Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0393754 (HSA)
2,996 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Autoimmune hyperlipidemia (AIH) may be induced a variety of antibodies which inhibit different stages of the lipolytic process by which the lipid load is removed from the circulating lipoproteins. In a patient having a monoclonal gammopathy and a nephrotic syndrome with a glomerulonephritis and a marked hypertriglyceridemia, it was found previously that the monoclonal IgG gamma Lac. reacted with human VLDL as well as with human serum albumin. Here it is demonstrated that the purified IgG gamma inhibits the lipolysis of triglyceride substrates by reacting with a substance (Lac. S) necessary for lipoprotein lipase activity. The interaction of IgG lambda Lac. with serum or HDL-activated triglyceride substrates inhibits the lipolytic activity of human and rat plasma post heparin and also adipose tissue lipases. It slightly inhibits the activity of swine pancreatic lipases. The Lac S. which reacts with IgG Lac. is associated to whole and delipidated VLDL and HDL and not to LDL or purified APo-A. It may be an Apo-C or a non-peptidic co-factor of the lipases which remains bound to the apoprotein core after delipidation. Its lack of species specificity and its presence as traces in HSA preparations favors the latter hypothesis. The Lac. substances is different from the Pg and As substances which were found to react with IgA anti-Pg and IgG anti-As antibodies in previously reported antilipoprotein AIH.
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PMID:Inhibition of lipoprotein lipase activity by a monoclonal immunoglobulin in autoimmune hyperlipidemia. 83 49

The effect of protein antigens on the locomotion of lymphocytes from the lymph nodes draining the site of antigenic challenge in immunized mice, and from the same nodes in control mice, was studied in filters using a checkerboard assay in which the absolute concentration and the concentration gradient of attractant was varied in a series of chambers. Serum albumin (HSA or BSA) was chemokinetic for unimmunized lymphocytes inasmuch as the distance migrated into filters by cells in its presence varied with the absolute concentration of albumin, but not with the concentration gradient, indicating an influence of the serum albumin on the rate but not on the direction of locomotion. Ovalbumin and nonalbumin proteins did not show this effect. Using the same assay, the migration of primed lymphocytes in the presence of the priming antigen was shown to be influenced by the antigen gradient in a way that suggested a positive chemotactic response of the lymphocytes to antigen. This response was only shown clearly when the cells were in a chemokinetic medium containing serum albumin.
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PMID:Antigen-induced locomotor responses in lymphocytes. 85 98

Studies were undertaken to determine whether BSA immobilized in collodion membranes adherent to activated charcoal particles, would be capable of specifically removing circulating BSA antibody in vitro and in vivo in an extracorporeal system in dogs. Up to 59-8 mg of BSA were retained in collodion membranes adherent to small particles. In vitro studies demonstrated that immobilized BSA could specifically reduce BSA binding activity from circulating antisera. For in vivo studies, an extracorporeal circulation system was established and arterial blood was circualted through a continuous flow celltrifuge in which plasma was separated from formed elements of the blood. Only plasma was circulated over the BSA collodion-charcoal immunoadsorbent. Anti-BSA and anti-HSA atibodies were passively infused into dogs and, after an equlibration period of 12 or 15 min, plasma was passed over the BSA collodion-charcoal immunoadsorben. Plasma exhibited a sharp reduction in BSA binding over the next 30-60 min with only slight reduction in anti-HSA binding the same period. Dogs, actively immunized to BSA and HSA, were also treated by extracorporeal plasma perfusion over BSA collodion-charcoal. A specific decline in BSA binding of sera, was again observed with minimal changes in HSA binding. A post-perfusion rebound of BSA binding was observed which reached pre-perfusion levels after 6-8 days. A second treatment during the rebound period also resulted in a specific decline in BSA binding with a similar pattern of antibody rebound. There were no significant changes in I-labelled BSA recorded on the charcoal before and after in vivo procedures and no signifcant alterations in haematocrit, serum sodium, potassium, calcium, magnesium or creatinine levels before and after the procedures. These data suggests that antigen-coated charcoal may specifically withdraw circulating antibodies in vivo with minimal release of the entrapped antigen and little alteration in the host's haematological and biochemical status.
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PMID:Specific removal of antibody by extracorporeal circulation over antigen immobilized in collodion-charcoal. 86 46

Drug induced immunosuppression of chicken immune response was studied in F1 hybrids of the CB and IC inbred lines. In tuberculin reaction complete inhibition of wattle swelling was induced by the administration of methotrexate, colcemid (1 mg/KBW), and 6-mercaptopurine. The cellular infiltration was substantially reduced in these cases. Cyclophosphamide and colcemid (0.1 mg/KBW) reduced partially the wattle swelling but had no apparent effect on the cellular infiltration. Acetinomycin D did not affect in measurable degree the wattle swelling. The histologic picture was in this case the same as in the control animals. The same drug administration schedule had less pronounced effect on anti-HSA antibody production. No anti-HSA antibody was found after the 500 mg/animal doses of 6-mercaptopurine. Significant reduction of anti-HSA titres was found after 50 mg/animal doses of 6-mercaptopurine, colcemid (1 mg/KBW), 25 MG/KBW or cyclophosphamide and after the methotrexate treatment.
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PMID:Activity of various immunosuppressive drugs on tuberculin hypersensitivity reaction in chickens. 89 78

Cyclic precordial variations of radiation after i.v. administration of 15 mCi 99mTc-HSA correspond to cyclic volume changes of ventricular volumes of the heart. The "gated blood pool procedure" yields reliable data. Extensive analysis of these data results in subsequent information concerning left ventricular myocardial behaviour: 1. extent of the regional myocardial contraction 2. homogeneity of the contraction 3. regional contraction velocity 4. regional relaxation velocity. Four parametric scans present the distribution of each one of those parameters within the heart. Gated blood pool data have been compared with angiographic data. Reliability of those parameters obtained by extensive analysis of the gated blood pool data could be proven.
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PMID:[Regional myocardial motility as evaluated by analysis of "gated blood pool" data (author's transl)]. 91 63

Partial suppression of antibody formation in neonatally induced tolerance to HSA as observed during immunization at 6 weeks of age or at a later time, is caused mainly by a rapid escape from tolerance. The following findings support this view: 1. After immunization at 4 weeks of age with a larger dose of HSA, which elicits detectable circulating antibody formation in all control birds, anti-HSA antibodies cannot be demonstrated in a large majority of tolerant chickens. 2. Surgical bursectomy performed in tolerant birds on the day of hatching or 7 or 11 days after hatching increases considerably the degree of suppression of anti-HSA antibody formation and slows down the return of reactivity to HSA. These findings suggest that new immunocompetent cells originating in the bursa are responsible for escape from tolerance in this experimental system. The existence of suppressor cells in birds tolerant to HSA was not demonstrated by the transfers of spleen cell mixtures from immune and tolerant donors to young, irradiated recipients.
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PMID:Attempts to characterize cellular mechanisms of immunologic tolerance to HSA in chickens. 92 58

The formation of homocytotropic antibodies (IgE) as determined by immunochemical characteristics against penicilloyl in rabbits was shown. The production of such antibodies to azidocilloyl-human serum albumin (AzO10-HSA) in alum was found optimal using 1 mg of antigen in the tested range of 0.01-8 mg. At the lowest dose (0.01 mg) only haemagglutinating but no IgE antibodies were formed. Immunization with azidocilloyl-bovine gamma-globulin (AzO9-BGG) resulted in a slower increase in antibody levels than was caused by AzO10-HSA. Univalent benzylpenicilloyl-epsilon-aminocaproate or ampicillin given together with the antigen upon immunization decreased the levels of penicllloyl specific IgE and haemagglutinating antibodies, but induced the formation of IgE antibodies against the carrier molecule. Further, the administration of penicilloyl specific IgG antibodies diminished formation of both IgE and haemagglutinating antibodies, but no antibodies specific for the carrier were formed. The usefulness of this animal model for the experimental study of penicillin allergy is discussed.
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PMID:Formation of homocytotropic antibodies with penicilloyl specificity in the rabbit. 94 64

To give an overview of the kinds of issues expected to be encountered by the new Health Systems Agencies being established in conformity with Public Law 93-641, the authors draw from the experiences of the Comprehensive Health Planning agency and Regional Medical Program of an Upstate New York area. Problems faced together in the years 1972 to 1975 in health planning, development, review, and public policy are described. The unusual geographic and working relationship of these agencies makes them, together, a useful prototype of the HSA to examine.
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PMID:Difficult issues in health planning, development, and review. 96 41

Rabbits were injected with one dose of 2-4 mg. isolated nuclear DNA (from spleens of adult donors) at 3-5 days of age and their antibody response to a later administered soluble HSA antigen was followed. A) Rabbits receiving antigen only at 9 days of age, without previous DNA, did not form antibodies even after the second dose of HSA antigen given at 8 weeks of age. Nor were antibodies detected in the serum of rabbits treated before antigen, i.e., at 4-5 days of age, with DNA-N (from spleens of non-immunized rabbits), or DNA-P (from spleens of the pig immunized with a different antigen). Only rabbits treated with DNA-Ia (from spleens of rabbits immunized with soluble HSA antigen) formed antibodies to HSA antigen given at 9 days after birth. Antibodies were detectable in the serum at 21 days after antigen administration and retained increased levels as long as 50 days after the first dose of antigen. B) When HSA antigen was injected at 17-18 days after birth, even the DNA-N (4 mg.) given at 3-5 days after birth increased the antibody response in the recipients. Substantial acceleration and increase in antibody formation was obtained in rabbits treated with DNA-Ib after birth as compared to control rabbits (after antigen only with DNA). On the contrary, DNA-H from spleens of rabbits intensively immunized with HSA in adjuvant, given in a larger dose (4 mg.), suppressed the antibody response of rabbits over 8 weeks of age after the second dose of antigen. DNAs from spleens of immunized donors injected into rabbit offspring, without subsequent HSA antigen administration, did not lead to the appearance of detectable anti-HSA antibodies in the serum of young rabbits under the conditions of our experiments A and B. Long-term effects of DNAs injected in the postnatal period into rabbits on their immune response are discussed.
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PMID:Enhancement of antibody response to soluble HSA antigen of young rabbits pretreated with deoxyribonucleic acids from adult donors. 96 8

Spleen cell DNA from 6-month-old rabbits, that has received the first dose of soluble HSA antigen at 9 days of age and the second at 2 months of age and did not form antibodies incorporated 3H-thymidine in vitro as early as 1 hour after restimulation of rabbits with HSA antigen in vivo. The incorporation rate (in muCi/mg.) of isolated cellular DNA was higher than that of DNA from rabbits that had been pretreated with nuclear DNA from the spleens of adult non-immunized rabbits or from the spleens of pigs immunized with a different antigen (DNP-BGG), 4-5 days before the first dose of antigen. The inhibitory effect of pig DNA was stronger. Decreased incorporation of DNA was noted at 8 hours after restimulation of rabbits treated in the same manner as the previous group. The difference between the incorporation rate at 1 hour and at 8 hours after the restimulation was most marked in the DNA obtained from rabbits not treated with nuclear DNA in the postnatal period. The activity of lymphoid cell DNA after antigenic stimulation is discussed.
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PMID:Decreased in vitro incorporation of 3H-thymidine into spleen cell DNA of antigenically stimulated rabbits treated in the postnatal period with nucleic acid from adult donors. 96 9


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