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PubMed1978

Glucocorticoid induction of hepatic alpha2u-globulin synthesis and messenger RNA level in castrated male rats in vivo.

alpha2u-Globulin is a male rat liver protein of Mr = 20,000 which is synthesized in the liver of adult male rats, secreted into the serum, and excreted in the urine. Its function is unknown. The hepatic synthesis of this protein is under complex hormonal control. We had previously shown that castration of male rats diminishes hepatic alpha2u-globulin synthesis and the level of its mRNA, and that administration of androgen to these castrated animals results in the reinduction of the synthesis of this protein and the level of its mRNA. We now report that alpha2u-globulin synthesis and the level of its mRNA can be fully reinduced in castrated males by administration of glucocorticoid alone. This induction is much more rapid than the androgenic induction and is inhibited by the glucocorticoid antagonist progesterone. Administration of glucocorticoid to intact male animals does not induce alpha2u-globulin synthesis above normal levels; however, if alpha2u-globulin synthesis has been depressed in intact male rats by pretreatment with estrogen or cyproterone acetate, the level of this protein can be reinduced by administration of glucocorticoids. The implications for the control of alpha2u-globulin gene expression are discussed.

Animals↗
PubMed1976

Synergistic effect of immune gamma-globulin fraction on protection by antibiotic against corneal ulcers in experimental mice infected with Pseudomonas aeruginosa.

Synergistic effects of immune gamma-globulin fraction containing antibodies of OPE, protease and elastase of Pseudomonas aeruginosa on the activities of antibiotic, dibekacin (DKB), in the cornea of mice were examined for the purpose of studying therapy for corneal ulcers due to Pseudomonal infection. In the case of the intramuscular injection, a medium effective dose (ED50) of DKB alone against corneal ulcers caused by strain IID 1210 of P. aeruginosa in experimental mice was 620 mug per mouse. When 15.6 to 18.7 mg of gamma-globulin fraction was subcutaneously given to each mouse prior to the infection with strain IID 1210, opacity instead of severe ulcers was observed only in the central area of cornea. The immune gamma-globulin fraction was far more effective in the protection of cornea from the infection than the calf serum that showed no antibody titer against OEP, protease and elastase. The ED50 values of DKB's combined with the immune gamma-globulin, Fr. 1 and Fr. 2, and the calf serum were 34 and 73, and 480 mug per mouse respectively. There was found no statistical difference in ED50 value between DKB combined with the calf serum and one without it. There was, however, significant difference in ED50 value between DKB's combined with Fr. 1 and Fr. 2, and one with the calf serum. When DKB alone is dropped in the eye of mouse for the protection, the ED50 value was 15 mug per mouse. When 1.56 to 1.87 mg of the immune gamma-globulin fraction was dropped in the eye after the infection with P. aeruginosa, there was observed no protection against corneal ulcers. the ED50 values of DKB's combined with Fr. 1, Fr. 2 and the calf serum were 0.96, 0.94 and 13 mug per mouse, respectively. There was no significant difference between the ED50 values of 0.96 and 0.94 mug, and between 15 and 18 mug. There was, however, significant difference between the former ED50 values (0.96 and 0.94 mug) and the latter ones (15 and 18 mug). The combination of DKB and the immune gamma-globulin fraction was found to be superior to the combination of DKB and the calf serum in the therapeutic effect on corneal ulcers caused by strain IID 1210 of P. aeruginosa.

Abscess↗
PubMed1984

A study of the interaction between bromocresol green dye and bovine, ovine and equine serum globulins.

In human medicine it has been shown that the bromocresol green (BCG) dye-binding method for the determination of serum albumin is not entirely specific, the dye reacting also with certain human serum globulins. This causes over-estimation of albumin when reaction times are prolonged beyond 30 seconds. In the present study, serum albumin values obtained from three animal species by the "immediate", i.e. less than 30 seconds, BCG reaction were compared with those by the 10-minute BCG reaction. Albumin-depleted sera were prepared using an affinity chromatography technique and their reactions and those of purified gamma globulin preparations with the dye were studied. In cattle, sheep and horses, serum albumin values obtained by the 10-minute reaction were higher than those obtained by the "immediate" BCG reaction, the differences being statistically significant. Purified gamma globulin did not react with the BCG dye after 10 minutes, but other globulins did. There were differences between the species in the magnitude of the reaction of their globulins with BCG dye.

Animals↗
PubMed1977

The different electrophoretic forms of post gamma-globulin their antigenic identity and their structural variability.

Post gamma-globulin, first described as a constant component of protein of cerebrospinal fluid and urine from patients with tubular disorders has also been found in other biological fluids. Post gamma-globulin from a single individual always migrated as several bands after storage. Three electrophoretic forms, immunochemically identical, have been isolated by gel chromatography, preparative continuous flow electrophoresis and ion-exchange chromatography. Their molecular weight was found to be approximately between 11 000 to 12 000. No difference between the three forms could be detected. The N-terminal amino acids were found to be Lys, Arg and Leu respectively for the three forms of post gamma-globulin. The "slow" and "fast" forms of post gamma-globulin seemed to differ by elimination of small basic peptides or amino acids from the N-terminal end of the protein. No enzymatic activity of post gamma-globulin was found, but this requires further investigations.

Amino Acids↗
PubMed1962

The site of synthesis of the 19S gamma-globulins in dysgammaglobulinemia.

Lymph nodes and splenic tissue from patients with congenital agammaglobulinemia and dysgammaglobulinemia and from normal subjects were studied with the use of immunofluorescence and histochemical stains to determine the site of synthesis of the 19S gamma(1)-globulins. The two patients with dysgammaglobulinemia had high serum concentrations of the 19S gamma(1)-globulins and a marked deficit of the 7S gamma-globulins. These patients, as well as agammaglobulinemic children, had only rare or no plasma cells in their tissues. Cells were identified in sections of spleen from a dysgammaglobulinemic child as well as from normal individuals which exhibited specific fluorescence with an anti-19S gamma-globulin antiserum adsorbed with 7S gamma(2)-globulins and which stained positively with PAS and methyl green pyronine. These cells resembled the transitional cells described by Fagraeus.

Agammaglobulinemia↗
PubMed1964

PROTEIN-PROTEIN INTERACTIONS AMONG L POLYPEPTIDE CHAINS OF BENCE-JONES PROTEINS AND HUMAN GAMMA-GLOBULINS.

The L polypeptide chains of certain Bence-Jones proteins of group I have been found in three forms: monomers of molecular weight of about 20,000, dimers which monomerize in dissociating solvents, and dimers which are stable in such solvents. The L polypeptide chains of some Bence-Jones proteins of group II were found to occur naturally only as stable dimers. The L chains of normal human gamma-globulin have been obtained in a reduced unalkylated form, and a fraction of these chains was found to form stable dimers under oxidizing conditions. It is suggested that a single disulfide bond is involved in stabilization of the dimer. In experiments on the reconstitution of 7S gamma-globulin, it was found that stable dimers of L polypeptide chains did not associate appreciably with H(gamma) chains to form a soluble product. L chains in the monomeric form, both of a reduced alkylated Bence-Jones protein and of reduced unalkylated gamma-globulin, combined with H(gamma) chains to form a 7S product. After hydrolysis with papain, the 7S material containing the Bence-Jones L chains yielded fragments comparable to the fragments of papain-treated myeloma proteins. As indicated by spectrofluorometric measurements, dissociable dimers and stable dimers of the L chains of a Bence-Jones protein both underwent identical thermally induced transitions in the temperature range 48-58 degrees C. When L polypeptide chains were present in reduced alkylated gamma-globulin or reduced alkylated S fragments, no transition occurred until 65 degrees C, the coagulation temperature of gamma-globulin and S fragments. Above this temperature, L chains were released into solution. These experiments suggested that free L chains and L chains bound to H(gamma) chains have different conformational stabilities.

Bence Jones Protein↗
PubMed1965

METABOLISM AND FUNCTION OF GAMMA GLOBULIN IN ALEUTIAN DISEASE OF MINK.

Aleutian disease-affected mink, which are markedly hypergammaglobulinemic, show a decreased half-life of the serum gamma globulin indicating that the hyperglobulinemia is due to increased production. No evidence that the gamma globulin was antibody to the infectious agent, to autologous or isologous tissues, or to antigens the animal was responding to prior to development of the disease was obtained. The increased gamma globulin was found to be of the 6.4S variety, and gamma globulin containing protein-protein complexes of 9S to 17S and 22S to 25S classes were observed in serums of affected mink. The findings are most consistent with the Aleutian disease virus acting as a direct and somewhat selective stimulus to plasma cell proliferation. There is no evidence that the arterial and glomerular lesions of Aleutian disease have an immunologic pathogenesis. It seems possible that these vascular changes may be directly caused by the viral agent, or may be the result of the increased gamma globulin levels.

Aleutian Mink Disease↗
PubMed1954

Synthesis of all plasma protein fractions except gamma globulins by the liver; the use of zone electrophoresis and lysine-epsilon-C14 to define the plasma proteins synthesized by the isolated perfused liver.

Lysine-epsilon-C(14)-labeled plasma proteins produced by the normal rat and the isolated perfused rat liver have been fractionated by preparative zone electrophoresis. The isolated perfused liver incorporates lysine-epsilon-C(14) into the plasma albumin, alpha globulin, and beta globulin (including fibrinogen) fractions. No significant C(14) incorporation into the trichloracetic acid-precipitable proteins of the gamma globulin fraction was observed. Presumptive evidence indicates that the alpha globulins turn over more rapidly than any other major plasma protein fraction. The increased production of gamma globulins in liver disease is discussed.

Animals↗
PubMed1964

GAMMA GLOBULIN ANTIGENIC TYPES DEFINED BY HEAVY CHAIN DETERMINANTS.

Two populations of immunologically distinguishable 7S gamma globulins in normal human serum and two corresponding antigenic types of myeloma 7S gamma globulins have been detected with rabbit antiserums to proteins associated with pathological conditions, the differences being related to the H-chains of 7S gamma globulin. No relationship exists with type I and type II antigenic classification, determined by L-chains. Human serums with various hereditary gamma globulin (Gm) specificities contain both types of 7S gamma globulin.

Antigens↗
PubMed1978

Rapid changes in the serum total protein and globulin levels in complications caused by facultatively pathogenic Gram-negative bacteria.

The changes in the levels of total protein and four globulin fractions were followed up throughout the entire course of complications caused by Gram-negative facultative pathogens in 37 acute cases of respiratory insufficiency accompanying different underlying illnesses and in 9 chronic, bedridden patients given artificial ventilation. At the onset of the infectious complications, in the first place in septic shock, the levels of various globulin fractions showed a decrease corresponding to a half-life of 2 to 4 days. Neither the increased catabolism, nor the protein losses by the urine and tracheal secretions offer a sufficient explanation for the escape of globulins of this extent from the plasma. It seems that this is a consequence of the increase in capillary permeability due to the effect of antigen-antibody reactions and that of endotoxin. As a result, in the critical phase of the infectious complications, at the point of culmination, e.g. in septic shock, diminished amount of different globulins is transported to the site of utilization, that is, to the inflammatory area.

Adult↗
PubMed1997

Three subsets of genes whose tissue specific expression is sex and age-dependent can be identified within the rat alpha 2u-globulin family.

The rat alpha 2u-globulins are encoded by a multigene family whose 20-25 members are subjected to multihormonal regulation that is dependent upon the sex of the animal, the developmental stage and the tissue being examined. Using RT-PCR and diagnostic restriction analysis of the products, we have examined the specificity of the expression of different members of the gene family. All family members can be classified into three subsets, depending on how the amplified cDNA responds to digestion with ApaLI, SstI and VspI. Subset A contains the restriction sites for both ApaLI and SstI but not VspI and typifies the genes expressed in the salivary glands of both mature and juvenile animals of both sexes, where it is the only subset expressed. This subset of genes also accounts for all the transcripts observed in the kidneys and mammary glands of juvenile males. Although subset A was represented in the transcript populations of all the other tissues examined, its proportion relative to the total varied greatly. The two other subsets were subset V, which contains only the restriction site for VspI, and subset N, which lacks all three restriction sites. In all the other tissues examined, two or all three of the subsets were expressed, usually in a manner that was unique to the sex and age of the tissue in question. The proportion of each of the three alpha 2u-globulin subsets in the alpha 2u-globulin gene family was determined by quantitation of the restriction products of amplified genomic DNA. Interestingly, the most prevalent subset in the genome (N) has the most limited tissue expression pattern, but is found in liver and preputial glands, the tissues expressing the most substantial quantities of alpha 2u-globulin. These results indicate the complexity of the regulation of the alpha 2u-globulins and point to the necessity for gene specific analyses if the expression of the family is to be understood in molecular terms.

Age Factors↗
PubMed2002

Effect of succinylation on the functional and physicochemical properties of alpha-globulin, the major protein fraction from Sesamum indicum L.

alpha-Globulin the major protein fraction from Sesamum indicum was succinylated to different levels and the effect of the chemical modification was evaluated both on the functional and physicochemical properties. The results suggest that the pH of minimum solubility shifted to the more acidic side (pH approximately 4.5-5.5) for the succinylated alpha-globulin whereas for control alpha-globulin the pH of minimum solubility was 6.5. Succinylation also increased emulsion activity and emulsion stability of the protein. The emulsion stability increased from a control value of 53 +/- 3 s to a value of 122 +/- 5 s. Bulk density, water absorption capacity, oil absorption capacity, foam capacity and foam stability were evaluated in phosphate buffer (pH 7.0) containing 0.5 M sodium chloride and all these properties showed increased values as a result of succinylation. Ultracentrifugation studies showed that the % composition of 7S component increases with concomitant decrease in that of 11S fraction with the increase in percentage of succinylation. Further increase in succinylation resulted in only 2S component which is a dissociated form of 11S and/or 7S protein fractions. The fluorescence emission studies showed a decrease in the fluorescence emission intensity of alpha-globulin as a result of succinylation. The thermal stability of the protein molecule decreased due to progressive succinylation as indicated by decrease in the apparent thermal denaturation temperature from a control value of 84 to 62 degrees C at a succinylation level of 40%. These results suggest that succinylation improves the functional characteristics of alpha-globulin. Such changes in the functional properties have been attributed partly to the dissociation of the protein molecule at higher levels of succinylation and the increase in the net negative charge on the protein.

Alpha-Globulins↗
PubMed1990

Intravenous gamma globulin therapy in systemic juvenile rheumatoid arthritis.

Intravenous (IV) gamma globulin has been successfully used as replacement therapy for antibody-deficient patients and, more recently, in the treatment of autoimmune diseases such as idiopathic thrombocytopenic purpura, myasthenia gravis, and Kawasaki disease. In view of the successful treatment of these diseases, we initiated a pilot study of the effect of IV gamma globulin in systemic juvenile rheumatoid arthritis (JRA). Eight patients with active systemic JRA that was unresponsive to first-line agents, second-line agents, and/or corticosteroids received this therapy monthly for 6 months. Outcome measures included changes in articular and extraarticular features, steroid dosage, and laboratory parameters. Following IV gamma globulin therapy, there was significant improvement in arthritis and/or morning stiffness in 5 of 8 patients, while extraarticular features significantly improved in 7 of 8 patients. At study entry, 6 of 8 patients were receiving prednisone; at study end, prednisone was discontinued in 3 patients and decreased by more than 50% in the other 3. Overall, there was an 80% reduction in the prednisone dosage. Initially, all patients had anemia, low levels of serum albumin, and an elevated erythrocyte sedimentation rate, while a thrombocytosis was seen in 7 of 8 patients. Serum IgG was initially elevated in 6 patients. IV gamma globulin therapy resulted in a significant increase in hemoglobin and albumin levels and a significant decrease in the mean serum IgG level, platelet count, and erythrocyte sedimentation rate. In only 1 patient did IV gamma globulin fail to significantly improve the clinical or laboratory features of the disease. We suggest that this therapy may be beneficial in the treatment of systemic JRA.

Arthritis, Rheumatoid↗
PubMed1989

Alpha-globulins suppress human leukocyte tumor necrosis factor secretion.

The secretion of tumor necrosis factor (TNF) by human peripheral blood mononuclear cells was suppressed by either whole human plasma alpha-globulins or purified alpha 1-acid-glycoprotein, alpha 1-antitrypsin and alpha 2-macroglobulin in a concentration-dependent manner. alpha 1-Antitrypsin was found to be the most suppressive of the purified proteins tested and completely blocked TNF release at concentrations above 1.25 mg/ml. Both alpha 1-acid glycoprotein and alpha 1-antitrypsin blocked TNF secretion by leukocytes which were simultaneously stimulated with either recombinant human interferon-gamma (IFN-gamma) or lipopolysaccharide (LPS). IFN-gamma- and LPS-activated cells were also susceptible to suppression mediated by these two alpha-globulins and the inhibition produced by 5 mg/ml alpha 1-antitrypsin was greater than that caused by either 1 microM prostaglandin E2 or 10 ng/ml transforming growth factor-beta 1. The level of TNF mRNA in TNF-secreting and alpha-globulin-suppressed cells was examined and found to be equal in both groups. The suppressive effect of whole alpha-globulins was confined to the inhibition of TNF secretion and these plasma proteins had no effect on the cytolytic activity of the recombinant cytokine as measured on murine L-929 target cells. Thus the alpha-globulins, which are a major fraction of the circulating plasma proteins, may function in TNF homeostasis by controlling TNF secretion without inhibiting the biological activity of the released cytokine.

Adult↗
PubMedDate not supplied

Changes in serum alpha2u-globulin levels in castrated male rats treated with testosterone propionate in a Hershberger assay.

The Hershberger assay has been proposed as a candidate screening test method for the detection of androgenic and anti-androgenic chemicals and is being validated presently under the test guideline programme of the Organization for Economic Cooperation and Development (OECD). Rat alpha2u-globulin is male rat-specific protein appearing in their serum and urine, and the protein is known to be induced by androgens. We investigated the usefulness of measuring serum alpha2u-globulin levels as a parameter for the androgenic activity of chemicals tested in the Hershberger assay. The serum alpha2u-globulin level was measured after the administration of testosterone propionate at dosages of 0, 20, 100 or 500 microg kg(-1) day(-1) for ten consecutive days in the castrated male rats. The ventral prostate, balbocavernosus/levator ani muscles, glans penis and Cowper's gland were collected and weighed. Although all the androgen-responsive organ weights were increased significantly at dosages of 100 and 500 microg kg(-1) day(-1), the serum alpha2u-globulin level was increased significantly only at a dosage of 500 microg kg(-1) day(-1). These results show that the serum alpha2u-globulin level may be a useful biomarker for detecting androgenic activity caused by test chemicals, but it is less sensitive than the organ weights of androgen-responsive tissues in the Hershberger assay.

Alpha-Globulins↗
PubMed1982

Multihormonal induction of alpha 2u-globulin in an established rat hepatoma cell line.

A subclone of the FU5-5 rat hepatoma cell line has been isolated which is inducible more than several hundred fold for the 20,000 dalton form of the major rat urinary protein alpha 2u-globulin. The basal relative synthetic rate (RSR) in growth medium containing 10% fetal calf serum was less than 2 X 10(-6) of total protein synthesis. Both dexamethasone and insulin were necessary for induction, and yielded a maximum induced RSR of 4-8 X 10(-3). Triiodothyronine (T3), dihydrotestosterone (DHT), rat growth hormone (GH), and estrogen, all of which have been shown to influence the induction of alpha 2u-globulin in the intact rat, were without effect on the cell line. A factor present in fetal calf serum was also necessary for maximum induction, since dexamethasone plus insulin in serum-free medium raised the RSR to only 3 X 10(-5); exogenous T3, GH, and DHT could not substitute for this serum factor. The kinetics of induction by dexamethasone were slow, with a lag of approximately 48 hr followed by a period of increasing RSR for 6-20 days. Removal of dexamethasone from induced cells led to an exponential decline in the RSR (t 1/2 15 hr). The concentrations of dexamethasone and insulin that could yield half maximum induction were 5 X 10(-8)M and 3 X 10(-11)M, respectively. Higher concentrations of insulin, although still in physiological range (10(-9)M), inhibited induction. At yet higher insulin levels, beyond the physiological range, alpha 2u-globulin synthesis returned to maximum values. The lack of DHT, T3, and GH requirement for alpha 2u-globulin induction in this cell line may mean that a regulatory aberrancy has occurred in this transformed cell line, or, alternatively, that these hormones act indirectly in the intact animal. This cell line should prove useful for the study of the molecular events associated with alpha 2u-globulin induction and for genetic approaches to the problem of multihormonal regulation of gene expression.

Alpha-Globulins↗
PubMed1997

Binding of hexachlorobutadiene to alpha 2u-globulin and its role in nephrotoxicity in rats.

Hexachlorobutadiene (HCBD) is nephrotoxic in rats causing damage to the proximal tubules. Renal toxicity is presumed to be due to bioactivation by glutathione S-conjugate formation and further processing by the enzymes of the mercapturic acid pathway to reactive intermediates. Recent studies revealed major sex-dependent differences in the pattern of urinary metabolites and gave evidence for the excretion of unmetabolized HCBD in the urine of male, but not female, rats. The objective of this study was to investigate the basis for the excretion of unchanged HCBD in the urine. We administered [14C]-HCBD (200 mg/kg bw, po) to male and female Sprague-Dawley (SD) and NCI Black-Reiter rats (NBR), an alpha 2u-globulin-deficient strain. No major differences in the disposition and in the rates of excretion of [14C]-derived radioactivity were observed between animals of both strains. Previously observed sex-specific differences in the formation of urinary metabolites in Wistar rats were now confirmed in SD rats and were also found in NBR rats. In contrast to male SD rats, however, NBR rats did not excrete unmetabolized HCBD with urine. [14C]-HCBD (10% of total urinary metabolites) was only present in the urine of male SD rats. Anion-exchange HPLC showed radioactivity associated with the alpha 2u-globulin fraction in urine and renal cytosol of male SD rats; the radioactive compound was identified as HCBD bound to the protein. The results indicate that the male-specific urinary excretion of HCBD is associated with its binding to alpha 2u-globulin. Light microscopic examination revealed the formation of hyaline droplets indicative of the accumulation of alpha 2u-globulin in the kidney of male SD rats after staining with Lee's methylene blue basic fuchsin. H&E staining additionally confirmed the finding of more pronounced necrotic changes in renal tubules of male SD rats than in females as previously described for Wistar rats. Binding of HCBD to alpha 2u-globulin may contribute to the pronounced nephrotoxicity in male rats.

Alpha-Globulins↗
PubMed1985

Rat alpha 2u-globulin mRNA expression in the preputial gland.

Rat alpha 2u-globulin and the mouse major urinary proteins (MUP) are encoded by homologous multigene families whose members exhibit diverse tissue-specific, developmental, and hormonal controls of expression. Although their patterns of expression and hormonal control appear to be very similar in many respects, we have found high levels of alpha 2u-globulin mRNA in rat preputial glands, whereas MUP mRNA could not be detected in the male mouse preputial gland. Male and female rat preputial have similar concentrations of alpha 2u-globulin mRNA, suggesting an absence of endocrine regulation as occurs in the liver and lachrymal glands. Two-dimensional polyacrylamide gel electrophoresis of proteins encoded by hybrid-selected alpha 2u-globulin mRNA indicates that the liver and lachrymal translation products have different mobilities. However, many of the preputial gland products comigrate with most or all of the liver and lachrymal products. Among the possibilities suggested by these results is that alpha 2u-globulin genes expressed in liver and lachrymal glands under endocrine control are also expressed constitutively in the preputial gland.

Alpha-Globulins↗