Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30536 (PBS)
 9,886 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Both insulin-like growth factor-I (IGF-I) and IGF-II have been shown to promote granulosa cell differentiation and proliferation. While both type I and type II IGF receptors have been observed in rat granulosa cells, the identity of the IGF receptor type(s) mediating IGF hormonal action remains uncertain. Whereas the role of the rat type I IGF receptor cannot be completely evaluated at this time due to the lack of specific reagents, the availability of antibodies specific for the rat type II IGF receptor (R-II-PAB1) has made studies of this receptor type possible. To validate the utility of the R-II-PAB1 antiserum at the level of the rat granulosa cell, its ability to immunoneutralize the granulosa cell type II IGF receptor was examined. Significantly, R-II-PAB1 (10-100 micrograms/ml) proved a potent inhibitor of [125I]IGF-II (but not [125I]IGF-I) binding to granulosa cell membrane preparations. Substantial, albeit finite, R-II-PAB1-mediated inhibition of the cross-linking of [125I]IGF-II was also observed. Moreover, R-II-PAB1 proved highly potent in immunoprecipitating the rat granulosa cell type II IGF receptor. In light of these observations, we have proceeded to use R-II-PAB1 to assess the functional role of the rat granulosa cell type II IGF receptor in IGF-I and IGF-II hormonal action. To this end, FSH (20 ng/ml)-primed granulosa cells were cultured for 72 h in the absence or presence of IGF-I or IGF-II (50 ng/ml) with or without increasing (receptor-active) concentrations of R-II-PAB1 (10-100 micrograms/ml). Control incubations were carried out with an ammonium sulfate precipitate of nonimmune rabbit serum dialyzed against PBS. Significantly, both R-II-PAB1 and nonimmune rabbit serum were without effect on the cytodifferentiative action of either IGF-I or IGF-II. Subject to limitations inherent to the immunoneutralizing potency of R-II-PAB1, these findings are in keeping with the notion that (inasmuch as the conventional cytodifferentiative process is concerned) the granulosa cell type II IGF receptor does not appear to participate in transmembrane IGF signalling. By inference, these findings also suggest that IGF-I and IGF-II hormonal action at the level of the granulosa cell may be exerted largely, if not exclusively, via the type I IGF receptor. Thus, the potential relevance and the functional role(s), if any, of the granulosa cell type II IGF receptor remain to be determined.
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PMID:Insulin-like growth factor-I (IGF-I) and IGF-II hormonal action in cultured rat granulosa cells: mediation via type I but not type II IGF receptors. 215 63

Three experiments were performed to evaluate the inflammatory response, the antibody response and protection from experimental challenge of various Actinobacillus pleuropneumoniae serotype 5 (Ap5) vaccines in swine. In the first experiment, subcutaneous injections of either a water-in-oil (W/O) emulsion or Freund's complete adjuvant (FCA) caused lesions at the site of injection, while intraperitoneal injection of the W/O emulsion caused no lesions. In the second experiment, intraperitoneal (IP) injection of a W/O emulsion containing unwashed Ap5 cells (6-h culture) and/or supernates from a 24-h culture resulted in severe peritoneal lesions, while W/O emulsion containing PBS-washed Ap5 cells resulted in minimal peritoneal lesions. Ap5 alone or W/O alone failed to cause peritoneal lesions. The third experiment compared the antibody response and protection from challenge of pigs immunized with either 6-h PBS-washed Ap5 cells emulsified in oil - IP, 6-hour Ap5 cells adjuvanted with dimethyl diodacyl ammonium bromide - IP, Ap5 antigen alone - IP, a commercial vaccine - subcutaneously or saline - IP. All groups, except the saline-treated group, responded with high antibody titers to Ap5 2 weeks following vaccination; however, titers from the W/O plus antigen group were significantly higher than the three other groups (P less than 0.05). Following intranasal challenge with Ap5, all animals responded with increased antibody titers. All pigs were euthanized 10 days after challenge and evaluated for pneumonia and the lungs cultured for bacteria. The lungs of all pigs, excepting the W/O plus antigen group, contained pneumonic lesions and A. pleuropneumoniae was cultured from these lesions. These results, along with results from other groups, suggest that intraperitoneal immunization using oil-adjuvanted vaccine may be an effective method for protecting pigs from pneumonia due to A. pleuropneumoniae. Its efficacy may be due to stimulation of local respiratory mucosal immunity.
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PMID:Comparison of protective immunity and inflammatory responses of pigs following immunization with different Actinobacillus pleuropneumoniae preparations with and without adjuvants. 281 78

Proliferating cell nuclear antigen (PCNA), also called cyclin, was purified from PBS extract of rabbit thymus by using a combination of ammonium sulfate fractionation, DEAE-Sephacel, HPLC ion exchange, and HPLC gel filtration column chromatography. PCNA was purified more than 600 times and was analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting. SDS-PAGE showed that a 36 kD protein was selectively isolated in this purification process, and this protein was identified as PCNA by immunoblotting. Other previously identified nuclear antigens, Sm, nRNP, SS-A/Ro, SS-B/La, histone, and DNA, were not detected in this preparation by counterimmunoelectrophoresis and enzyme-linked immunosorbent assay (ELISA). Purified PCNA was used as an antigen to develop ELISA for rapid and specific detection of anti-PCNA in human sera. For further purification, the 36 kD band was electrophoretically eluted from SDS gel slices. The amino acid composition and the first 25 residues from the N-terminus of the protein were determined by using electroeluted PCNA. This amino acid sequence was found to be unique and showed little sequence homology with existent proteins in the protein identification resources databank.
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PMID:Purification and N-terminal amino acid sequence of proliferating cell nuclear antigen (PCNA)/cyclin and development of ELISA for anti-PCNA antibodies. 286 7

Searching for the best procedure for simultaneous estimation of the anterior pituitary hormones, extraction efficiencies of various media, additives such as urea and triton X-100, and physical treatments such as freezing-thawing (F-T) and sonication, were examined by measuring prolactin (PRL), growth hormone (GH), lutropin (LH), follitropin (FSH), and thyrotropin (TSH) in the extracts. Ethanolic media (60% EtOH) gave high yields of PRL at neutral to alkaline pH, but poor extraction of GH accompanied by a marked loss of its immunoreactivity during storage. Ethanolic media also gave a poor yield of LH even at high pH. Aqueous media like PBS at various pH, 0.1 M acetic acid and distilled water were considerably effective in the extraction of GH, LH, FSH and TSH if they were coupled with F-T and sonication. However, high yields of PRL could not be obtained with these aqueous media even with F-T and sonication. Hartree's 40% EtOH-6% ammonium acetate, pH 5.1, solubilized considerable amounts of glycoprotein hormones, but yielded almost no GH and only a small amount of PRL. The addition of triton X-100 to PBS (pH 7) at 0.1% resulted in the maximum extraction of glycoprotein hormones with homogenization and F-T, but further sonication was necessary for GH and PRL. When the anterior pituitaries were homogenized and frozen-thawed in PBS (pH 7) containing 1 M urea, yields of PRL, GH, LH, FSH, and TSH were maximum, and sonication did not cause any additional extraction, indicating that this procedure, i.e. homogenization and F-T in 1 M urea-PBS, would be the best for the simultaneous estimation of these anterior pituitary hormones.
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PMID:Choice of extraction procedure for estimation of anterior pituitary hormone content. 343 4

High-performance hydrophobic interaction chromatography (HP-HIC) was found to be an effective method for the separation of lectins into isolectin fractions. All of the purified lectins used in this study, Phaseolus vulgaris haemagglutinin (PHA), wheat germ agglutinin (WGA), Ricinus communis agglutinin (RCA), and Arachis hypogaea agglutinin (AHA), were prepared by affinity chromatography. HP-HIC was performed on a column (15 X 2.1 cm) of TSK gel Phenyl-5PW at room temperature. The lectin sample, dissolved in 1.0 or 0.5 M ammonium sulphate in phosphate buffered saline (pH 7.4) (PBS), was applied to the column and eluted with a linear gradient from 1.0 or 0.5 M ammonium sulphate in PBS to 0 M ammonium sulphate in PBS at a flow-rate of 4 ml/min. In the case of RCA, addition of glycerol to the elution buffer resulted in sharper isolectin peaks. PHA, WGA, RCA, and AHA were rapidly separated into 5, 5, 4, and 6 isolectins, respectively.
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PMID:Separation of isolectins by high-performance hydrophobic interaction chromatography. 366 61

An amyloid enhancing factor (AEF) was extracted from spleens and livers of casein-treated hamsters. It shortened the induction time of experimental amyloidosis in recipient hamsters from 14 days to 4 days. Sepharose-4B gel filtration resolved the extract into 4 different fractions, with molecular weights of: higher than IO(7) (Vo-fraction), about 280 000, 59 000 and 12 000 respectively. In all 4 fractions AEF was present, indicating that AEF is probably a low molecular weight substance that easily aggregates, or associates with other compounds present in the spleen extract. AEF was precipitable at 50% ammonium sulphate saturation. On anion exchange chromatography in PBS (pH 7.2) of this precipitate, AEF was found in the fraction eluting at high NaCl concentration. This fraction did not show any relation to hamster protein AA, IgG or albumin with double immunodiffusion. Ultraviolet absorption spectrophotometry indicated nucleotide-like material, suggesting AEF to be related to nucleoproteins.
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PMID:Amyloid enhancing factor in hamster. 408 49

Thermal transition profiles were recorded for a variety of natural and synthetic DNA and double-stranded RNA preparations in the presence of tetramethylammonium (TMA+) and tetraethylammonium (TEA+) cations. Double-stranded RNAs of natural origin, with GC contents of 50% exhibited the same profiles and Tm values as native DNA containing normal bases. Hence the tetraalkylammonium cations liquidate not only the effects of base composition, and the difference in stability between A-T and A-U base pairs (further confirmed by measurements with uracil-containing DNA from phage PBS-2), but also that of the 2'OH. In the presence of TMA+ cations, there is very marked enhancement of the stability of U-U base pairs in poly(rU) and poly(Um). In 2.4 M TEA, the 1:1 complex of poly(G) with poly (C) formed readily and melted reversibly with a Tm as low as 87 degrees C. At concentrations of TMA and TEA for which dTm/dXGC = 0, the Tm values for various phage DNA preparations containing atypical bases (phages T2, T4, phi e, phi W-14, PBS-2) differ appreciably from those with 'normal bases'. Analysis of these findings indicates that the selective interaction of TMA and TEA cations with A-T base pairs occurs in the minor groove of the DNA helix. The overall results show that the action of these quaternary ammonium cations is not due exclusively to preferential binding to A-T base pairs, but must involve other factors, including modifications of solvent structure. They also underline the utility of TMA and TEA solvent systems for placing in evidence transition profiles not accessible in other solvent systems.
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PMID:The effects of tetraalkylammonium salts on helix-coil transition parameters in natural and synthetic ribo- and deoxyribo-polynucleotides. 615 17

The fluorescence emission spectra and degree of fluorescence polarization of hematoporphyrin derivative (HpD) have been investigated using HpD-containing KK-47 cells, PBS and cetyl trimethyl ammonium chloride (CTAC) micellar solutions. The fluorescence emission bands in the HpD-containing cell suspension were red-shifted and broadened as compared to those in the PBS solution. The degree of the polarization in the PBS and CTAC micellar solutions did not change with increasing incubation time, but in the cell suspension it increased temporarily and then decreased 4 h after incubation. These results suggest that HpD monomers and dimers may bind weakly to the outer cell membrane, and then slowly distribute throughout the intracellular loci in strong-binding form. In addition, the cellular uptake and/or binding loci of HpD were considered to be the mitochondria and nuclear membrane by subcellular fractionation and fluorescence microscopic studies.
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PMID:Cellular uptake of hematoporphyrin derivative in KK-47 bladder cancer cells. 623 94

The effect of prostaglandin E2 (PGE2), on the intracellular pH (pHi) in BCECF-loaded Madin Darby Canine Kidney (MDCK) cells was investigated. PGE2 elevated the pHi. Under resting conditions, pHi of MDCK cells suspended in PBS at pH 7.4 was 7.11 +/- 0.08; PGE2 increased pHi with an EC50 of 0.16 microM. PGF2 alpha elicited a similar response to PGE2, with an EC50 of 0.24 microM. Amiloride (0.4 mM) reversed the response to PGE2 (control 7.18 +/- 0.05; PGE2 7.26 +/- 0.05; after amiloride 7.18 +/- 0.05). In MDCK cells exposed to a Na(+)-free solution, alkalinization induced by this eicosanoid was blocked (Ringer-choline 7.16 +/- 0.03; PGE2 7.16 +/- 0.02). PGE2 increased by 100% the rate of recovery after an acidification pulse with ammonium chloride. In the presence of Ringer-HCO3- (pH 7.4), there was a delay in the maximal response to this prostaglandin (PBS 2.2 +/- 0.27, Ringer-bicarbonate 3.4 +/- 0.55 min) and the pHi increment was less marked than in PBS (0.09 pH units in HCO3- versus 0.16 pH units in PBS; P < 0.001). This effect of PGE2 was not blocked by 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (1.0 mM). PMA (100 nM), activator of protein kinase C, mimicked the response to PGE2, suggesting the participation of this kinase on the effect of the prostanoid. As expected, two inhibitors of protein kinase C, staurosporine and sphingosine, abolished the response to PGE2. Staurosporine (0.10 microM), an inhibitor of protein kinase C, blocked the response to PGE2 (control 7.02 +/- 0.04; PGE2 and staurosporine 7.03 +/- 0.04, n = 9, not significant). Sphingosine, another inhibitor of protein kinase C, also blocked the response to PGE2. Two analogues of cAMP did not modify the pHi. In summary, PGE2 induced an intracellular alkalinization via stimulation of a Na+/H+ exchanger, with the participation of protein kinase C, in MDCK cells.
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PMID:Induction of alkalinization in cultured renal cells (MDCK line) by prostaglandin E2. 748 Jul 99

Anti-A reagent for the detection of the relevant antigen in human red cells and saliva has been developed. The reagent is prepared by dissolution of purified Vicia villosa lectin in the serum of group AB or B diluted 8 times with PBS. This solvent appreciably improves the anti-A selectivity of lectin and is used for titration. Purification of lectin by ammonium sulfate precipitation is described. The reagent agglutinates group A red cells in the minimal lectin concentration of 2.5 to 10 micrograms/ml and does not agglutinate group 0 and B red cells in concentration 10 mg/ml. Moreover, the reagent is fit for the detection of antigen A in traces of blood and saliva by the absorption-elution method.
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PMID:[The preparation of an anti-A reagent from the lectin of hairy vetch (Vicia villosa) for detecting antigen A in human erythrocytes and saliva]. 772 54


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