to the various amyloid fibril proteins was strikingly similar to that of 35 sera from patients with myelomatosis. In the age group of 50--70 years the proportion of SAA-positive sera in BMG (53%) and myelomatosis (56%) was strikingly higher than that of the normal controls (5%). In older subjects (70--90 years), however, the frequency of SAA in BMG or myelomatosis, although increased (53%--54%), was not significantly greater than that of a control group of apparently healthy individuals (44%).
Amyloid↗
Structural similarities between a protein extracted from normal human tissues and a component of amyloid fibrils.
Comparative immunologic and chemical studies of crude or fractionated amyloid fibrils and materials obtained from corresponding normal tissues have been performed. Materials from the amyloidotic and normal tissues were subjected to identical methods of extraction, chemical treatment and protein fractionation. Antigenic similarities between crude amyloid fibrils and corresponding normal tissue extracts were observed, however, a considerably larger concentration of the latter antigens was needed to obtain immunologic reactivity in double diffusion in gel. Striking similarities were observed when the amino acid composition of a high molecular weight subcomponent of amyloid fibrils was compared with that of normal tissue extracts. Crude, intact amyloid fibrils were highly effective in absorbing Congo-red while the ability to absorb Congo-red was by far less if the high molecular weight subcomponent of amyloid fibrils as well as the corresponding normal tissue extracts were used. The high molecular weight subcomponent of amyloid, which seems to be an integral part of the amyloid fibrils, most probably is a protein derived from normal tissue.
Adult↗
Immunoglobulin class of antilymphocyte antibodies in systemic lupus erythematosus patients and their families.
Antilymphocyte antibody (ALA) in systemic lupus erythematosus (SLE) was studied using an indirect immunofluorescent technique with air-dried, acetone-fixed lymphocytes. Ninety-four per cent of patients with SLE and 65 per cent of their relatives had ALA. The ALA response in SLE patients involved antibodies of all classes. However, the ALA in their relatives was primarily of the IgM class. Restriction of the class of ALA in asymptomatic relatives is analogous to that seen with anti-RNA antibodies and suggests that the switch to production of autoantibodies of the IgG class may be important in the pathogenesis of SLE.
Antibodies↗
Antibodies to human caudate nucleus neurons in Huntington's chorea.
Antibodies reacting with neuronal cytoplasmic antigens present in normal human caudate and subthalamic nuclei were detected in 37 of 80 probands afflicted with Huntington's disease (HD). IgG antibodies were detected by immunofluorescence using frozen sections of unfixed normal human and rat brain. Specificity of IgG binding was confirmed using pepsin F(ab')2 fragments of IgG isolated from positive sera. In vitro complement fixation of IgG antibody was detected in 22 of 31 sera tested. Neuronal cytoplasmic antigens reacting with positive HD sera were diminished after trypsin or RNAase treatment of tissue sections but were not removed by DNAase, neuraminidase, EDTA, or dithiothreitol treatment. Antibody staining of neurons could be removed after absorption with isolated caudate nucleus neurons or by using perchloroacetic acid extracts of caudate nucleus. Prevalence of antibody reacting with neuronal cytoplasm was 3% in 60 normal controls and 6% among a wide variety of patients with diverse neurological disorders. However, one-third of 33 patients with Parkinson's disease showed presence of antineuronal antibody. Among patients with HD, a significant association was noted between duration of clinical disease greater than 7 yr and titers of antibody of 1:2 or greater (P less than 0.001). When 115 family members of HD probands were tested, 30% of unaffected spouses showed presence of antineuronal antibody. 23.2% of first-degree relatives at risk for developing HD was also positive (P less than 0.001). 10.5% of second-degree relatives showed presence of antineuronal antibody. These data may support an environmental or infectious factor somehow involved in the ultimate expression of HD.
Adult↗
Serum immunoglobulins and organ non-specific antibodies in diseases of the liver.
Serum immunoglobulins and C3 levels, auto-antibodies to smooth muscle (SMA), mitochondria (MA), and nuclei (ANA), rheumatoid factors (RF), HB-antigen and HB-antibody were studied in 9 groups of liver disease. Hypergammaglobulinaemia was a prominent feature in most groups, IgG being particularly raised in active chronic hepatitis, IgM in primary biliary cirrhosis, and IgA in alcoholic liver disease, respectively. IgE was often increased in alcoholic liver disease and was frequently low in hepatic tumours, whereas IgD showed no typical pattern in any liver disorder. SMA was most frequently found in active chronic hepatitis (68%), and MA in primary biliary cirrhosis (58%), while ANA was detected in 50% of the patients with active chronic hepatitis. However, a pronounced over-lap of tissue antibodies was observed among the various groups of liver disease, particularly in active chronic hepatitis and primary biliary cirrhosis. The concurrent presence of SMA and ANA was most frequent in active chronic hepatitis. It was not excluded that antibody titres might have provided better diagnostic discrimination, since titration of antibodies was not performed. Low C3 levels in active chronic hepatitis were correlated with low levels of other liver-synthetized proteins, and no evidence was found of increased consumption by immunologic reactions.
Acute Disease↗
Detection of antilymphocyte antibodies in patients with systemic lupus erythematosus by indirect immunofluorescence on acetone-fixed lymphocytes.
Antilymphocyte antibodies in normal and SLE sera were found to react with lymphocytes fixed in acetone at -30 degrees C. for 10 minutes. At a dilution of 1:40, 3.7 per cent of normal and 90.9 per cent of SLE sera were positive with the use of indirect immunofluorescence with a pepsin-digested, FITC-labeled anti-Fab serum. The reaction was independent of temperature between 4 degrees and 37 degrees C. Three patterns of staining were seen in the lymphocyte surface: reticular, ring, and globular. The ring pattern appeared to correlate with IgM, and the reticular and globular patterns with IgG antilymphocyte antibodies. Absorption with lymphocytes, insolubilized extracts of rat liver and kidney, and human brain revealed that antilymphocyte and ANA activity could be independently removed. Variation in reactivity with cells from different normal donors was similar to that seen with the microcytotoxicity test. Acetone-fixed lymphocytes appear to be a much more sensitive target than viable cells in suspencion in IIF tests for antilymphocyte antibodies. The IIF test with fixed cells also appears slightly more sensitive than cytotoxicity testing and has the advantage of allowing storage of target cells.
Antibodies, Antinuclear↗
Amyloid-related serum protein SAA from three animal species: comparison with human SAA.
The amyloid-relates serum protein SAA has been isolated by gel filtration in 10% formic acid from three animal species: mink, mouse, rabbit. Sera used in the isolation procedure were obtained from animals in which high concentrations of SAA had been induced by treatment with LPS. The isolated SAA proteins had a subunit size similar to that of human SAA, with m.w. values ranging from 10,000 to 11,700 (estimated by gel filtration in 6 M guanidine-HC1) or 12,400 to 15,000 (estimated by SDS-PAGE). The m.w. studies and amino acid sequence data indicated that SAA and the amyloid fibril protein AA in the mouse, and probably also the mink, are related in the same way as in man, the two proteins having common NH2-terminal amino acid sequences and SAA being extended by 20 to 40 residues at the COOH-terminal end of the molecule.
Alpha-Globulins↗
Antibodies reacting with cytoplasm of subthalamic and caudate nuclei neurons in chorea and acute rheumatic fever.
46% of sera from 30 children with rheumatic chorea showed IgG antibody reacting with neuronal cytoplasm of human caudate and subthalamic nuclei. The antibody was also detected in 14% of 50 children with active rheumatic carditis. 55 normal control sera, as well as 148 sera from a broad variety of other disease states showed a low prevalence (1.8-4.0%) of positive reactions. In rheumatic chorea the presence of anti-neuronal antibody appeared to correlate with severity and duration of clinical attacks. Antibody reacting with neuronal cytoplasm was completely removed by absorption with Group A streptococcal membranes or with isolated human neurons from caudate nucleus. Partial absorption of antibody was also recorded using Group A cell wall preparations but not with Group A carbohydrate. No absorption of positive reactions was seen with streptococcal Group D membranes or cell walls. In rheumatic chorea, anti-neuronal antibody appeared to represent cross-reaction with antigens shared by Group A streptococcal membranes.
Acute Disease↗
The complete amino acid sequence of an amyloid fibril protein AA1 of unusual size (64 residues).
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Adult↗
Amyloid-related serum protein SAA in endotoxin-induced amyloidosis of the mink.
The concentration of the amyloid AA-related serum protein (SAA) was markedly increased after endotoxin injections in mink, mouse, rabbit, and man. It was particularly studied during the development of endotoxin-induced amyloidosis of the mink. Protein SAA was markedly elevated in all mink 24 h after the first endotoxin injection but had fallen to relatively low levels before the onset of amyloidosis at about 4 wk. These results are consistent with SAA being a circulating precursor of the amyloid fibril protein, AA. However, both proteins may be derived by proteolysis from a common precursor.
Amyloid↗
Coexistence of protein AA and immunoglobulin light-chain fragments in amyloid fibrils.
Coexistence of amyloid fibril protein AA and homogeneous immunoglobulin light-chain fragments was found in the isolated amyloid fibrils of two patients with amyloidosis secondary to rheumatoid arthritis. The light-chain amyloid fibril protein showed antigenic identity with a light-chain amyloid from a patient with primary amyloidosis, which was identified as the VlambdaIV subgroup by amino acid sequence analysis. In the amyloid fibrils isolated from another patient with primary amyloidosis there was a mixture of VlambdaIV and VlambdaV homogeneous immunoglobulin light chains. Thus, a mixture of protein AA had lambda light chains or two different types of homogeneous light chains may be found in the amyloid fibrils of some patients.
Amino Acid Sequence↗
Amyloid-related serum protein (SAA) in patients with inherited amyloidosis and certain viral conditions.
Amyloid-related serum protein (SAA) was studied with a double immunodiffusion method. Only 2 of 21 patients with inherited systemic amyloidosis and lattice corneal dystrophy had elevated SAA levels in their sera. Several pseudoexfoliation patients had elevated levels of SAA, but it was not possible to differentiate an age-related elevation of SAA from that associated with this disease. In addition, SAA was found in the sera of many groups of patients with acute viral infections, including 10 of 11 patients with measles and 7 of 11 persons vaccinated against rubella. Elevation of SAA protein appeared in the serum before the 6th day after the vaccination, had its peak value between days 6 and 12, but was absent already on the 20th day. In this relation the SAA protein appears to behave as an acute-phase reactant.
Adult↗