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PubMed2003

Sample preparation of human serum for the analysis of tumor markers. Comparison of different approaches for albumin and gamma-globulin depletion.

LC-MS is a powerful method for the sensitive detection of proteins and peptides in biological fluids. However, the presence of highly abundant proteins often masks those of lower abundance and thus generally prevents their detection and identification in proteomic studies. In human serum the most abundant proteins are albumin and gamma-globulins. We tested several approaches to specifically reduce the level of these proteins based on either specific antibodies, dye ligands (for albumin) and protein A or G (for gamma-globulins). The resulting, depleted serum was analyzed by sodium dodecylsulfate-polyacrylamide gel electrophoresis and LC-MS for the residual presence of these abundant proteins as well as for other serum proteins that should remain after depletion. To test the applicability of this method to real-life samples, depleted serum of a cervical cancer patient was analyzed for the presence of a specific tumor marker protein SCCA1 (squamous cell carcinoma antigen 1; P29508), which is present at ng/ml concentrations. The results demonstrate that SCCA1 can be detected by LC-MS in patient serum following depletion of albumin and gamma-globulins thus opening the possibility of screening patient sera for other, so far unknown, tumor markers.

Albumins↗
PubMed2000

New affinity nylon membrane used for adsorption of gamma-globulin.

Microporous polyamide membranes were first modified by acid hydrolysis and subsequently bound with hydroxy-ethylcellulose to amplify reactive groups and reduce nonspecific interactions with proteins. Then 1,6-diaminohexane as space arm and phenylalanine as ligand were immobilized onto the nylon membranes by s-triazine trichloride activation. Affinity membranes thus obtained were set in a stack and used to adsorb gamma-globulin. The adsorption capacity (qm) of the affinity membrane is 53 micro gamma-globulin per m2 membrane and the desorption constant (Kd) is 2.35 x 10(-6) mol/l. The effects of feed, washing and elution rates on adsorption and desorption behavior were investigated. The results showed that affinity purification through these membranes could not be operated at very high flow-rates. A stack of 20 membranes with 47 mm diameter can adsorb 7.8 mg gamma-globulin with a purity of 91.6% from 4 ml of human plasma in a single-pass mode.

Adsorption↗
PubMed1997

A complex of histamine/mouse gamma-globulin preferentially inhibits allergen-induced peritoneal accumulation of eosinophils, but not neutrophils, in mice.

A complex of histamine/human gamma-globulin (HhG) has been widely used in Japan for more than 25 years as a nonspecific hyposensitization drug in the treatment of allergic diseases. It has been reported that HhG decreases the number of eosinophils in the nasal secretions and peripheral blood of patients with allergy. In this study we used a mouse system to explore the possibility that HhG may actively inhibit the accumulation of eosinophils at inflammation sites. A complex of 0.15 microg of histamine dihydrochloride/12 mg of mouse gamma-globulin (HmG) was incubated for 2 hours in saline solution in the normal fashion for HhG. HmG at 50 to 150 mg/kg/day inhibited the peritoneal accumulation of eosinophils induced by ragweed pollen in BALB/c mice in a dose-dependent fashion when the HmG was administered subcutaneously six times during a 20-day sensitization period. The inhibitory effect of HmG on this eosinophil accumulation was significant at 24 and 48 hours after challenge, but HmG had no effect on neutrophil accumulation. Complexes of serotonin/mouse gamma-globulin (mgammaG), glutamine/mgammaG, and histamine dihydrochloride (His)/mouse albumin had no inhibitory effect when administered in the same way. The optimum combination ratio was between 0.15 microg of His/12 mg of mgammaG and 0.015 microg of His/12 mg of mgammaG for this eosinophil inhibition. Moreover, a 1- to 2-hour incubation period of His and mgammaG was needed to induce a plateau inhibition of the eosinophil accumulation. These results in mice suggest that HhG may actively inhibit allergen-induced eosinophil accumulation, which may be therapeutically useful in the treatment of allergic disease.

Allergens↗
PubMed2001

Fourier-transform infrared spectroscopic study of globulin from Phaseolus angularis (red bean).

The conformation of red bean globulin dispersions (approximately 10% in D2O or deuterated phosphate buffer pD 7.4) under the influence of pH, chaotropic salts, protein structure perturbants, and heating conditions was studied by Fourier-transform infrared (FTIR) spectroscopy. The FTIR spectrum of red bean globulin showed major bands from 1682 to 1637 cm(-1) in the amide I' region, corresponding to the four types of secondary structures, i.e. beta-turns, beta-sheets, alpha-helix and random coils. At extreme pH conditions, there were changes in intensity in bands attributed to beta-sheet (1637 and 1618 cm(-1)) and random coil (1644 cm(-1)) structures, and shifts of these bands to lower or higher wave numbers, indicating changes in protein conformation. Chaotropic salts caused progressive increases in random coil structures and concomitant decreases in beta-sheet bands, following the lyotrophic series of anions. In the presence of sodium dodecyl sulfate and ethylene glycol, pronounced increases in the random coil band were observed, accompanied by slight shifts of the beta-sheet band. Addition of dithiothreitol and N-ethylmaleimide did not cause marked changes in the FTIR spectra. Heating at increasing temperature led to progressive decreases in the intensity of the alpha-helix and beta-sheet bands and increases in random coil band intensity, leveling off at around 60 degrees C. The data suggest that re-organization of protein structure occurred at temperatures well below the denaturation temperature of red bean globulin (86 degrees C) as determined by differential scanning calorimetry. This was accompanied by pronounced increases in the intensity of the two intermolecular beta-sheet bands (1682 and 1619-1620 cm(-1)) associated with the formation of aggregated strands at higher temperatures (80-90 degrees C). Increases in intensity of the aggregation bands were also observed in the heat-induced buffer-soluble and insoluble aggregates.

Calorimetry, Differential Scanning↗
PubMed1992

Association of proteins in acidic solutions--a case study with beta-globulin.

The investigation of the effect of acid pH on the structure of beta-globulin indicated several transitions as a function of pH. Upon reducing the pH from 7.0, the beta-globulin molecule underwent an expansion due to hydration up to pH 5.0, and a further increase in H+ concentration resulted in unfolding. This is a single step cooperative denaturation as indicated by the viscosity profile. At extreme acid pH values (below pH 2.0) the protein associates or folds to a different conformational motif as shown by blue shift of ultraviolet fluorescence emission maximum and decrease in reduced viscosity values by more than 30% due to an entropically driven hydrophobic interaction. The conformational analysis of beta-globulin showed a decrease up to pH 3.0, followed by an increase in the ordered structure at low pH values indicating that the low pH values stabilized this new conformation. These results are discussed in view of the molten globule structure of proteins.

Beta-Globulins↗
PubMedDate not supplied

[Short-term effects of gamma-globulins on sleep organization in epileptic patients (author's transl)].

A study of the effect of gamma-globulins on sleep was conducted in 8 patients aged 1 to 35 years with epilepsy not responding to any of the conventional treatments. Two polygraphic recordings were carried out during the 4th and 5th nights following a placebo injection and then an injection of gamma-globulin 16 Merieux (1 ml/kg). The short-term effects of the gamma-globulins were : --reduction in percentage of paroxysms, --an acceleration in the electroencephalographic tracings of the different stages of sleep and those of the waking period, --a statistically significant increase in the percentage of paradoxical sleep, though the general organization of sleep remained unchanged.

Adolescent↗
PubMed1998

Sex-hormone binding globulin as an indicator of the hepatic impacts of continuous combined hormone replacement regimens.

OBJECTIVES: Nonoral administration of hormone replacement therapy avoids the first pass metabolism of steroids in the liver. We wanted to determine to what extent it has an effect on the serum concentrations of sex-hormone binding globulin and the free testosterone index. METHODS: Postmenopausal women received 50 microg per day transdermal estradiol associated with the use of a levonorgestrel-releasing intrauterine device (20 women) or a daily oral dose of 2 mg of estradiol and 1 mg of norethisterone acetate (20 women) for 1 year. Eight women, five in the nonoral and three in the oral therapy group discontinued the study. RESULTS: Although serum sex-hormone binding globulin concentrations decreased in women receiving transdermal estradiol in combination with a levonorgestrel-releasing intrauterine device, the free testosterone index did not change significantly. In the continuous oral regimen, no significant changes in serum sex-hormone binding globulin or free testosterone index were observed. The free testosterone index, however, was significantly higher in the nonoral therapy group after 6 and 12 months of treatment than in the oral therapy group. CONCLUSIONS: Continuous progestin combined with continuous estrogen in oral and nonoral replacement therapy does not lead to a substantial androgenic excess in postmenopausal women. The intrauterine administration of levonorgestrel appears to have some hepatic effect.

Administration, Cutaneous↗
PubMedDate not supplied

Estradiol induction of cAMP in breast cancer cells is mediated by foetal calf serum (FCS) and sex hormone-binding globulin (SHBG).

Plasma sex hormone-binding globulin (SHBG or SBP), the specific carrier for estradiol and androgens, after binding to its membrane receptor (SHBG-R), causes a significant increase of cAMP in the presence of estradiol, in both breast (MCF-7) and prostate (LNCaP) cancer cells maintained in serum-free medium. On the other hand, it has been proposed that estrogens, in addition to the well-known nuclear receptor pathway, exert their biological effect inducing cAMP, as a consequence of a direct membrane action, in breast cancer and uterine cells. The aim of the present study was to clarify this controversial issue by verifying if the cAMP increase in MCF-7 cells was a direct effect of estradiol, or if it was mediated by FCS proteins, such as bovine sex hormone-binding globulin; and to reevaluate the effect of human SHBG on cAMP induction in the presence of FCS. MCF-7 cells were maintained in DCC-FCS (treated with DCC to remove steroids), in SHBG-FREE/DCC-FCS (treated with DCC and with a specific affinity chromatography to remove bovine sex hormone-binding globulin), or in serum-free medium (SFM). It was observed that estradiol determined a significant time-dependent increase of cAMP only in MCF-7 cells maintained in 10% DCC-FCS. When cells were maintained in 10% SHBG-FREE/DCC-FCS, estradiol had no detectable effect. However, its ability to increase cAMP was observed again after the addition of human SHBG, in doses ranging from 5 to 50 nM. Moreover, in the presence of 10% SHBG-FREE/DCC-FCS, SHBG, even in the absence of estradiol, caused a significant increase of cAMP. In conclusion, the data reported in the present study suggest that the ability of estradiol to induce cAMP in MCF-7 cells is not due to a direct membrane effect of the hormone, but rather it is mediated by FCS. SHBG is one of the serum factors mediating estradiol action. Lastly, it was proven that SHBG triggers the cAMP pathway in MCF-7 cells in a physiologic culture condition and at physiologic concentrations.

Animals↗
PubMed1987

Cytoplasmic androgen binding protein of rat liver: molecular characterization after photoaffinity labeling and functional correlation with the age-dependent synthesis of alpha 2u-globulin.

The liver of the mature male rat contains a moderate affinity (Kd = 10(-8)M), low-capacity, cytoplasmic androgen binding protein (CAB) whose appearance during puberty and disappearance during senescence correlate with the androgen-dependent synthesis of alpha 2u-globulin. Molecular properties of CAB were examined by photoaffinity labeling with tritiated methyltrienolone (R-1881), a synthetic androgen, and by its localization within the hepatocytes which are competent to produce alpha 2u-globulin. Photoaffinity labeling of the liver cytosol derived from postpubertal male rats, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography, showed a predominant androgen binding band corresponding to Mr 31,000. This 31-kilodalton (kDa) binding component was conspicuously absent in the liver of androgen-insensitive prepubertal and senescent male rats and in adult male rats treated with estradiol-17 beta. In addition, unlike the cytoplasmic extract, the nuclear lysate of the male rat hepatocytes did not contain the 31-kDa androgen binder. Disappearance of the 31-kDa androgen binding band from the cytosolic fraction of androgen-insensitive animals was associated with a concomitant appearance of a minor androgen binding component of apparent Mr 29,000. The livers of postpubertal male rats normally contain two subpopulations of hepatocytes, only one of which is highly active (competent) in alpha 2u-globulin synthesis. Separation of these two subpopulations through a fluorescence-activated cell sorter followed by whole cell labeling showed more than a 2-fold higher uptake of R-1881 by the competent cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Affinity Labels↗
PubMedDate not supplied

An investigation of the binding site of alpha 2u-globulin using isotopically labeled ligands and inverse nuclear magnetic resonance techniques.

A series of isotopically labeled ligands were bound to the protein alpha 2u-globulin. These protein complexes were studied using 13C, 19F, and selective inverse detection NMR experiments to determine chemical shifts and nuclear Overhauser effect correlations for the labeled sites of the ligands. The NMR data indicate that the labeled portions of the ligands are located in a highly aromatic region of the alpha 2u-globulin binding pocket. Molecular modeling based on the NMR data and a medium resolution X-ray crystal structure of alpha 2u-globulin predicts a model for ligand binding which is consistent with experimental observations and calculated ring current effects. Conformational changes in the aromatic region of the binding site upon binding these ligands in solution may be supported by this model.

Alpha-Globulins↗
PubMed1997

Characterization of a novel rice bZIP protein which binds to the alpha-globulin promoter.

Many plant basic leucine-zipper (bZIP) proteins have been isolated several of which have been shown to play a role in seed-specific gene expression. We isolated a novel bZIP protein (REB) gene encoding 425 amino acid residues from rice endosperm, which is similar to Opaque-2 heterodimerizing protein (OHP) of maize. The gene product, termed REB, contains Pro- and Gly-rich regions at its N terminus, followed by the typical basic and leucine-repeat regions. Recombinant REB binds to the region from -754 to -562 in the alpha-globulin gene promoter, but not to promoters of other major storage genes such as glutelin, prolamin and albumin. The 5' region of the alpha-globulin gene possesses three binding sites for REB, which were determined as GCCACGT(A/C)AG, by using synthetic oligonucleotides. A Super-shift assay using anti-REB antibody suggested that REB is a major DNA-binding protein for the alpha-globulin gene promoter in rice endosperm.

Alpha-Globulins↗
PubMed1981

Hormonal inducibility of rat alpha 2u globulin genes in transfected mouse cells.

Two different genes coding for the hormonally regulated rat liver protein alpha 2u globulin were introduced into mouse Ltk- cells through co-transfection with the HSV-1 thymidine kinase gene. Three to ten copies of the alpha 2u globulin genes were detected several tk+ clones, over 50% of which could be induced with dexamethasone, the produce alha 2u globulin mRNA and protein. This suggests that the information necessary for hormonal response is contained in the DNA fragment used for transfer.

Alpha-Globulins↗
PubMed1969

Isolation of human beta1A-globulin by modern techniques.

1. Human beta(1A)-globulin was isolated from serum by precipitation with ammonium sulphate, gel filtration and electrophoresis in polyacrylamide gel. 2. The product was found by ultracentrifugation, analytical electrophoresis in polyacrylamide gel and two-dimensional immunoelectrophoresis to be of satisfactory quality for further study. 3. The amino acid composition of beta(1A)-globulin was determined. 4. In ordinary dilute buffers near neutrality, beta(1A)-globulin had S(0) (20,w) 6.42s and M 131 000, but some reversible aggregation occurred at lower pH. In neutral 6m-guanidine hydrochloride the molecular weight was not measurably different from that in dilute buffer.

Amino Acids↗
PubMedDate not supplied

Fetal cell counting as an evaluation of Rh prophylaxis with antenatally administered anti-Rh O (D) gama globulin.

Fetal cell counts were performed on pregnant women at 34 weeks' gestation following an injection of Anti-Rh O (D) gamma globulin at 28 weeks' gestation. In cases where the fetus subsequently proved to be Rh O (D) positive and ABO compatible, the fetal cell detection rate and the mean number detected detected were considerably less than those where the fetus was Rh negative. Postpartum fetal cell counts after one and two antenatal anti-Rh O (D) gamma globulin injections were also less when the baby was Rh positive than when the baby was Rh negative. These findings provide evidence that antigen clearance is definitely part of the mechanism involved in Rh prophylaxis by the use of anti-Rh O (D) gamma globulin.

ABO Blood-Group System↗
PubMed1990

Immunohistochemical localization of sex hormone-binding globulin in normal and neoplastic breast tissue.

The distribution of sex hormone-binding globulin-like antigens (SHBG-LA) in normal and neoplastic human breast tissues was investigated by immunohistochemistry, employing a monospecific polyclonal antiserum against highly purified human SHBG and an avidin-biotin-peroxidase complex (ABC) method in formalin-fixed paraffin embedded tissue sections. In normal breast tissues the staining of SHBG-LA was present exclusively in the cytoplasm of epithelial cells of ductal and ductular types. Nuclei as well as stromal and lymphatic tissues remained unstained. While the staining was positive in all cases of intraductal carcinoma, only 4 out of 15 infiltrating carcinomas revealed SHBG-LA. The demonstration of a plasma sex steroid binding globulin in the cytoplasm of endocrine target cells is consistent with the hypothesis that steroid-binding globulins are able to enter target cells. The apparent loss of this specific cell function in infiltrating carcinomas may result from dedifferentiation and change of cell membrane properties occurring during the process of neoplastic progression.

Breast Neoplasms↗
PubMed1999

Clinical outcomes after hepatitis C infection from contaminated anti-D immune globulin. Irish Hepatology Research Group.

BACKGROUND AND METHODS: In February 1994, batches of anti-D immune globulin used in Ireland during 1977 and 1978 to prevent Rh isoimmunization were found to be contaminated with hepatitis C virus (HCV) from a single infected donor. In March 1994, a national screening program was initiated for all women who had received anti-D immune globulin between 1970 and 1994. Of the 62,667 women who had been screened when this study began, 704 (1.1 percent) had evidence of past or current HCV infection, and 390 of those 704 (55 percent) had positive tests for serum HCV RNA on reverse-transcription-polymerase-chain-reaction analysis. All 390 were offered a referral for clinical assessment and therapy. We evaluated 376 of these 390 women (96 percent); the other 14 were not seen at one of the designated treatment centers. RESULTS: The mean (+/-SD) age of the 376 women was 45+/-6 years at the time of screening. They had been infected with hepatitis C for about 17 years. A total of 304 women (81 percent) reported symptoms, most commonly fatigue (248 [66 percent]). Serum alanine aminotransferase concentrations were slightly elevated (40 to 99 U per liter) in 176 of 371 women (47 percent), and the concentrations were 100 U per liter or higher in 31 (8 percent). Liver biopsies showed inflammation in 356 of 363 women (98 percent); in most cases the inflammation was slight (41 percent) or moderate (52 percent). Although the biopsy samples from 186 of the 363 women (51 percent) showed evidence of fibrosis, only 7 women (2 percent) had probable or definite cirrhosis. Two of the seven reported excessive alcohol consumption. CONCLUSIONS: Most of the women with HCV infection 17 years after receiving HCV-contaminated anti-D immune globulin had evidence of slight or moderate hepatic inflammation on liver biopsy, about half had fibrosis, and 2 percent had probable or definite cirrhosis.

Adult↗
PubMed1996

Partial characterization of the lysine rich 280kD globulin from common buckwheat (Fagopyrum esculentum Moench): its antigenic homology with seed proteins of some other crops.

A high molecular weight (HMW) globulin, the main storage protein in grains of the common buckwheat (Fagopyrum esculentum Moench) has been partially characterized. The protein exists as an oligomeric complex with molecular mass of 280 kD and is composed of three groups (alpha, beta and gamma of polypeptides with molecular weights ranging between 55-60, 32-44 and 16-29 kD respectively. The protein showed serological cross reactivity with globulins of soya bean, mung bean and pea. Antibodies raised against the purified protein did not recognize the storage proteins from broad bean, rice, wheat and grain amaranth. The 280 kD globulin of buckwheat grains belongs to the legumin family of proteins.

Chromatography↗
PubMed1965

Distribution among the gamma-globulin molecules of different genetically determined antigenic specificities in the Gm system.

Isolated myeloma proteins and anti-Rh antibodies were utilized for determination of the distribution among the gamma-globulin molecules of various Gm(b) and Gm(f) determinants. All of these genetic factors are as a rule inherited together in Caucasians, but not in other races. The Gm(b) determinants, except (b(2)), were found together in the same Caucasian myeloma globulins of the Vi H chain group, which never carried Gm(f) or (b(2)). The Gm(f) and (b(2)) determinants were found together in other myeloma globulins, of the We group. Anti-Rh antibody molecules appeared to be similar to myeloma molecules in these respects. A few myeloma proteins and anti-Rh antibodies were encountered which reacted with some but not other anti-Gm(b) or anti-Gm(f) reagents; the only available Vi type myeloma protein from a Negro, specifically lacked the Gm(b(3)) factor. The observations might be explained by the following hypothesis: In Caucasians with the common Gm(f) Gm(b) gene complex the Gm(b) antigenic determinants, except (b(2)), co-occur in certain molecules, which contain a polypeptide chain determined by the Gm(b) gene; the Gm(f) and (b(2)) determinants co-occur in other molecules, which contain a polypeptide chain determined by the Gm(f) gene. Individuals that lack some Gm(b) or Gm(f) determinants most likely have a gene partly different from Gm(b) or Gm(f). The value of studies with myeloma proteins from individuals of different racial groups was apparent from this study. One myeloma protein from a Chinese was unique in that it was both Gm(a+) and Gm(f+).

Antigens↗