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At least 19 recordsLinked to original sources
PubMed1992

Differences in alpha 2u-globulins increased in male rat kidneys following treatment with several alpha 2u-globulin accumulating agents: cystein protease(s) play(s) an important role in production of kidney-type-alpha 2u-globulin.

Effects of alpha 2u-globulin accumulating agents on alpha 2u-globulins in rat kidneys were examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting analysis. Treatment of male animals with decalin (150 mg/kg), 2,2,4-trimethylpentane (50 mg/kg), isophorone (150 mg/kg), d-limonene (150 mg/kg) or 1,4-dichlorobenzene (150 mg/kg) by gavage for 14 consecutive days in each case resulted in a marked intensification of a protein band corresponding to kidney-type-alpha 2u-globulin, with a molecular mass calculated to be approximately 16 kDa. However, intraperitoneal treatment with leupeptin and E-64 (two times 0.07 mmol/kg, for each), well known cystein protease inhibitors, while only slightly increasing this kidney-type-alpha 2u-globulin band, caused the intensification of a approximately 19-kDa molecular mass protein band which was revealed to be a native-type-alpha 2u-globulin by SDS-PAGE and immunoblotting. These results indicated that at least two types of alpha 2u-globulin can be increased in male rat kidney by chemical treatment. Moreover, cystein protease(s) appear(s) to play an important role in the degradation of alpha 2u-globulin and particularly in the conversion of native-type-alpha 2u-globulin to kidney-type-alpha 2u-globulin in rat kidneys.

Alpha-Globulins↗
PubMed1990

Elevation of serum thyroxine-binding globulin (but not of cortisol-binding globulin and sex hormone-binding globulin) associated with the progression of human immunodeficiency virus infection.

PURPOSE: In order to assess the relation of thyroid function tests to human immunodeficiency virus (HIV) infection, we determined the levels of serum thyroid hormones, serum binding proteins [thyroxine-binding globulin (TBG), cortisol-binding globulin (CBG), and sex hormone-binding globulin (SHBG)], and serum tumor necrosis factor (TNF) in HIV-seropositive subjects at different clinical stages. PATIENTS AND METHODS: Thirty-seven HIV-seropositive patients were studied: 7 at stage II, 13 at stage III, and 17 at stage IV (eight ambulatory and nine hospitalized) according to the Centers for Disease Control's criteria. RESULTS: As compared with stage II and stage III patients, stage IV patients had significantly higher mean TBG and total thyroxine (TT4) values, similar and normal total triiodothyronine (TT3) levels, and similar and abnormally low reverse triiodothyronine (rT3) concentrations. However, stage IV hospitalized patients had significantly lower TT3 values than stage IV ambulatory patients. In contrast to TBG, mean levels of CBG and SHBG were comparable in the three groups and within normal limits. For the whole population of HIV patients, there was a highly significant correlation between the CD4 lymphocyte count and TBG (r = -0.529, p less than 0.001) but not with CBG and SHBG levels. Finally, TNF values higher than 10 pg/mL were detected in six of the 17 stage IV patients and in only one of the 13 stage III patients (p = 0.059); elevated TNF levels correlated with a lower CD4 count (p less than 0.01) but not with serum TBG levels. CONCLUSION: The progression of HIV infection is associated with an elevation of serum TNF and TBG, but not of CBG or SHBG. HIV-infected patients have an unexpectedly normal TT3-low rT3 state.

Acquired Immunodeficiency Syndrome↗
PubMed1991

Sex hormone binding globulin, cortisol binding globulin, thyroxine binding globulin, ceruloplasmin: changes in treatment with two oral contraceptives low in oestrogen.

It is generally assumed that the oral contraceptives cause the carrier proteins to change. Notoriously this effect is used to evaluate indirectly their estrogenicity/gestagenicity ratio. In order to assess the residual intrinsic androgenic activity of two new 19-nor-derivative components, Desogestrel (DG) 150 micrograms and Gestodene (GD) 75 micrograms, both in association with Ethinylestradiol (EE) 30 micrograms, Sex Hormone Binding Globulin, Thyroxine Binding Globulin, Ceruloplasmin and Free Androgen Index (FAI), were studied in 40 young normally cycling healthy volunteers, matched for body mass index and age. The participants were randomly assigned to either EE-DG or EE-GD treatment. A marked significant increase in all the carrier proteins was found. Conversely, the values for FAI decreased significantly. The changes in the two groups were substantially of the same magnitude. These results are an indirect confirmation of the well-known negligible receptor binding affinity of the two progestogen in vitro, also supporting for these compounds the lack of relevant androgenic effects.

Carrier Proteins↗
PubMed1977

Development of an intravenous gamma-globulin with Fc activities. II. Reconversion of S-sulfonated human gamma-globulin into the original gamma-globulin.

The reconversion of S-sulfonated antitetanus gamma-globulin (S-GG) into the original gamma-globulin was studied. S-sulfonate groups in S-GG could be converted into disulfide bonds in vitro. The conversion restored the greater part of both complement-fixing and skin-sensitizing activities. S-GG administered intravenously formed interchain disulfide bonds again in vivo, which was accompanied by restoration of the C-dependent passive hemolytic activity. Intravenous injection of S-GG did not cause a significant decrease in serum complement level.

Biotransformation↗
PubMed1970

Immunologic responses of graft recipients to antilymphocyte globulin: effect of prior treatment with aggregate-free gamma globulin.

The immunologic response of graft recipients to antilymphocyte globulin has been studied. The clearance from the serum of (125)I-labeled antilymphocyte globulin was studied in 15 graft recipients previously treated with antilymphocyte globulin and in 4 control patients not previously treated with antilymphocyte globulin. The mean serum half-life of antilymphocyte globulin was 7.2 days in control patients, 3.8 days in 13 renal graft recipients, and 22 hr in 2 heart graft recipients. All but one of the antilymphocyte globulin-treated patients had rapid clearance. Patients treated with equine antilymphocyte globulin had rapid clearance of rabbit and goat antilymphocyte globulin as well as horse antilymphocyte globulin. All patients with rapid clearance of antilymphocyte globulin had circulating antibodies to xenogeneic gamma globulin. Two patients with rapid clearance of antilymphocyte globulin had circulating complexes of antilymphocyte globulin. Five renal graft recipients were treated with aggregate-free equine gamma globulin before antilymphocyte globulin therapy in an attempt to induce tolerance to xenogeneic gamma globulin. In these five patients neither rapid clearance of antilymphocyte globulin nor significant titers of circulating antibody to xenogeneic gamma globulin developed. The induction of tolerance to xenogenic gamma globulin may benefit patients treated with antilymphocyte globulin.

Animals↗
PubMed1963

Antigenic relationships of Bence Jones proteins, myeloma globulins, and normal human gama-globulin.

By means of immunodiffusion and immunoelectrophoresis study has been made of antigenic relationships of Bence Jones proteins, and the three classes of normal and pathological immunoglobulins, 7S gamma, beta(2A), and beta(2M). All thirty-nine Bence Jones proteins studied could be classified into either one of two distinct antigenic types, A or B. Both types are related to the immunoelectrophoretically slow (S) fragment of a papain digest of normal gamma-globulin; B is related more closely than A, but neither has antigenic determinants in common with the fast (F) fragment. The 7S gamma myeloma globulins were either immunological type I or II. The papain digests of these proteins produced the S and F precipitin lines in immunoelectrophoresis but multiple bands in starch gel electrophoresis, especially in the F region. The S fraction of type I myeloma globulins is antigenically similar to Bence Jones protein of type B, and the S component of type II myeloma globulins has antigenic determinants in common with type A Bence Jones protein. Correspondingly, myeloma patients with type I globulins and proteinuria usually excrete type B Bence Jones proteins, whereas patients with type II excrete type A proteins. The F fragment is the part common to normal 7S gamma-globulin and types I and II myeloma globulins but is absent in beta(2A) and beta(2M) pathological globulins and in both types of Bence Jones proteins. Papain digests of beta(2A) myeloma globulins produced a single precipitin line in immunoelectrophoresis. beta(2A) myeloma globulins appeared to have two antigenic units, one in common with type B Bence Jones protein and normal gamma-globulin, and another specific to beta(2A). The beta(2A) myeloma patients excreted type B Bence Jones protein. The papain digest of a macroglobulin produced two precipitin lines, the faster of which had antigenic determinants in common with type B Bence Jones protein, the slower seemed specific for the macroglobulin. Five serum micromolecular globulins proved to be either type A or B Bence Jones proteins. From the above results, an antigenic map was constructed showing which determinants are shared and which are specific for normal 7S gamma-globulin, types I and II myeloma globulins, beta(2A) myeloma globulins, a macroglobulin, and types A and B Bence Jones proteins.

Aged↗
PubMed1964

EVIDENCE FOR SPECIES' DIFFERENCES IN THE EFFECT OF SERUM GAMMA-GLOBULIN CONCENTRATION ON GAMMA-GLOBULIN CATABOLISM.

The fractional rates of catabolism of isotopically labeled mouse, human, bovine, and guinea pig gamma-globulins and human serum albumin were determined in mice and in guinea pigs whose serum gamma-globulin and serum albumin levels were elevated by immunization or by injections of exogenous serum proteins. These serum proteins were also followed in mice with different serum gamma-globulin levels due to different bacterial environments. The fractional rates of catabolism of the labeled gamma-globulins from all species tested were markedly increased in mice with elevated gamma-globulins due to immunization; to injections of human, mouse, guinea pig, or rabbit gamma-globulins; to exposure to supra normal numbers of bacteria in the environment. Injections of bovine gamma-globulin were only partially effective, and injections of human serum albumin had no effect. The gamma-globulin catabolic rates were decreased in mice with subnormal serum gamma-globulin levels (germfree mice). The catabolic rate of human serum albumin was essentially the same in all mice in spite of differences in serum gamma-globulin levels. In contrast, elevation of the serum gamma-globulin levels by injections of exogenous gamma-globulins or by hyperimmunization with keyhole limpet hemocyanin produced no change in the fractional catabolic rates of the isotopically labeled gamma-globulins and labeled albumin in guinea pigs. Thus, a feedback mechanism for the control of the serum gamma-globulin concentration appears to be operative in the mouse, but not in the guinea pig. Guinea pigs immunized with antigens in complete Freund's adjuvant or a saline suspension of killed E. coli had an increase in the catabolic rates of all labeled proteins tested including human serum albumin. Evidence is presented that the mechanism of this increase in catabolism is not the same as that seen in mice with elevated serum gamma-globulin levels.

Animals↗
PubMed1972

Anti-gamma globulins and chronic infection: comparative studies of the immune response to various bacteria and gamma globulin preparations.

A study of the relationship of clinical states associated with prolonged infection (bacterial endocarditis and osteomyelitis) and generation of serum anti-gamma globulins was made with particular reference to quantitative amounts of staphylococcal protein A in various infecting strains. No correlation between individual strain amounts of protein A and presence of anti-gamma globulins was detected. Thirty-eight rabbits were immunized intravenously with various strains of bacteria (Staphylococcus aureus, enterococci, Streptomyces viridans, pneumococci, pseudomonas, and Escherichia coli) for periods of 6 weeks, and antibacterial as well as anti-gamma globulin antibodies were assayed. No single group or strain of bacteria stood out as being more prone to produce anti-gamma globulins than others tested. Most rabbits developed anti-gamma globulins reacting with human gamma globulins, whereas the specificity for rabbit gamma globulin appeared more restricted. In 16 rabbits immunized with eight different strains of S. aureus, quantitative elevation of serum gamma globulin above 2.5 g per 100 ml often seemed to be correlated with presence of detectable serum anti-gamma globulins. By contrast 15 rabbits immunized with autologous or isologous rabbit gamma globulins in many instances developed extremely high titers of anti-gamma globulins showing primary specificity for human rather than rabbit gamma globulin. These studies further amplify the remarkably heterogeneous anti-gamma globulin reactivity associated with various types of immune response.

Animals↗
PubMed1976

[Prophylaxis and therapy with gamma globulin. General characterization and clinical use of gamma globulin preparations].

For accurate evaluation of the usefulness of gamma-globulin treatment, the clinical indications for passive immune prophylaxis and immunotherapy and the specific characteristics of commercially available gamma-globulin preparations have to be considered. Detailed investigations of currently used gamma-globulin preparations have shown that as yet no ideal product is available. Classical standard gamma-globulin and, in particular, enzymatically treated (Gamma-Venin, Veinoglobuline) or chemically modified preparations (Gamma-Globulin i.v. SRK, Intraglobin) for intravenous use have some deficiencies and involve potential risks for the patient. Nor is the infusion of "fresh frozen plasma" a safe and generally applicable alternative to the use of gamma-globulin concentrates. Thus from the outset the preconditions for effective treatment with gamma-globulin are not optimal. Standard and hyperimmune preparations, given once intramuscularly, are suitable for the prophylaxis of viral and bacteriotoxic diseases. In patients apt to react abnormally it is important to distinguish clearly between the few accepted indications and those that are more doubtful. Anti-D immunoglobulin is essential for the prevention of Rhesus sensitization after the delivery of a Rhesus-positive child. In general, gamma-globulin is recommended for substitution therapy and for the prophylaxis of recurrent acute bacterial infections in patients suffering from transient, congenital and acquired antibody-deficiency states. In such cases, high doses of an intravenously administrable preparation with a relatively long biologic half-life are recommended. The evidence for the effectiveness of gamma-globulin treatment of bacterial infections in patients without manifest disturbance of humoral immunity is equivocal. This is true, for example, of the oft-recommended combined use of antibiotics and high doses of intravenous gamma-globulin which is said to provide optimum antibacterial and antitoxic protection. There is even less chance of obtaining beneficial effects if gamma-globulin is given as an "ultimo ratio" in severe generalized bacterial infections resistant to antibiotic treatment. Localized and predominantly chronic infections are barely influenced by gamma-globulin. It is still too early to make a final assessment regarding the place and value of immunoglobulin concentrates for prophylactic and therapeutic purposes. This will only be possible if a preparation becomes available which contains all immunoglobulins in a biologically optimum state and concentration, is well tolerated and can be given in adequate doses both intramuscularly and intravenously.

Complement System Proteins↗
PubMed1990

Lysosomal degradation of alpha 2u-globulin and alpha 2u-globulin-xenobiotic conjugates.

A diverse group of chemicals cause a male rat-specific nephrotoxicity in which alpha 2u-globulin accumulates in renal lysosomes. It has been suggested that these chemicals bind to the protein and decrease its degradation by lysosomal proteinases. To test this hypothesis, the lysosomal degradation of native alpha 2u-globulin and that to which d-limonene, d-limonene-1,2-oxide, isophorone, 1,4-dichlorobenzene, and 2,5-dichlorophenol were bound was studied. alpha 2u-Globulin was purified from male rat urine, and male rat renal cortical lysosomes, isolated by differential centrifugation, served as the proteolytic enzyme source. Pepstatin, an inhibitor of aspartic acid proteinases, and leupeptin, an inhibitor of cysteine proteinases, reduced alpha 2u-globulin degradation to 28 +/- 8 and 17 +/- 5% of control, respectively, whereas addition of both inhibitors decreased alpha 2u-globulin degradation to 8 +/- 1% of control values. These results indicate that both classes of endopeptidases are important in the degradation of alpha 2u-globulin. Under the incubation conditions used, 30% of native alpha 2u-globulin was degraded in a 4-hr period. Conjugates of the protein were made for in vitro binding experiments. Binding of d-limonene and 1,4-dichlorobenzene to alpha 2u-globulin did not alter the degradation of the protein, whereas binding of d-limonene-1,2-oxide, 2.5-dichlorophenol, and isophorone decreased alpha 2u-globulin degradation by 33%. These results indicate that not all chemicals which have been shown to bind in vivo to alpha 2u-globulin alter the in vitro lysosomal degradation of the protein. However, in all cases, one metabolite of each hyaline droplet inducer did alter degradation of alpha 2u-globulin, suggesting that a decrease in lysosomal degradation is involved in the accumulation of this protein in male rat kidney lysosomes.

Alpha-Globulins↗