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)

Purified and desialylated glycoprotein M from human O erythrocytes precipitates with B and H specific lectin from Evonymous europaeus seeds, both in PBS and 0.2% Triton X-100. Desialylated, N-terminal fragment (MT-1) obtained by trypsin digestion of M glycoprotein does not precipitate with Evonymous lectin but inhibits precipitation.
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PMID:Localization and immunochemical characterization of the lectin Evonymous europaeus receptor site on the glycoprotein from human O erythrocytes. 74 64

Wistar rats were fed a normal protein (25% casein) or an isoenergetic low protein (8% casein) diet from the day of giving birth until pups were weaned. Some litters were killed at weaning; others (both normal and malnourished animals) received the 25% protein diet until d 90 when they were killed. Intermediate filament (IF) preparations were obtained by extraction of the cerebral cortex with a high salt PBS solution containing 1% Triton X-100. The pellet contained the bulk of the cytoskeleton proteins from tissue, identified as the 150- and 68-kDa subunits of neurofilaments (NF-M and NF-L, respectively), the 66-kDa associated protein, the 57-kDa intermediate filament-like protein, and the 50-kDa glial fibrillary acidic protein. Intermediate filament-enriched fractions from control and malnourished rats at both d 21 and 90 were scanned following two-dimensional gel electrophoresis to determine the effects of postnatal malnutrition on the intermediate filament protein content. The results indicated that postnatal malnutrition imposed during the brain growth spurt period did not alter the expression of IF proteins of the cerebral cortex in 21-d-old rats, but increased the expression of NF-L and NF-M proteins in adult rats.
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PMID:Malnutrition induces an increase in intermediate filament protein content of rat cerebral cortex. 190 92

A modification of the in vitro immobilization assay together with freeze-fracture analysis was used to determine the factors responsible for the prolonged time required in vitro to achieve killing of Treponema pallidum subsp. pallidum. The modified immobilization assay permitted separate determination of the time required for binding of antibody to the surface of T. pallidum and for C activation. Treponemes were preincubated in heat-inactivated immune rabbit serum (IRS) followed by washing the organisms in 2.5% BSA/PBS to remove unbound IRS antibody before the addition of C. The results showed that a comparable degree of C-dependent killing occurred when treponemes were preincubated in heat-inactivated IRS for either 30 min or 16 h, indicating that treponemicidal antibody rapidly binds to the surface of T. pallidum. Preincubation of treponemes for 17 h in heat-inactivated IRS followed by a 1-h incubation in C resulted in the loss of 80% treponemal motility, indicating that C activation results in rapid killing of T. pallidum. Treponemes preincubated in IRS for 1 h, then incubated for 8 h and 16 h in heat-inactivated normal serum also lost a significant level of motility after the addition of C; in contrast, motility was unaffected after 30 min and 4 h of incubation in heat-inactivated normal serum under similar conditions. These results demonstrate that, whereas antibody binding to and C-mediated killing of treponemes can proceed rapidly, the prolonged time to C activation limits the rate at which treponemicidal activity occurs in vitro. In addition, treponemicidal activity using the modified immobilization assay could not be demonstrated with antiserum against T. pallidum endoflagella, antiserum against proteins solubilized from T. pallidum using the detergent Triton X-114, and a mAb to the T. pallidum r190-kDa "4D" protein, suggesting that these molecules are not accessible to surface binding antibody. Freeze-fracture analysis, recently used in our laboratory to demonstrate that the outer membrane of T. pallidum has rare constituent protein, was utilized to demonstrate outer membrane target Ag of IRS antibody. T. pallidum rare outer membrane protein (TROMP) molecules were shown in freeze-fracture electron micrographs to be consistently aggregated following a 16-h incubation of treponemes in IRS. In contrast, no aggregation of TROMP was present in treponemes incubated in normal rabbit serum for 16 h or in treponemes incubated in IRS for 2 h. These findings suggest that the rate of C activation leading to in vitro treponemicidal activity is limited by the time required for aggregation of antibody-bound TROMP molecules.
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PMID:Complement activation limits the rate of in vitro treponemicidal activity and correlates with antibody-mediated aggregation of Treponema pallidum rare outer membrane protein. 240 84

The actions of 1,25-dihydroxyvitamin D3 [1,25-(OH)2D3] are thought to be mediated through receptor proteins which have been described in a variety of avian and mammalian tissues, but not in the liver. To determine if a binding protein for 1,25-(OH)2D3 is present in this tissue, rat liver was homogenized in a low ionic strength buffer containing 10 mM Tris (pH 7.4), 2.2 m sucrose, 3 mM calcium chloride, 0.2% Triton X-100, and 0.04% Trasylol (sucrose buffer) and centrifuged over a 10-ml cushion of sucrose buffer at 61,000 x g for 80 min at 4 C. The resultant nuclear pellet was extracted in a 26 mM Tris (pH 7.4) buffer containing 0.3 M potassium chloride, 5 mM dithiothreitol, 1 mM EDTA, and 10 mM sodium molybdate. Saturable 1,25-(OH)2D3 binding was identified in high salt extracts of rat liver nuclei and was eliminated by treatment with trypsin. This liver binding protein cosediments on high salt 5-20% sucrose density gradients with the 1,25-(OH)2D3 receptor protein from intestine and is distinct from the 6.OS tissue binding protein for 25-hydroxyvitamin D3. Perfusion of rat liver with PBS to remove receptor-positive blood cells before isolation of the nuclei did not change 1,25-(OH)2D3 binding. The nuclear protein bound 1,25-(OH)2D3 more avidly than either 24,25-(OH)2 D3 or 25-hydroxyvitamin D3. Saturation analysis of 1,25-(OH)2D3 binding revealed an apparent equilibrium dissociation constant of 20.6 +/- 2.2 pM (mean +/- SEM) at 4 C and a maximum binding capacity of 49.0 +/- 14.6 fmol/extract from 1.0 mg DNA. The 1,25-(OH)2D3-binding binding protein was present in liver nuclei isolated from mice, rabbits, and chicks and in nuclei isolated from cultured rat hepatocytes. The ligand specificity, sedimentation coefficient, limited binding capacity, trypsin sensitivity, and nuclear location of the hepatic 1,25-(OH)2D3-binding protein are similar to those of 1,25-(OH)2D3 receptors described in other tissues and suggest that the liver may be a target organ for [1,25-(OH)2D3] action.
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PMID:A 1,25-dihydroxyvitamin D3 receptor-like protein in mammalian and avian liver nuclei. 283 67

We have solubilized and reassembled the peripheral-type benzodiazepine receptor, a component of the mitochondrial outer membrane, from rat adrenal gland mitochondria. The ligand binding site of this receptor undergoes denaturation during solubilization in digitonin, Triton X-100, or 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate at detergent concentrations above 0.1%, which is evident from the loss of high-affinity binding of [3H]PK11195, a ligand selective for the mitochondrial benzodiazepine receptor. The conformation of the binding site for PK11195 can be stabilized during solubilization in sodium cholate by relatively low concentrations of supplementary soybean lipid. Drug displacement studies demonstrate that the pharmacological properties of the receptor are preserved under these conditions. Electron micrographs of the solubilized preparation show a heterogeneous population of many small particles (less than 100 A) and some larger membranous aggregates (up to 500 A). Sucrose gradient centrifugation indicates that these lipoprotein complexes are of high buoyant density. They can be incorporated in liposomes via cholate dialysis in the presence of additional supplementary lipid. The behavior of the mitochondrial benzodiazepine receptor during solubilization and reassembly suggests that it is an integral protein of the outer membrane.
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PMID:Solubilization and reassembly of the mitochondrial benzodiazepine receptor. 301 Oct 77

F-actin has been identified in the preprophase band of Allium cepa. Cells attached to subbed slides were obtained from formaldehyde-fixed root tips digested in EGTA and Cellulysin. The air-dried cells were extracted in Triton X-100, treated with rhodamine-phalloidin, rinsed briefly in PBS, and viewed in the fluorescence microscope. Interphase cells contain a network of actin fibers that extends into all areas of the cytoplasm. During preprophase, the network is replaced by a band of fibers aligned in the position of the preprophase band. Colocalization of F-actin with rhodamine-phalloidin and microtubules with tubulin immunocytochemistry confirms that the two bands are coincident. The actin appears to comprise a thin layer of fibers next to the plasmalemma. Like the microtubule preprophase band, the actin band narrows as preprophase progresses and disappears by midprophase. Fluorescent actin bands are not seen in fixed cells pretreated with excess unlabeled phalloidin before staining. They are also absent in roots exposed to cytochalasins B and D before fixation, but preprophase band microtubules at all stages of aggregation are still present. Colchicine treatment leads to the loss of both preprophase band microtubules and actin. The possible function of preprophase band actin is discussed.
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PMID:Actin in the preprophase band of Allium cepa. 329 55

Using a monospecific, monoclonal antibody against the glucocorticoid receptor (GR), an immunocytochemical study was performed to investigate the intracellular localization of GR both in the presence or absence of ligand. With all fixation methods tested (paraformaldehyde, acetic acid in ethanol, Bouin's fixative, and bensochinone in PBS), it was possible to obtain specific GR staining. Fixation with paraformaldehyde was chosen for further studies on the effect of permeabilization, using several concentrations of Triton X-100 or saponin. A rat Rueber hepatoma (H-4-II-E) and a human uterus carcinoma (NHIK 3025) cell line were used as well as cultured hepatocytes from normal rat. The accessibility of the different cell compartments after fixation and permeabilization was tested for by using antibodies against cellular constituents with known locations (i.e. core-nucleosome proteins and tubulin), in combination with the anti-GR antibody in double immunofluorescence staining experiments. The specific GR stain obtained with the indirect peroxidase antiperoxidase technique or with fluorescein isothiocyanate-labeled second antibodies was shown to be present both in the cytoplasm and in the nucleus. Staining of all cellular compartments was abolished (peroxidase antiperoxidase) or diminished (fluorescein isothiocyanate) if the monoclonal antibody was preincubated with a 90% pure GR preparation. These findings are in contrast to recently reported immunocytochemical studies, where a strict nuclear existence of the estrogen and progestin receptors has been reported. Consequently, generalizations with regard to steroid receptor localization cannot be made. Furthermore, an in vitro model is described, where the effect of dexamethasone administration upon the localization of receptor staining in H-4-II-E cells can be studied.
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PMID:Intracellular localization of the glucocorticoid receptor: evidence for cytoplasmic and nuclear localization. 354 55

Concanavalin A (Con A)-induced anchorage of the major cell surface sialoglycoprotein component complex (ASGP-1/ASGP-2) was studied in 13762 rat mammary adenocarcinoma sublines with mobile (MAT-B1 subline) and immobile (MAT-C1 subline) cell surface Con A receptors. Treatment of cells, isolated microvilli, or microvillar membranes with Con A resulted in marked retention of ASGP-1 and ASGP-2, a Con A-binding protein, in cytoskeletal residues of both sublines obtained by extraction with Triton X-100 in PBS. When Con A-treated microvillar membranes were extracted with a buffer containing Triton X-100, the sialoglycoprotein complex was found associated in the residues with a transmembrane complex composed of actin, a 58,000-dalton polypeptide, and a cytoskeleton-associated glycoprotein (CAG), also a Con A-binding protein, in MAT-C1 membranes, and of actin and CAG in MAT-B1 membranes. Untreated membrane Triton residues retained very little ASGP-1/ASGP-2 complex. Association of the sialoglycomembrane complex and the transmembrane complex was also demonstrated in Con A-treated, but not untreated, microvilli by their comigration on CsCl gradients. Association of both complexes with the cytoskeleton of microvilli was shown by sucrose density gradient centrifugation. A fraction of the polymerized actin comigrated with the transmembrane complex alone in the absence of Con A and with both the transmembrane complex and the sialoglycoprotein complex in the presence of Con A. From these results we propose that anchorage of the sialoglycoprotein complex to the cytoskeleton on Con A treatment occurs by cross-linking ASGP-2, the major cell surface Con A-binding component, to CAG of the transmembrane complex, which is natively linked to the cytoskeleton via its actin component. Since Con A-induced anchorage occurs in sublines with mobile and immobile receptors, the anchorage process cannot be responsible for the differences in receptor mobility between the sublines.
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PMID:Mechanism of concanavalin A-induced anchorage of the major cell surface glycoproteins to the submembrane cytoskeleton in 13762 ascites mammary adenocarcinoma cells. 653 71

Bullous pemphigoid antigen (BP Ag) is a cell surface marker of epidermal basal cells. The functional role of this molecule is unknown. Epidermal cell suspensions obtained by trypsinization of skin show a population of epidermal basal cells with a polar rim of antigen as demonstrated by indirect immunofluorescence technique. This study shows that treatment of these cells suspensions with a variety of proteolytic and glycosidic enzymes failed to remove the antigen from these basal cells. BP Ag was also stable upon incubation with distilled water, Triton X-100, PBS, and 1 M NaCl. Treatment of epidermal basal cells with 2 N NaSCN, 1% periodic acid, and 4 M urea, as well as acidic pH or 56 degrees C temperature, abolished the reactivity of these cells with BP antibodies.
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PMID:Some biochemical properties of pemphigoid antigen bound to the surface of dissociated epidermal basal cells. 701 11

Nerve growth factor (NGF) was recently found to be largely associated with sedimentable fractions of adult rat brain and treatments of the fractions by alkaline pH increased the measurable amount of their NGF antigen as well as its solubilization [M.C. Hoener, E. Hewitt, J.M. Conner, J.W. Costello and S. Varon, Nerve growth factor (NGF) content in adult rat brain tissues is several-fold higher than generally reported and is largely associated with sedimentable fractions, Brain Res., 728 (1996) 47-56; M.C. Hoener and S. Varon, Effects of sodium chloride, Triton X-100, and alkaline pH on the measurable contents and sedimentability of the nerve growth factor (NGF) antigen in adult rat hippocampal tissue extracts, J. Neurosci. Res., in press (1997); C. Zettler, D.C.McL. Bridges, X.-F. Zhou and R.A. Rush, Detection of increased tissue concentrations of nerve growth factor with improved extraction procedure, J. Neurosci. Res., 46 (1996) 581-594]. We have further investigated the reversibility of these pH effects. Reversal of the pH of an adult rat hippocampal tissue extract from 10.5 to 7.4 led to an almost complete transfer of NGF back from nonsedimentable to sedimentable fractions and to a remasking of the previously unmasked portion of NGF antigen. Thus, molecules causing masking and sedimentation of NGF at pH 7.4 were likely to be present in the alkaline extract. A gel filtration column in PBS, pH 10.5 was used to separate such putative binding molecules from the NGF. All of the NGF antigen from rat hippocampal alkaline extract was found to elute with 19 kDa fractions. The same apparent molecular weight was found for mouse submaxillary beta-NGF and recombinant human beta-NGF. Masking and sedimentation no longer occurred when newly generated 19 kDa rat brain NGF was returned to pH 7.4. When high molecular weight fractions derived from the same gel filtration (in PBS, pH 10.5) were added back to the 19 kDa NGF pool at pH 7.4 and the mixture incubated and centrifuged, the measurability of 19 kDa rat brain NGF antigen was markedly reduced and half of the antigen was recovered in sedimentable fractions. Similar but less dramatic results were obtained when mixing the same high molecular weight fractions with 19 kDa mouse or human beta-NGF. These findings provide new opportunities to identify molecules to which NGF may be bound within intact brain tissues.
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PMID:Reversible sedimentation and masking of nerve growth factor (NGF) antigen by high molecular weight fractions from rat brain. 940 49


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