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At least 631 records · Page 35Linked to original sources
PubMed1961

Immunologic studies of heart tissue. III. Occurrence of bound gamma globulin in auricular appendages from rheumatic hearts. Relationship to certain histopathologic features of rheumatic heart disease.

Using fluorescent antibody methods, deposits of bound gamma globulin, as determined in unfixed washed sections of auricular appendages from rheumatic hearts, were noted in a significant number (18 per cent) of 100 specimens studied. Such deposits were observed in myofibers, sarcolemma, interstitial connective tissue, and vessel walls. Albumin and fibrin were generally found absent from these sites. Control hearts from normal and pathologic material, including postmortem and biopsied specimens, in general, did not reveal such deposits. These various tissue sites which contained bound gamma globulin frequently exhibited evidence of alteration as indicated both by enhanced affinity for eosin and by strongly positive reaction with the periodic acid-Schiff reagent, and appeared comparable in some cases to "fibrinoid." Bound gamma globulin was not observed in cellular or stromal components of Aschoff lesions, nor was the occurrence of Aschoff lesions correlated with presence of bound gamma globulin. It is suggested that deposition of gamma globulin and the eosinophilic alteration associated with such deposition are related to certain of the pathologic changes of rheumatic heart disease. The nature of such deposits of gamma globulin was considered from immune and non-immune points of view.

Atrial Appendage↗
PubMed1967

Heavy chain subclasses of human gamma G-globulin. Serum distribution and cellular localization.

Two antigenic types of naturally occurring proteins related to the papain produced F(c) fragment of gammaG-globulin have been studied. Most normal and myeloma gammaG-globulins are related to one or the other of these proteins, based on antigenic and structural characteristics of their heavy chain. Molecules bearing the determinant "Cr" are approximately 10 times as abundant as those bearing the determinant termed "Zu" in pools of normal gammaG-globulin and among a large group of gammaG-myeloma globulins. Both populations have properties of typical gammaG-globulin antibodies. Splenic cells, stained for these two populations with specific fluorescent antibody preparations, are found to contain one or the other of the two populations of gammaG-globulin, but not both. Approximately 10 times as many cells contain the Cr determinant as contain the Zu determinant.

Animals↗
PubMed1996

Ciprofibrate represses alpha 2u-globulin expression in liver and inhibits d-limonene nephrotoxicity.

Peroxisome proliferators are a class of compounds which induce hepatomegaly and peroxisome proliferation in liver parenchymal cells. One of the earliest known effects of peroxisome proliferators is the rapid transcriptional activation of the genes responsible for the peroxisomal beta-oxidation system in liver. Long term administration of these chemicals to rats and mice results in the development of hepatocellular carcinomas. Here we report that mRNA for alpha 2u-globulin, a rodent male specific protein, is markedly reduced or undetectable by Northern blot analysis of total RNA in the livers of rats treated with ciprofibrate. This was further confirmed by immunoblot analysis using antibodies against alpha 2u-globulin. Nevertheless, immunohistochemical staining and in situ hybridization showed respectively the presence of a few cells that contained alpha 2u-globulin protein and its mRNA. The alpha 2u-globulin mRNA reappeared in the liver 2 weeks following the cessation of ciprofibrate treatment. Feeding of ciprofibrate for two weeks followed by simultaneous feeding of ciprofibrate and a nephrotoxic chemical d-limonene for 5 weeks revealed that ciprofibrate prevented the renal accumulation of alpha 2u-globulin and the nephrotoxicity associated with the binding of d-limonene with alpha 2u-globulin.

Alpha-Globulins↗
PubMed1997

Ascorbic acid deficiency decreases the renal level of kidney fatty acid-binding protein by lowering the alpha2u-globulin gene expression in liver in scurvy-prone ODS rats.

The evidence for the role of ascorbic acid in gene expression or protein synthesis in vivo is limited. To investigate this role of ascorbic acid, we surveyed proteins whose tissue levels are changed by ascorbic acid deficiency by using ODS rats with a hereditary defect in ascorbic acid biosynthesis. Male ODS rats (7 wk old, body weight approximately 130 g) were fed a basal diet containing ascorbic acid (300 mg/kg diet) or an ascorbic acid-free diet for 14 d. Ascorbic acid deficiency decreased a renal protein with an apparent molecular mass of 17 kDa. The amino-terminal amino acid sequence of 16 residues of this 17-kDa protein was identical to a kidney fatty acid-binding protein known to be generated by proteolytic degradation of alpha2u-globulin, a major urinary protein of adult male rats. alpha2u-Globulin is synthesized in liver, secreted into blood and excreted into urine, but partially reabsorbed by renal proximal tubules. It exists in kidney in a proteolytically modified form. Ascorbic acid deficiency lowered the renal level of kidney fatty acid-binding protein to 53% (P < 0.05) and lowered the serum level of alpha2u-globulin to 52% (P < 0.05) of the level of the control group, but did not affect the amount of alpha2u-globulin excreted into urine. The hepatic level of alpha2u-globulin mRNA of the ascorbic acid-deficient rats was significantly lower (30%) than that of the control rats. These results suggest that in male ODS rats, ascorbic acid deficiency decreases the renal level of kidney fatty acid-binding protein by lowering alpha2u-globulin gene expression in liver.

Alpha-Globulins↗
PubMed2003

Subcellular localization of soybean 7S globulin in HepG2 cells and LDL receptor up-regulation by its alpha' constituent subunit.

The aims of this work were to monitor the subcellular localization of soybean 7S globulin in HepG2 cells and determine its interaction with cell protein components, by using laser-induced fluorescence capillary electrophoresis (LIF-CE). Furthermore, we evaluated in the same cell line the involvement of the alpha' constituent subunit from 7S globulin in the modulation of LDL catabolism. The results indicated a main fluorescein isothiocyanate-tagged 7S globulin (FITC-7S) component in the cytosolic fraction, that was not present in the nuclear compartment. The electrophoretic mobility of this tagged component suggested either a dissociation of the 7S oligomer or its partial intracellular degradation. Interactions of soybean 7S globulin with FITC-thioredoxin 1 and FITC-cyclophilin B, HepG2 cell membrane proteins, were demonstrated in in vitro assays. In a separate experiment with HepG2 cells, the ability of the alpha' subunit purified from soybean 7S globulin to modulate the activity of the LDL receptors was evaluated by tracking the uptake and degradation of labeled LDL. The up-regulation of LDL receptors by the alpha' subunit, as further confirmed by a LDL receptor promoter assay, was significantly greater than that found in the control cells. In conclusion, this study, while confirming our previous indirect evidence of the key role of alpha' subunit on the cell cholesterol homeostasis, reveals a potentially interesting association of soybean 7S globulin with proteins, such as thioredoxin 1 and cyclophilin B, that are involved in cell protection against oxidative stress.

Antigens, Plant↗
PubMed1981

Hormone binding globulin levels in patients with hereditary angiooedema during treatment with Danazol.

Five patients with hereditary angiooedema were treated with Danazol for periods up to 10 months. This therapy resulted in normalization of serum levels of the inhibitor of the first complement component and disappearance of clinical disease symptoms in all patients. Although a variety of hormones were measured, only those of the pituitary-gonadal axis altered during treatment: a moderate decrease in leuteinizing hormone levels and a sharp fall of testosterone in adult men were observed. In all patients, however, both sex hormone binding globulin and thyroxine binding globulin concentrations were considerably suppressed during Danazol therapy. However, levels of corticosterone binding globulin and thyroxine binding globulin concentrations were considerably suppressed during Danazol therapy. However, levels of corticosterone binding globulin remained unchanged. The fraction of endogenous testosterone not bound to sex hormone binding globulin invariably increased. The possible relevance of these findings to the understanding of the mode of action of Danazol both in these patients and in general, are discussed.

Adult↗
PubMed1975

Clinical tolerance and catabolism of plasmin-treated gamma-globulin for intravenous application.

Plasmin-treated gamma-globulin of placental origin was tested in clinical and laboratory studies and found to be suitable for intravenous use both for prophylactic and therapeutic purposes. Plasmin treatment of gamma-globulin (IgG) results in proteolytic cleavage of 60-70% of the molecules into Fab and Fc fragments whereas 30-40% of the molecules are plasmin resistant. The antibody spectrum of plasmin-treated gamma-globulin is similar to that of standard gamma-globulin. Catabolic properties of the plasmin-resistant portion of this preparation and of standard gamma-globulin are identical. Plasmin-treated gamma-globulin has no anticomplementary activity and its intravenous administration is well tolerated even by highly sensitive immunodeficient patients.

Adolescent↗
PubMed1987

Comparison of the 5' upstream putative regulatory sequences of three members of the alpha 2u-globulin gene family.

We have isolated and characterized seven members of the alpha 2u-globulin gene family from a rat genomic library. The 5' upstream region (up to 1250 base pairs starting from the EcoRI site in exon 2) of three clones was sequenced. The major transcriptional start points were located 25 base pairs downstream from the 'TATA' box. A very high degree of homology was observed over the entire studied region. Two of the examined genes displayed structural features which suggest that their expression may be impeded. A high degree of homology was observed between the promotor regions of alpha 2u-globulin and those of the major urinary protein (MUP) multigene family of the mouse. A remarkable feature is the variable length of an A-rich region between the putative 'CAAT' and the 'TATA' consensus sequences. The size of this region differs markedly between MUP and alpha 2u-globulin and between different members of the alpha 2u-globulin gene family. Comparison of the alpha 2u-globulin promotor with the corresponding region of other androgen-dependent genes (the C1, C2 and C3 subunits of prostatic steroid binding protein) reveals the presence of an A-rich region of homology located approximately 378 base pairs upstream from the cap site in the alpha 2u-globulin genes. This region compares well with a sequence of putative enhancer function previously demonstrated in the alpha-fetoprotein promotor and in the immunoglobulin heavy chain promoter.

Alpha-Globulins↗
PubMed2005

Purification of severe acute respiratory syndrome hyperimmune globulins for intravenous injection from convalescent plasma.

BACKGROUND: Severe acute respiratory syndrome (SARS) is a new infectious disease caused by the SARS virus. Current first-line treatments are experimental, and their effectiveness remains open to question. For more effective treatment and prevention of SARS, human SARS hyperimmune globulins for intravenous (IV) injection were purified in this study. STUDY DESIGN AND METHODS: A combination of cold ethanol precipitation and ion-exchange chromatography was used to process pooled SARS convalescent plasma samples. Virus inactivation and removal approaches were taken to ensure safety. RESULTS: The purified hyperimmune globulins were formulated as a 5 percent solution, with an antibody titer specifically against the SARS virus of 1:83, 1:1600, and 1:200, as determined by enzyme-linked immunosorbent assay, immunofluorescence assay, and neutralizing antibody test, respectively. The purity of the SARS hyperimmune globulins was 99.0 percent, and the monomer and dimer content was 100 percent. Other variables analyzed met the Chinese Requirements of Biologics for IV immune globulin. The SARS hyperimmune globulins prepared were subsequently approved for clinical evaluation by the Chinese National Institute for the Control of Pharmaceutical & Biological Products. CONCLUSION: IV-injectable, purified, and concentrated human SARS hyperimmune globulins were prepared from pooled convalescent plasma samples, which are ready to be further evaluated.

Antibodies, Viral↗
PubMed1996

Globulin-enriched protein supplements shorten the pre-compaction mitotic interval and promote hatching of murine embryos.

PROBLEM: To determine whether Synthetic Serum Substitute (SSS), which contains human globulins in addition to Human Serum Albumin (HSA), is superior to HSA alone as a protein supplement for embryo culture. METHOD: Development of mouse zygotes to eight-cell/compacting morulae and to hatching/hatched blastocysts was assessed in Human Tubal Fluid (HTF) medium containing either SSS of HSA. RESULTS: Although there was no difference in the overall blastocyst rate at 120 h in HTF+SSS versus HTF+HSA, significantly more embryos at 54 h were at the eight-cell/compacting morula stage in HTF+SSS. At 120 h, there were more hatching/hatched blastocysts in HTF+SSS, and hatching correlated with SSS concentration. Addition of isolated globulins to HSA significantly stimulated the number of hatching/hatched blastocysts. Hatching could be "rescued" by transfer of embryos grown in HTF+HSA to globulin-containing media and prevented by removal of globulins as late as the compacted morula stage (54 h). CONCLUSIONS: SSS is superior to HSA alone for embryo culture. The stimulatory effects on mitosis and hatching may be mediated directly by globulins or by other components in the globulin-enriched fraction.

Animals↗
PubMed1969

Proteolytic activity during the absorption of 131-I-gamma-globulin in the new-born calf.

1. Proteolytic activity within the small intestine of unsuckled calves less than 20 hr of age, anaesthetized with sodium pentobarbitone, has been assessed from the break-down of [(131)I]bovine serum gamma-globulin infused into the duodenum.2. Absorption of [(131)I]gamma-globulin was measured by analysis of venous blood, the levels of radioactivity attained in which were comparable with those when [(131)I]PVP K.60 (mean mol.wt. 160,000) was administered. When lymph collected from the thoracic duct during the absorption of [(131)I]gamma-globulin was injected into the femoral vein, the levels of radioactivity in the blood were close to those expected if the labelled material in the lymph had been retained within the plasma. These observations suggested that [(131)I]gamma-globulin was absorbed into the circulation of the anaesthetized young calf without significant break-down.3. Gel-filtration of lymph and plasma from calves fed [(131)I]gamma-globulin has confirmed that proteolysis before and during absorption was slight, since little (131)I labelled material of low mol.wt. was found.4. Gel-filtration of the contents of the alimentary tract from calves fed [(131)I]gamma-globulin showed that some hydrolysis occurred in the abomasum and duodenum and that this was reduced by barbiturate anaesthesia. Protein break-down in the terminal ileum was slight both in the conscious animal and in animals anaesthetized with sodium pentobarbitone.

Abomasum↗
PubMed1975

Alterations of alpha2-globulin and the clinical response in patients with prostatic cancer following cryotherapy.

Evaluation of alterations in the level of alpha2-globulin in the serum of 18 patients with prostatic cancer prior to and following cryotherapy of their primary prostatic tumor and the clinical response of these patients disclosed: (1) a progressive increase in the level of alpha2-globulin and the incidence of patients with significantly elevated levels of alpha2-globulin, i.e., greater than or equal to 1.30 g/100 ml, with a progression of the stage of their malignancy; (2) a decrease in the levels of alpha2-globulin in the serum of 14 of 18 (78%) patients following cryotherapy, and (3) a favorable clinical response in 11 of 14 (79%) patients with prostatic cancer showing a decrease in alpha2-globulin following cryotherapy. While limited to the study of a relatively small patient population, the present results suggest a prognostic potential for alpha2-globulin, particularly as applied to stage identification in prostatic cancer. Pending confirmation by evaluation of a larger patient population, it may even provide objective criteria for monitoring the clinical response of an individual following cryotherapy of the prostate.

Alpha-Globulins↗
PubMed1967

Light and heavy chain components of gamma globulins in urines of normal persons and patients with agammaglobulinemia.

A heavy chain component of gammaG-globulins in normal urines has the characteristics of the proteolytic digestion product, Fc-fragment. This fragment is estimated to compose up to 15% of the gamma globulins present in urines. In contrast to urinary light chains, the urinary Fc-like fragment probably represents a catabolic component in normal gammaG-globulin metabolism. The light chains of the urine constitute more than half the total gamma globulin present. The calculated kappa/lambda ratio of light chains averaged 1.9 in ten urines, but the ratio in individual urines varied widely to either side of this figure. In two adult patients with agammaglobulinemia whose sera contained less than one-hundredth the normal gamma globulin levels, the urinary Fc-like fragment was absent, whereas the light chain levels were only one-tenth the average normal level. Treatment with exogenous gamma globulins resulted in normal or near normal Fc-like fragment excretion, whereas light chain excretion was only modestly affected.

Adult↗
PubMed1982

Synthesis and immunocytochemical localization of alpha 2u globulin in the duct cells of the rat submaxillary gland.

Alpha 2u globulin, a protein of unknown function so far believed to be synthesized exclusively in the male liver under multihormonal control, is now shown to be localized by immunocytochemistry in the granular convoluted tubules of the adult male submaxillary gland. In addition, using Northern blot analysis, we have shown specific alpha 2u globulin mRNA sequences in the RNA extracted from the submaxillary gland. Thus, it is evident that the protein is being synthesized therein. Alpha 2u globulin was also detected in the submaxillary gland duct cells of adult female and immature animals of both sexes, all of which are known not to synthesize alpha 2u globulin in their livers. The present data have established that alpha 2u globulin is synthesized in the rat submaxillary gland and indicate that the control of alpha 2u globulin gene expression in the rat liver and in the submaxillary gland is different.

Alpha-Globulins↗
PubMed1986

Differential endocrine regulation of alpha 2U-globulin messenger ribonucleic acid activity: effect of age at hypophysectomy.

Three alpha 2U-globulin products were identified on two-dimensional gel electrophoretograms of the [35S]methionine-labeled products formed in response to total hepatic RNA by the reticulocyte lysate translational assay. These products, arbitrarily designated A, B, and C, were quantified by video-imaging of two-dimensional electrophoretograms. At both 65 and 85 days, they represent approximately 13%, 10%, and 77%, respectively, of the total translational products coding for alpha 2U-globulin. Hypophysectomy at either 30 or 55 days resulted in a marked decrease in all three products when measured at 60 and 85 days. Products A and B were not induced in animals hypophysectomized (hypox) at 30 days and subsequently reinjected for 10 days beginning on day 50 with GH alone; with T4, corticosterone, and dihydrotestosterone (three hormones); or with a four-hormone combination. Product C was significantly induced by the four-hormone combination. In animals hypox at 55 days and reinjected for 10 days beginning on day 75, GH alone and the three-hormone combination failed to increase product A. In contrast to the observations in animals hypox at 30 days, the four-hormone combination induced a significant increase in products A and B in animals hypox at 55 days, and product C was induced by the three-hormone as well as the four-hormone combination. Measurement of total alpha 2U-globulin mRNA by cDNA hybridization indicated that animals hypox at 30 days achieved only 33.8% of age-matched normal levels, whereas animals hypox at 55 days achieved 69% (P less than 0.05) when injected with all four hormones. Furthermore, the three-hormone combination increased total alpha 2U-globulin mRNA in animals hypox at 55 days, but not in animals hypox at 30 days. The observations on the individual alpha 2U-globulin products suggest that endocrine regulation of individual alpha 2U sequences is not identical. The different magnitude of response observed in the animals hypox at different ages suggests that exposure of the liver to a pituitary-dependent factor between 30 and 55 days modifies the ability of the liver to regulate alpha 2U-globulin mRNA levels.

Aging↗
PubMed1994

Binding and aggregation of human gamma-globulin by cis-diamminedichloroplatinum(II) through disulfide bond.

The incubation of gamma-globulin with cis-diamminedichloroplatinum (II) (cis-DDP) resulted in gradual formation of insoluble aggregates. Since the precipitates, composed of polymerized gamma-globulin and cis-DDP, were completely solubilized with urea, the reaction mixture containing precipitate was examined in terms of the binding of cis-DDP and the effect on disulfide (S-S) bonds in the gamma-globulin. When gamma-globulin was incubated with 30 molar excess cis-DDP at pH 7.4 and 37 degrees C, cis-DDP gradually bound to as much as 12 mol per mol of gamma-globulin in 14 d. Concurrently, about four disulfide bonds were cleaved without reaching a certain plateau. An sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the aggregated gamma-globulin induced by cis-DDP was significantly different from that of the heat-denaturated aggregate form or the reduced form by sulfitolysis. The aquated complexes of cis-DDP also produced an insoluble precipitate and affected the S-S bond to a greater extent than the parent drug.

Cisplatin↗
PubMed1978

Relationship between the pituitary gland and gonadal steroids: involvement of a hypophysial factor in reduced alpha 2u-globulin and increased transcortin concentrations in rat serum.

Evidence is presented that the level of alpha 2u-globulin in the serum of male rats depends, at least in part, on neonatal androgens. After castration of adult animals the concentration of this protein falls but remains measurable, whereas in intact or ovariectomized female rats alpha 2u-globulin cannot be detected. Moreover, alpha 2u-globulin is found in adult male and female rats gonadectomized at birth and treated with a single injection of testosterone propionate immediately thereafter. The mechanism by which neonatal androgens increase the concentration of alpha 2u-globulin has been investigated. Transplantation of a supplementary pituitary gland under the renal capsule of male rats resulted in reduced levels of alpha 2u-globulin and increased levels of transcortin. The changes discussed here were observed only in those animals in which the transplant was functional and they were amplified or reversed by modulators of prolactin secretion such as oestrogens or bromocriptine respectively. The hypothesis is advanced that neonatal androgens stimulate the production of a hypothalamic inhibitory factor that controls the secretion of prolactin, or another hypophysial hormone subjected to similar neuroendocrine control. Measurements in gonadectomized animals and in rats receiving both oestradiol benzoate and bromocriptine indicate that, besides these pituitary-mediated effects, both oestrogens and androgens exert direct effects on the level of alpha 2u-globulin.

Alpha-Globulins↗
PubMed1986

Cellular interactions in the hormonal induction of alpha 2u-globulin in rat liver.

The role of hepatocellular interaction in the androgen-dependent synthesis of rat alpha 2u-globulin was examined by immunochemical analysis of liver sections. Both after androgen administration to the ovariectomized female and during puberty in the male, only a subpopulation of hepatocytes became competent to synthesize alpha 2u-globulin. These competent hepatocytes first appeared as discontinuous patches along the wall of the central vein. After the formation of a confluent layer around the central vein, cellular competency was seen to propagate toward the periportal direction through the cords of hepatic cells. Although the periportal progression of cellular competency for the synthesis of alpha 2u-globulin appeared to be an all-or-none phenomenon, it did not require cell division. From these results we conclude that certain components of the central vein are necessary for the hormonal induction of alpha 2u-globulin in the rat liver. We also propose that a primary endocrine influence on the hepatic vein results in the production of a secondary paracrine mediator which can trigger the synthesis of alpha 2u-globulin in adjacent hepatocytes. Perivenous to periportal flow of this putative secondary mediator can explain cell recruitment for the synthesis of alpha 2u-globulin along the hepatic cords.

Alpha-Globulins↗