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PubMed1992

Alpha 2u-globulin is the only member of the lipocalin protein superfamily that binds to hyaline droplet inducing agents.

The rate-limiting step in chemically induced, male rat-specific hyaline droplet nephropathy is the reversible binding of a xenobiotic to alpha 2u-globulin. In this study, equilibrium saturation binding experiments were conducted to evaluate the in vitro binding of d-limonene-1,2-oxide (dLO) and 2,4,4-trimethyl-2-pentanol (TMP-OH) to alpha 2u-globulin and members of the alpha 2u-globulin protein superfamily. Both dLO and TMP-OH bound to alpha 2u-globulin, with Scatchard analysis yielding dissociation constants of 5.6 and 6.4 x 10(-7) M, respectively. The Bmax for binding (nmol bound/mg protein) was 50.7 and 61.1 for dLO and TMP-OH, respectively, yielding a molar ratio of approximately 1 for both ligands. The ability of dLO and TMP-OH to bind to human-derived alpha 1-acid glycoprotein, rat-derived retinol-binding protein, human protein-1, and bovine beta-lactoglobulin was also studied. These superfamily proteins are generally abundant in plasma, are freely filtered across the glomerulus, and can bind a wide range of ligands. However, neither dLO nor TMP-OH bound to any of the superfamily proteins. In contrast, under identical experimental conditions, alpha 1-acid glycoprotein did bind progesterone (Kd = 10(-6) M), whereas both beta-lactoglobulin and retinol-binding protein bound retinol (Kd = 10(-8) M for both proteins). These results indicate that, under conditions where alpha 2u-globulin superfamily proteins bind to established ligands, the proteins do not interact with hyaline droplet inducing agents. Thus, the interaction between male rat-specific nephrotoxicants and alpha 2u-globulin is unique to this protein. More importantly, these results provide direct evidence that the presence of the alpha 2u-globulin superfamily proteins does not predispose humans to develop hyaline droplet nephropathy and renal cancer from this class of chemicals.

Alpha-Globulins↗

PubMed1988

Changes in transcriptional activity and matrix association of alpha 2u-globulin gene family in the rat liver during maturation and aging.

Hepatic synthesis of alpha 2u-globulin in the male rat begins at puberty (about 40 days), reaches a peak level at about 80 days, and ceases at about 750-800 days of age. The age-dependent changes in alpha 2u-globulin synthesis are correlated with both the steady-state level of the hepatic mRNA for this protein and the rate of transcription of the alpha 2u-globulin gene family. Transcriptional activation of the alpha 2u-globulin gene family at puberty and cessation of transcription at senescence correlate with the association and dissociation of this gene domain with the nuclear matrix. Unlike the alpha 2u-globulin gene, the albumin gene in the liver shows preferential association with the nuclear matrix throughout the life. From these results we conclude that the age-dependent changes in alpha 2u-globulin synthesis are due to the alteration in the rate of transcription of the alpha 2u-globulin gene, and that the association of this gene domain to the nuclear matrix is a prerequisite to its transcriptional activation.

Aging↗

PubMed1990

Increased hyaline droplet formation in male rats exposed to decalin is dependent on the presence of alpha 2u-globulin.

A peculiar decalin-induced male rat nephropathy associated with the altered renal handling of filtered protein appears limited to the accumulation of the protein, alpha 2u-globulin. Several strains of male rats that produce alpha 2u-globulin (Fischer-344, Sprague-Dawley, Buffalo, and Norway Brown) demonstrate spontaneous renal cortical hyaline droplets which are exacerbated after exposure to decalin. In all cases, a close correlation exists between hyaline droplet formation observed histologically and alpha 2u-globulin accumulation measured biochemically. In stark contrast, the NCI-Black-Reiter strain, which does not produce measurable quantities of alpha 2u-globulin, neither forms hyaline droplets nor accumulates any filtered protein in its kidney cortex either spontaneously or after exposure to decalin. Also, female rats injected ip with male rat alpha 2u-globulin exhibit increased hyaline droplet formation and alpha 2u-globulin accumulation when treated with decalin. These data provide evidence that the presence of alpha 2u-globulin is key in understanding why this nephropathy appears unique to the male rat.

Alpha-Globulins↗

PubMed1986

Alpha 2U-globulin: measurement in rat kidney following administration of 2,2,4-trimethylpentane.

Hyaline droplet formation was stimulated markedly in the kidneys of post-puberty male rats 24-48 h after a single oral dose of 12/24 mmol/kg 2,2,4-trimethylpentane [TMP]. Renal hyaline droplet formation could not be detected in female rats or in pre-puberty male rats following similar doses of TMP. A dose-dependent increase in the renal concentration of the androgen-dependent low molecular weight protein, alpha 2U-globulin was observed in post-puberty male rats 24 h after a single oral dose of TMP, over the range 0.3-12.0 mmol/kg. After administration of a single dose of 12 mmol/kg TMP to male rats, the renal concentration of alpha 2U-globulin rose steadily up to a peak after 48 h and then returned slowly to near normal after 7 days. Renal alpha 2U-globulin could not be detected in female rats and in pre-puberty male rats. An immunocytochemical assay was developed to examine the distribution of alpha 2U-globulin within the kidney. alpha 2U-Globulin was localised primarily in the S2 segment of renal proximal tubules in untreated male rats. Rats which received a single dose of 12 mmol TMP/kg showed not only a greater staining intensity, due to the presence of a higher concentration of alpha 2U-globulin, but also staining in adjacent segments of the renal cortex. Several urinary biochemical indicators of nephrotoxicity were measured daily in male rats for up to 72 h following a single dose of 12 mmol TMP/kg. Renal proximal tubular function was unimpaired by TMP treatment. On the basis of studies in untreated and TMP-treated rats, a strong association has been found between the presence of renal hyaline droplets and the occurrence of renal alpha 2U-globulin. The findings in the present study provide an explanation for the occurrence of renal hyaline droplets only in adult male rats, but do not, as yet, establish the toxicological significance of increases in renal hyaline droplet formation.

Alpha-Globulins↗

PubMed1996

Sequence requirements for secondary glucocorticoid inducibility of rat alpha 2u globulin genes.

The transcription of the rat alpha 2u globulin gene family is under complex hormonal control, involving the participation of glucocorticoids, estrogens, insulin, and growth hormone. The glucocorticoid induction of alpha 2u globulin is a secondary response; that is, ongoing protein synthesis is necessary for induction of alpha 2u globulin mRNA by the hormone. This secondary response is maintained when alpha 2u globulin genes are transfected into tissue culture cells which contain the glucocorticoid receptor. We have found that the glucocorticoid induction of alpha 2u globulin occurs only in permanent cell lines, in which the alpha 2u globulin genes are integrated into the host cell DNA; induction in transient transfections is minimal. Further, the DNA sequences required for alpha 2u globulin secondary response lie entirely in the 5' proximal promoter region; no intragenic sequence elements are required for, or participate in, the secondary response to glucocorticoids.

Alpha-Globulins↗

PubMed1988

Prevention of giant coronary artery aneurysms in Kawasaki disease by intravenous gamma globulin therapy.

Previous studies have demonstrated the efficacy of intravenous gamma globulin in the prevention of coronary artery abnormalities in Kawasaki disease. We retrospectively reviewed our single-hospital experience with patients in whom Kawasaki disease was diagnosed from January 1979 to July 1987. Only 3 of 68 (4%) patients treated with intravenous gamma globulin in the first 10 days of illness developed coronary artery abnormalities (one of the three had abnormalities before gamma globulin therapy), in comparison with 39 of 119 (33%) patients not treated with gamma globulin (p less than 0.001). Giant coronary artery aneurysms, which are associated with the greatest morbidity and mortality rates in Kawasaki disease, developed in none of the 68 patients treated with gamma globulin but in 7 of 119 patients (6%) not treated with gamma globulin (p = 0.04). Intravenous gamma globulin appears to be effective not only in reducing the overall prevalence of coronary artery abnormalities in Kawasaki disease but, more important, in preventing the formation of giant aneurysms, the most serious form of coronary abnormality after this illness.

Child, Preschool↗

PubMed2005

11S and 7S globulins of coconut (Cocos nucifera L.): purification and characterization.

Total globulins extracted with 0.4 M NaCl in buffer from coconut endosperm separated into two peaks on gel filtration: peak I corresponding to 11S globulin or cocosin and peak II to 7S globulin with native molecular weights of 326 000 and 156 000, respectively. The percent composition of total globulins was estimated to be 11S, 86% and 7S, 14%. On SDS-PAGE, cocosin resolved into two closely migrating bands at approximately 34 000 (acidic polypeptide) and another set of 2 bands at 24 000 (basic polypeptide). Each set consisted of one darkly stained band and one lightly stained band. The 7S globulin consisted of three bands of 16 000, 22 000, and 24 000. Three isoforms of cocosin were identified after anion exchange chromatography. Cocosin, but not the 7S, was found to have disulfide bonds. Using periodic acid-Schiff's reagent, all of the bands of cocosin on SDS-PAGE were positive for carbohydrate. However, when con A-peroxidase was used, only the basic polypeptide stained positively for carbohydrate. For the 7S globulin, no carbohydrate group was detected using the PAS and con A-peroxidase tests. The 7S globulin was easily extracted with 0.10-0.15 M NaCl, whereas cocosin was extracted with 0.35 M NaCl. The N-terminal amino acid sequences of the 34 k band and 24 k band of cocosin were SVRSVNEFRXE and GLEETQ, respectively, and that of the 7S was EQEDPELQK.

Amino Acid Sequence↗

PubMed1997

Globulin and albumin proteins in dehulled seeds of three Phaseolus vulgaris cultivars.

Albumin and globulin fractions, obtained after modifications of the Osborne's fractionation scheme, were investigated in the seeds of three cultivars of Phaseolus vulgaris, after removal of the seed coats, to prevent interactions of tannins and phenols with the globulins. Also, by using an appropriate buffer to separate the globulins more efficiently, no cross-contaminations were observed in SDS-PAGE between these two fractions. The combination of these two procedures resulted in globulin to albumin ratios 70% higher than those published previously with the same cultivars. Amino acid compositions of total globulin, phaseolin and albumin fractions are presented. Whereas the albumins contained much more cysteine than the globulins, the concentrations of methionine were evenly distributed in these two fractions. Also, the bulk of methionine was found in phaseolin; cysteine was found in non-phaseolin proteins. In addition, the globulins contained unexpectedly high amounts of lysine.

Albumins↗

PubMed1986

The treatment of Kawasaki syndrome with intravenous gamma globulin.

We compared the efficacy of intravenous gamma globulin plus aspirin with that of aspirin alone in reducing the frequency of coronary-artery abnormalities in children with acute Kawasaki syndrome in a multicenter, randomized trial. Children randomly assigned to the gamma globulin group received intravenous gamma globulin, 400 mg per kilogram of body weight per day, for four consecutive days; both treatment groups received aspirin, 100 mg per kilogram per day, through the 14th day of illness, then 3 to 5 mg per kilogram per day. Two-dimensional echocardiograms were interpreted blindly and independently by two or more readers. Two weeks after enrollment, coronary-artery abnormalities were present in 18 of 78 children (23 percent) in the aspirin group, as compared with 6 of 75 (8 percent) in the gamma globulin group (P = 0.01). Seven weeks after enrollment, abnormalities were present in 14 of 79 children (18 percent) in the aspirin group and in 3 of 79 (4 percent) in the gamma globulin group (P = 0.005). No child had serious adverse effects from receiving gamma globulin. We conclude that high-dose intravenous gamma globulin is safe and effective in reducing the prevalence of coronary-artery abnormalities when administered early in the course of Kawasaki syndrome.

Aneurysm↗

PubMed1979

Cycloheximide inhibition of hormonal induction of alpha 2u-globulin mRNA.

The induction of hepatic alpha 2u-globulin synthesis by glucocorticoids in isolated hepatocytes occurs via an increase in the level of its mRNA as measured by cell-free translation and by hydbridization to an alpha 2u-globulin cDNA probe. To explore whether induction of this mRNA is a direct or an indirect consequence of the interaction of the dexamethasone-receptor complex with the alpha 2u-globulin genome, the requirement for ongoing protein synthesis was examined. Concentrations of cycloheximide too low to prevent precursor incorporation into total poly(A)-containing RNA do prevent the hormonal induction of alpha 2u-globulin mRNA. Furthermore, incorporation of 3H-labeled amino acids into total protein was decreased by only 40-50%, and the appearance of the dexamethasone-induced glycosylated forms of alpha 2u-globulin was completely prevented in these cycloheximide-treated hepatocytes. The results suggest that the synthesis of a protein mediator(s) may be required for the induction of alpha 2u-globulin mRNA by glucocorticoids and that the steroid-receptor complex may not interact directly with the alpha 2u-globulin genome.

Alpha-Globulins↗

PubMed1983

alpha 2u-Globulin is present in the rat anterior pituitary.

The possibility that the pituitary gland may contain as yet undiscovered regulatory factors is intriguing. Recent reports have suggested the presence, in the anterior pituitary, or a number of proteins of extrapituitary origin. alpha 2u-Globulin, a rat serum and urinary protein, previously shown to be synthesized in the submaxillary gland and in the liver under anterior pituitary control, has now been localized by immunocytochemistry in the cytoplasm of some cells of the anterior pituitary. No alpha 2u-globulin could be detected in either the intermediate or posterior pituitary. The presence of alpha 2u-globulin was confirmed and quantitated by radioimmunoassay. Using RNA blot analysis and cloned alpha 2u-globulin cDNA probes, we could not detect alpha 2u-globulin mRNA sequences in pituitary RNA, indicating that alpha 2u-globulin is not synthesized therein. The presence of alpha 2u-globulin, presumably of circulatory origin, in certain anterior pituitary cells suggests that it may play a role in anterior pituitary function.

Aging↗

PubMed1973

Cross-idiotypic specificity among monoclonal IgM proteins with anti- -globulin activity.

Through the use of absorbed idiotypic antisera prepared against single isolated monoclonal IgM anti-gamma-globulins, partial cross-idiotypic specificity was demonstrated with other IgM anti-gamma-globulins. Such antisera classified these proteins into at least three groups. The major group which included 60% of the anti-gamma-globulins was particularly homogeneous. The anti-gamma-globulin specific antigens were detected best in hemagglutination and hemagglutination inhibition systems. They were not found in monoclonal IgM proteins that lacked anti-gamma-globulin activity although related antigens were detected at low concentrations in pooled immunoglobulin preparations as well as in heterogeneous anti-Rh antibodies. Several lines of evidence were obtained indicating that the antibody combining site was involved in the specific determinants. Attempts were made to analyze the fine specificity of each anti-gamma-globulin for the Fc fragment of different subclasses of human immunoglobulins as well as those of other species. Differences were observed but these were not readily related to the cross-specificity antigens. The anti-gamma-globulin specific antigens were very analogous to those previously described for monoclonal IgM cold agglutinins. Although each protein could be distinguished from all the others on the basis of individual idiotypic antigens, the antigens common to the specific groups of proteins with each of these activities were prominent and readily detected with multiple antisera. The results indicate basic similarities between proteins of a given activity even in unrelated individuals.

Agglutinins↗

PubMed1975

Efficacy of modified human immune serum globulin in the treatment of experimental murine infections with seven immunotypes of Pseudomonas aeruginosa.

Modified immune serum globulin, prepared from human immune serum globulin by a nonenzymatic method, is apparently safe for intravenous administration to humans. The efficacy of the preparation was determined in experimental murine infections with seven immunotypes of Pseudomonas aeruginosa. Intravenously administered 0.85 percent NaCl, 0.3 m glycine, and 10 percent human albumin did not protect against lethal pseudomonas infection, whereas modified immune serum globulin given by the same route did protect mice. In the mouse protection test, the mean dose of the preparation that saved 50 percent of mice infected with any of eight strains of P. aeruginosa was 480 mg/kg (range, 12-2,333 mg/kg). For five strains the 50 percent effective dose was smaller than 200 mg/kg. There was no correlation between the efficacy of modified immune serum globulin in the mouse protection test and titers of antibody, as determined by bacterial agglutination. Therapy of pseudomonas infection in mice with modified immune serum globulin was followed by a prompt and persistent decrease in the numbers of intraperitoneal bacteria. This finding is consistent with the interpretation that modified immune serum globulin acts primarily as an opsonin and not as an antitoxin. Modified immune serum globulin may prove to be useful in the treatment of human infections.

Agglutination Tests↗

PubMed1998

Nutritional utilization by rats of chickpea (Cicer arietinum) meal and its isolated globulin proteins is poorer than that of defatted soybean or lactalbumin.

The effects on performance, digestibility, N utilization and plasma amino acid concentrations of dietary chickpea (Cicer arietinum, var. Kabuli) seed meal, globulin proteins or buffer-insoluble residue [starch + non-starch polysaccharides (NSP) + lignin] were studied in growing rats. Chickpea meal, defatted soybean meal, chickpea globulins and lactalbumin were each incorporated into diets as the sole source of dietary protein (100 g/kg). In addition, chickpea insoluble residue was included in a control diet in the same proportion found in the chickpea meal. Rats were killed while under halothane anesthesia after 10 d of consuming the diets, and ileal contents were washed out and freeze-dried for digestibility measurements. Weight gains and gain:feed ratios of rats fed chickpea diets for 10 d did not differ from those of rats fed defatted soybean but were significantly lower than those of rats given the control (lactalbumin) diet. However, ileal and fecal N digestibilities and N retention by rats fed the chickpea diet were significantly lower than those obtained with the lactalbumin or soybean diet. The inclusion of both chickpea meal or its globulin proteins in the diet significantly increased the amount of N excreted, primarily as urea, through the urine. However, although ileal N digestibility values for chickpea meal were significantly lower, those for its constituent globulins did not differ from control values. Urea levels in plasma in rats fed diets containing chickpea meal, globulins or soybean meal were significantly higher than in those fed lactalbumin. Furthermore, the concentrations of glycine, phenylalanine, histidine, arginine and ornithine in the plasma of rats fed chickpea meal, its globulins or defatted soybean were significantly higher, whereas those of threonine, leucine, lysine and tryptophan were significantly lower than lactalbumin-fed controls. The chickpea insoluble residue had no adverse effects on performance or N utilization by rats. We conclude that the low nutritional value of chickpea meal is likely to be due mainly to adverse effects of its globulin proteins on growth and N metabolism rather than to the action of any known antinutritional factor present in the diet.

Amino Acids↗

PubMed2001

Intravenous Rh immune globulin for treating immune thrombocytopenic purpura.

Intravenous Rh [corrected] immune globulin was licensed by the U. S. Food and Drug administration in 1995 for the treatment of acute and chronic immune thrombocytopenic purpura in children and chronic immune thrombocytopenic purpura in adults. In 1996, the American Society of Hematology published a practice guideline for immune thrombocytopenic purpura, but treatment recommendations of necessity were formulated using only results of early clinical trials with intravenous Rh immune globulin. To date, there are no published results of large-scale clinical trials comparing conventional doses of intravenous immune globulin with the most promising dose range for intravenous Rh immune globulin (50-75 microg/kg). However, clinical experience is accumulating to indicate that intravenous Rh immune globulin is as effective, probably safer, and easier to administer than intravenous immune globulin. Acute intravascular hemolysis after infusions of intravenous Rh immune globulin for immune thrombocytopenic purpura has been reported with an estimated incidence of 1 in 1,115 patients. The risk factors for this adverse event have not been defined.

Adult↗

PubMed1981

Storage proteins in Zea mays (L.): interrelationship of albumins, globulins and zeins in the opaque-2 mutation.

Mature endosperms from opaque-2 mutant seeds with various genetic backgrounds (B 37, W 64A, R 802A and Oh 43) contained twice as much globulin than the corresponding normals, reduced amounts of zein and an increased amount of albumin. The latter is caused by a diminished disappearance of albumins in mutant endosperms during the final phases of development as compared to normal endosperms. Albumins from the opaque-2 endosperms appeared on gel electrophoresis as a similar but heterogenous polypeptide population comparable to that of normal endosperms except that in all opaque-2 forms a 70-kDa polypeptide was increased. Similarly, one to three specific globulin polypeptides (47 kDa, 52 kDa and 58 kDa) were, depending on the genotype, increased in the mutant lines. The accumulation of albumins, globulins and zeins, studied in developing W 64A opaque-2 mutant and corresponding normal maize kernels from 10 days after pollination until maturity, demonstrated two-phasic accumulation patterns for all proteins in the mutant, the first phase extending to about 30 days post pollination and the second one from there on until maturity. The transition time-point from first to second phase was characterized in mutant endosperm by a sudden reduction in accumulating albumins (also seen in normal endosperm), by an enhanced accumulation of globulins and the cessation of further accumulation of zein. Preferential accumulation of certain globulins has been found in the mutant during the second phase of globulin formation. The increased accumulation of globulins in the opaque-2 mutant endosperm is considered a response to the arrest in zein synthesis.

Albumins↗

PubMed1966

In vitro absorption of gamma-globulin by neonatal intestinal epithelium of the pig.

1. An in vitro method, using fluorescent gamma-globulin and everted neonatal pig's intestinal slices, for the study of the active transport of large molecules is described.2. Uptake of gamma-globulin occurred within 15 min and required no exogenous substrates.3. In vitro absorption of gamma-globulin by intestinal epithelium was limited to the neonatal pig and 5-day-old mouse. No uptake was seen in intestines from a mature mouse, a pig with diarrhoea, a normal pig, a mature rabbit, a guinea-pig, a chick, and a chick embryo. Chick embryo yolk sac readily took up gamma-globulin.4. Rings of everted intestinal epithelium remained active (still absorbed gamma-globulin) after incubating for 4-6 hr in balanced salt solution (BSS).5. Uptake of gamma-globulin required oxygen and sodium and was reversibly inhibited by metabolic antagonists such as iodoacetate, arsenate, fluoride, 4,6-dinitro-varphi-cresol, phlorrhizin, anaerobiosis and cold. Under the conditions of the test, large colloidal molecules did not inhibit uptake of gamma-globulin.6. Similar results (although not as clear-cut) with metabolic inhibitors were obtained with preparations of chick embryo yolk sacs.7. Injuring mature pig's intestinal epithelium with surface-active agents did not produce non-specific absorption artifacts that resembled the specific absorption found in immature pig's intestinal epithelium.

Animals↗

PubMed1987

Rapid androgenic stimulation of alpha 2u-globulin synthesis in the perfused rat liver.

Hepatic synthesis of alpha 2u-globulin and its mRNA in the male rat is dependent on androgen, glucocorticoid, T4, insulin, and GH. Some of these hormones may act directly on the liver, while others may influence alpha 2u-globulin synthesis through indirect physiological changes. In the present study the specific role of androgen in the synthesis of alpha 2u-globulin was examined in an in vitro liver perfusion system. The addition of 5 alpha-dihydrotestosterone to the medium perfused through livers from castrated rats resulted in a rapid increase (approximately 10-fold over the vehicle control within 120 min) in the circulating level of alpha 2u globulin. Labeling with [35S]-methionine showed that the androgen-mediated increase in the circulating level of alpha 2u-globulin is due to release of the newly synthesized protein. Quantification of alpha 2u-globulin mRNA in the perfused livers with and without androgen supplementation indicated that the increased mRNA level can only partially account for the elevation of the circulating level of this protein. From these results it is concluded that androgen can act directly on the liver to stimulate alpha 2u-globulin synthesis, and the hormone may influence more than one regulatory step.

Alpha-Globulins↗