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PubMed2001

Subcellular distribution and glycosylation pattern of androgen receptor from sheep omental adipose tissue.

Sex steroids are known to have an influence on the distribution, metabolism and accretion of adipose tissue. These steroids carry out their function via specific receptors. We have previously reported the presence of oestrogen and progesterone receptors in sheep adipose tissues. In this study, we have tested the subcellular distribution of androgen receptor (AR) in sheep omental adipose tissue. Subcellular fractions - microsomes, plasma membrane and nuclei-cell debris - were isolated by differential and sucrose gradient centrifugation and confirmed by electron microscopy. The AR was determined in each fraction by Western blot analyses. As anticipated, the receptor was found in the cytosolic fraction, but a high concentration was also present in the microsomal fraction, a lesser amount in the plasma membrane fraction, and only a small amount was left in the nuclei-cell debris fraction. Two minor immunostaining bands with approximate molecular weights of 250 and 140 kDa and a major band at 110 kDa were detected in the cytosolic fraction, but only the 110 kDa band was detected in the membrane fractions. A 104 kDa band was observed on occasion and believed to be a degradation product. The cytosolic isoforms were tested for sensitivity to glycosidases. This treatment resulted in a decrease in the amount of the 250 and 140 kDa bands. To substantiate that the 250 and 140 kDa isoforms were glycoproteins, the cytosolic fraction was chromatographed on Concanavalin A-Sepharose. The 110 kDa band was eluted in the 0.4 M KCl salt wash while the 250 and 140 kDa bands were eluted with alpha-methylmannoside. Treatment of the glycoprotein (alpha-methylmannoside) peak with glycosidases converted the 250 and 140 kDa bands to the 110 kDa band. These data confirm the presence of AR in subcellular fractions of adipose tissue and suggest that it exists in various glycosylated isoforms.

Adipose Tissue↗
PubMed1988

Chemical modification of surfactant protein A alters high affinity binding to rat alveolar type II cells and regulation of phospholipid secretion.

Alveolar type II cells express a high affinity receptor for pulmonary surfactant protein A (SP-A), and the interaction of SP-A with these cells leads to inhibition of surfactant lipid secretion. We have investigated the binding of native and modified forms of SP-A to isolated rat alveolar type II cells. Native and deglycosylated forms of SP-A readily competed with 125I-SP-A for cell surface binding. Alkylation of SP-A with excess iodoacetamide yielded forms of SP-A that did not inhibit surfactant lipid secretion and did not compete with 125I-SP-A for cell surface binding. Reductive methylation of SP-A with H2CO and NaCNBH3 yielded forms of SP-A with markedly reduced receptor binding activity that also exhibited significantly reduced capacity to inhibit lipid secretion. Modification of SP-A with cyclohexanedione reversibly altered cell surface binding and the activity of SP-A as an inhibitor of lipid secretion. Two monoclonal antibodies that block the function of SP-A as an inhibitor of lipid secretion completely prevented the high affinity binding of SP-A to type II cells. A monoclonal antibody that recognizes epitopes on SP-A but failed to block the inhibition of secretion also failed to completely attenuate high affinity binding to the receptor. Concanavalin A inhibits phospholipid secretion of type II cells by a mechanism that is reversed in the presence of excess alpha-methylmannoside. Concanavalin A did not block the high affinity binding of 125I-SP-A to the receptor. Neither the high affinity binding nor the inhibitor activity of SP-A was prevented by the presence of mannose or alpha-methylmannoside. The SP-A derived from humans with alveolar proteinosis is a potent inhibitor of surfactant lipid secretion but failed to completely displace 125I-SP-A binding from type II cells. From these data we conclude that: 1) cell surface binding activity of rat SP-A is directly related to its capacity to inhibit surfactant lipid secretion; 2) monoclonal antibodies directed against SP-A can be used to map binding domains for the receptor; 3) the lectin activity of SP-A against mannose ligands does not appear to be essential for cell surface binding; 4) concanavalin A does not compete with SP-A for receptor binding; and 5) the human SP-A derived from individuals with alveolar proteinosis exhibits different binding characteristics from rat SP-A.

Animals↗
PubMed1981

Lysosomal enzyme targeting. N-Acetylglucosaminylphosphotransferase selectively phosphorylates native lysosomal enzymes.

Lysosomal enzymes contain 6-phosphomannosyl moieties which mediate their translocation to lysosomes. This recognition marker is synthesized by the sequential action of UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase and alpha-N-acetylglucosaminyl phosphodiesterase. A new assay for the N-acetylglucosaminylphosphotransferase, using alpha-methylmannoside as acceptor, is presented. Using this assay, we partially purified the transferase and examined its substrate specificity. The transferase exhibited a very high affinity toward lysosomal enzymes (apparent Km values of less than 20 microM) and was greater than 100-fold more efficient (Vmax/Km) when using lysosomal enzymes as acceptors as compared to nonlysosomal glycoproteins that contain high mannose oligosaccharide units. Heat denaturation of the lysosomal enzymes resulted in the loss of acceptor activity. The model compounds alpha-methylmannoside and Man5--8GlcNAc were poor acceptors. We propose that this enzyme catalyzes the initial, determining step by which synthesized acid hydrolases are distinguished from other newly synthesized glycoproteins and thus are eventually targeted to lysosomes.

Acetylglucosaminidase↗
PubMed1980

Separation and characterization of the acid lipase and neutral esterases from human liver.

Electrophoresis of human liver homogenates followed by reaction with 4-methylumbelliferyl palmitate reveals the presence of two major electrophoretic forms with esterase (lipase) activity toward this substrate. The two enzymes were isolated and partially purified based on their solubility differences and their relative affinities for the lectin column concanavalin A-Sepharose 4B. Lipase A was particulate with an acidic pH optimum (5.2) and could be solubilized with the non-ionic surfactant Triton X-100. Lipase B was soluble and had a more neutral pH optimum (6.3--6.6). Both forms bound to immobilized concanavalin A and could be specifically eluted. Buffers containing alpha-methylmannoside eluted lipase B, and buffers with alpha-methylmannoside and Triton X-100 eluted lipase A, giving a 22- and 257-fold purification, respectively, over whole-tissue homogenates. Cholesterol oleate, trioleoylglycerol, and 4-methylumbelliferyl palmitate were substrates for solubilized lipase A. Lipase B hydrolyzed 4-methylum-belliferyl palmitate but not trioleoylglycerol or cholesterol oleate. Lipase B was more thermolabile than lipase A, and it was selectively inhibited by diethyl-p-nitrophenyl phosphate at low concentrations. We conclude that lipase A and B are distinctly different enzymes and that they are probably not related polymorphic forms of one another.

Chromatography, Affinity↗
PubMed1991

Regulation of lymphokine expression in T cell activation. I. Rapid loss of interleukin-specific RNA after removal of the stimulating signal.

Resting T lymphocytes can be induced to express a variety of lymphokines after antigenic or mitogenic stimulation. Expression is regulated both at the transcriptional level, through induction of T cell-specific DNA-binding proteins, and at the post-transcriptional level through alteration of precursors or mRNA stability. To investigate whether lymphokine expression follows a preprogrammed course after activation of T cells or whether it is dependent on the continued monitoring of activating signals, we followed the fate of interleukin (IL) 2, IL 4 and IL 2 receptor mRNA after removal of the stimulating signal concanavalin (Con A) by alpha-methylmannoside (alpha MM). IL 2 and IL 4 needed continued stimulation of the cells for RNA expression, as shown by the rapid disappearance of IL 2 and IL 4 mRNA after addition of alpha MM to stimulated cells, while IL 2 receptor mRNA which is also induced after Con A stimulation was minimally influenced. In the case of both IL no new mature mRNA was generated after removal of the stimulating signal. The T1/2 of IL 2 mRNA remained unchanged after alpha MM treatment as compared to actinomycin D treatment, while IL 4 mRNA became labilized after withdrawal of the signal.

Animals↗
PubMed1981

Commitment and proliferation kinetics of human lymphocytes stimulated in vitro: effects of alpha-MM addition and suboptimal dose on concanavalin A response.

We have examined the effect of alpha-methylmannoside (alpha-MM) addition to concanavalin A (con A)-stimulated peripheral human lymphocytes. With a previously established kinetic model, we have, from the time course of proliferation, extracted the responding clone size, rate of entry of this clone into S phase and the length of the lag period. We have studied the effect of con A dose and time of addition of alpha-MM to optimally stimulated cells on these kinetic parameters. We show that neither a low dose of con A nor an early addition of alpha-MM to optimally stimulated cells results in a change in the responding clone size. This is, all of the potentially cells appears to become "committed" to enter the cell cycle regardless of the presence of alpha-MM early in the culture or in the presence of suboptimal stimulation. However, the rate at which these committed cells enter the first S phase is a function of the dose of con A and time of addition of alpha-MM and varies over a wide range. It is the variation in this parameter that accounts for virtually all of the diminished response previously interpreted as a time-dependent irreversible commitment of mitogen-stimulated cells. The previous work using only fixed time points for measuring thymidine uptake and the concept of commitment must be reevaluated in light of the kinetic evidence presented.

Adult↗
PubMed1976

Concanavalin A perturbation of membrane enzymes of mammary gland.

The plant lectin concanavalin A (Con A) specifically inactivates the 5'-nucleotidase of a plasma membrane-enriched fraction from lactating mammary gland. The lectin also causes an activation of the membrane Mg++-ATPase, but does not affect galactosyltransferase or alkaline phosphatase. The enzyme perturbations are prevented by alpha-methylmannoside, an inhibitor of Con A binding, indicating that specific binding to carbohydrate structures rather than nonspecific protein-protein interaction is involved. Solubilization of the 5'-nucleotidase in detergents (0.2% Triton X-100 or 1% deoxycholate) does not prevent Con A inactivation, indicating that incorporation into the membrane structure is not a requirement for the Con A effect. the results suggest that Con A inactivates the 5'-nucleotidase by a direct interaction with the enzyme and that this enzyme is a Con A receptor site on the surface of mammary cells.

Adenosine Triphosphatases↗
PubMed1975

Inhibitors of the adhesiveness of enteropathogenic E. coli.

The entero-pathogenic strain of E. coli 0125: K 70 was able to adhere to washed guinea-pig erythrocytes and to cause their agglutination. Electron microscopy revealed this strain to be rich in fimbriae. They were able to cause hemagglutination by themselves, generally at protein concentration of 10 to 100 mug per ml. D-mannose and alpha-methylmannoside were able to inhibit hemagglutination by the whole bacteria or their isolated fimbriae at concentrations of 0.003 to 0.012 mg/ml. L-mannose, D-lactose, D-glucose, N-acetylglucosamine, D-galactose, N-acetyl-D-galactosamine, D-fucose, did not exert any inhibiting effect at concentrations as high as 50 mg/ml. N-acetyl-neuraminic acid was also uneffective at concentration as high as 9 mg/ml.

Animals↗
PubMed1991

Removal of the artifactual peak associated with concanavalin A crossed affinoimmunoelectrophoresis of human serum transferrin.

During the first dimension of crossed affinoimmunoelectrophoresis (CAIE) with the lectin concanavalin A (Con A), an immobile glycoprotein-Con A affinoprecipitate may form near the application well and, subsequently, produce an artifactual peak in the second-dimension gel. In this study, we examined the effects of sample glycoprotein concentration and gel Con A concentration on the magnitude of the transferrin artifactual peak present in the analysis of human serum. In addition, we examined the potential for reducing or eliminating the artifact by including a competitive inhibitor of glycoprotein-lectin interaction, alpha-methylmannoside (alpha MM), in the application well. We demonstrate that the artifact can be eliminated through an appropriate choice of glycoprotein, Con A, and alpha MM concentrations. This approach should be applicable for diagnosing and eliminating the artifact in the Con A CAIE analyses of other glycoproteins.

Artifacts↗
PubMed1984

Eosinophil-particle interactions: a model system for study of cellular adherence and activation.

In its role as an effector capable of killing large multicellular parasites, the eosinophil must be especially adapted for dealing with noningestible surfaces. A model system of Sepharose beads coated with serum protein or concanavalin A (Con A) has been used to study interactions between guinea pig peritoneal exudate eosinophils and noningestible particles. A small percentage of eosinophils were adherent to serum treated Sepharose; however, many cells were adherent to Con A-Sepharose. Adherence to Con A-Sepharose was decreased by pretreatment with 1 mM alpha-methylmannoside (alpha-MM). As compared to resting eosinophils, incubation of eosinophils with serum-treated Sepharose led to activation of oxidative metabolism as indicated by an eight-fold increase in superoxide anion production and an approximately threefold increase in quantitative leukocyte iodination. Eosinophils which were adherent to Con A beads could not be activated by either phorbol myristate acetate (PMA) or preopsonized zymosan. However, if adherence was reduced by preincubation with alpha-MM, PMA was able to activate the eosinophils. Neither soluble Con A nor Sepharose beads interfered with the assay of superoxide anion. These studies demonstrate the utility of Sepharose beads for studying interactions between eosinophils and noningestible particles.

Animals↗
PubMed1980

Inhibition of acyltransferase in lymphocytes by concanavalin A.

The effects of concanavalin A and succinylated concanavalin A on the transformation of mouse splenic lymphocytes, and on early biochemical events in the transformation, were compared. 1. The transformation of lymphocytes is biphasic with respect to concanavalin A concentration with optimal activation at about 1 microgram/ml. Activation by succinyl concanavalin A is not biphasic over a range of lectin concentration of 1--16 microgram/ml. 2. In intact lymphocytes cultured for 4 h, the enzyme Acyl-CoA:1-acylglycero-3-phosphocholine O-acyltransferase (EC 2.3.1.23) was not activated by concanavalin A but was inhibited at all concentrations tested, and was about 60% inhibited at 16 micrograms concanavalin A per ml. Succinyl concanavalin A gave little or no inhibition at similar concentrations. 3. Lymphocytes become committed to divide while their acyltransferase activities are markedly inhibited by concanavalin A. 4. The inhibition of acyltransferase by concanavalin A can be lifted by displacing the lectin from the cells by alpha-methylmannoside. Lowered enzyme activity is not caused by cell agglutination or by direct cross-linking of lectin receptors. It is unlikely that the inhibition of acyltransferase is due to indirect cross-linking via the cytoskeleton since colchicine did not reverse the inhibition. 5. The inhibition of acyltransferase and the reduced stimulation of transformation by higher levels of concanavalin A appear to be due to hydrophobic interaction of the lectin with the plasma membrane, as shown by liposome aggregation studies.

1-Acylglycerophosphocholine O-Acyltransferase↗
PubMed1991

The putative role of members of the CEA-gene family (CEA, NCA an BGP) as ligands for the bacterial colonization of different human epithelial tissues.

Immobilized purified CEA (carcinoembryonic antigen), NCA (non-specific crossreacting antigen) and BGP I (biliary glycoprotein I) bind strains of E. coli (including EPEC) and some Salmonella species (including S. typhi, S. paratyphi A + B and S. java) while Shigella-, Yersinia- and Bacteroides- strains showed no adhesion. The binding was of high avidity, heat sensitive, dose dependent, saturable and nearly completely abolished in the presence of 10 mM alpha-methylmannoside. From inhibition studies with aromatic mannose compounds, it was suggested that in contrast to Salmonella strains E. coli strains exhibit a higher hydrophobicity in the binding region adjacent to the CEA-, NCA- and BGP-binding site. By further inhibition experiments it could be demonstrated that E. coli and Salmonella strains bind to high-mannose type oligosaccharides of these molecules via lectins on bacterial type I fimbriae. We conclude that the expression of products of this gene family on different human epithelial cells (colon-, bile canaliculi, uroepithel etc.) may function as ligands for bacterial colonization of epithelial tissues.

Antigens, CD↗
PubMed2000

Concanavalin A induced apoptosis in murine macrophage PU5-1.8 cells through clustering of mitochondria and release of cytochrome c.

Concanavalin A (ConA), normally a mitogen of T-lymphocytes, was found to be a cell cycle-independent apoptosis-inducing agent in cultured murine macrophage PU5-1.8 cells. This assertion is based on the following observations: (1) ConA increased the number of cells with hypodiploid DNA in a dose dependent manner as revealed by flow cytometry; (2) ConA elicited DNA fragmentation and the cytotoxicity of ConA was suppressed by alpha-D-methylmannoside which blocks the lectin site of ConA; (3) ConA was able to release cytochrome c (cyto c) into the cytosol of PU5-1.8 cells. When isolated mitochondria were incubated with ConA, release of cyto c was observed too. Interestingly, clustering of mitochondria was found in the cytosol under a confocal microscope after ConA treatment. When cells were incubated with ConA-FITC and subsequently with mitotracker red (a probe for mitochondria), co-localization of fluorescence signals was observed. These results suggest that ConA was delivered to the mitochondria, induced mitochondrial clustering and released cyto c. Our results also show that introduction of exogenous cyto c electroporationally into ConA-untreated cells elicited DNA fragmentation. On the other hand, introduction of specific antibody against cyto c into PU5-1.8 cells suppressed the ConA-mediated cell death. Taken together, our results indicate that ConA induced apoptosis in PU5-1.8 cells through mitochondrial clustering and release of cyto c and the release of cyto c was sufficient to elicit apoptosis in PU5-1.8 cells.

Animals↗
PubMed1997

Effects of concanavalin A on chondrocyte hypertrophy and matrix calcification.

Resting chondrocytes do not usually undergo differentiation to the hypertrophic stage and calcification. However, incubating these cells with concanavalin A resulted in 10-100-fold increases in alkaline phosphatase activity, binding of 1,25(OH)2-vitamin D3, type X collagen synthesis, 45Ca incorporation into insoluble material, and calcium content. On the other hand, other lectins tested (including wheat germ agglutinin, lentil lectin, pea lectin, phytohemagglutinin-L, and phytohemagglutinin-E) marginally affected alkaline phosphatase activity, although they activate lymphocytes. Methylmannoside reversed the effect of concanavalin A on alkaline phosphatase within 48 h. Concanavalin A did not increase alkaline phosphatase activity in articular chondrocyte cultures. In resting chondrocyte cultures, succinyl concanavalin A was as potent as concanavalin A in increasing alkaline phosphatase activity, the incorporation of [35S]sulfate, D-[3H]glucosamine, and [3H]serine into proteoglycans, and the incorporation of [3H]serine into protein, although concanavalin A, but not succinyl concanavalin A, induced a rapid change in the shape of the cells from flat to spherical. These findings suggest that concanavalin A induces a switch from the resting, to the growth-plate stage, and that this action of concanavalin A is not secondary to changes in the cytoskeleton. Chondrocytes exposed to concanavalin A may be useful as a novel model of endochondral bone formation.

Alkaline Phosphatase↗
PubMed1979

Interactions between human eosinophils and schistosomula of Schistosoma mansoni. II. The mechanism of irreversible eosinophil adherence.

Previous work (1)(1) has shown that normal human eosinophils show a preferential capacity, in comparison with neutrophils, to bind to antibody- coated schistosomula of Schistosoma mansoni. This effect is attributable to a temperature-dependent function of the eosinophil which renders its binding stable and irreversible by aggregated gamma globulin or Staphylococcus aureus protein A. In contrast, the binding of neutrophils is readily reversible by these agents. It has now been shown that the differences observed between eosinophils and neutrophils is a property of their interaction with living schistosomula. When dead or artificially damaged schistosomula were tested, neutrophils showed a markedly enhanced capacity to adhere, in both the presence and absence of anti-chistosomular serum. Subsequent experiments were designed to test the hypothesis that the strong, stable binding of eosinophils was attributable to degranulation, with release of granule contents which would then serve as ligands to bind the cell to the organism. First, an enhanced adherence both of eosinophils and of neutrophils could be demonstrated in the presence of eosinophil major basic protein (MBP) or of protamine, a high molecular weight cation. Second, the binding of eosinophils induced by concanavalin A (Con A) was found to differ markedly from that induced by antischistosomular serum. Con A-mediated binding of eosinophils was fully reversible by alpha-methyl-mannoside, was not associated with damage to the organism, and did not lead to degranulation of the cell, as estimated by measuring the release of MBP into the culture supernate. However, induction of degranulation of concanavalin A-bound eosinophils, but not of neutrophils, with the calcium ionophore A23187 converted the reaction into one which was no longer reversible by alpha- methylmannoside and in which damage to the organism now did occur. These findings support the hypothesis that the stable binding of eosinophils is associated with degranulation, a process which may contribute to the preferential capacity of this cell to mediate antibody-dependent damage to schistosomula.

Antibodies↗
PubMed1982

Attachment and ingestion of bacteria by trophozoites of Entamoeba histolytica.

Entamoeba histolytica trophozoites were found to be very selective in their interactions with bacteria. Two principal mechanisms were shown to be responsible for these interactions. Certain bacteria, such as a number of Escherichia coli and Serratia marcescens strains which are known to contain mannose-binding components on their cell surface, bound to mannose receptors on the amoeba membrane. This attachment was markedly inhibited by alpha-methylmannoside (0.5%), especially when the incubations were done at low temperature (5 degrees C). Other bacterial species, such as Shigella flexneri and Staphylococcus aureus, which do not possess a mannose-binding capacity, attached to the amoebae, but only with the aid of concanavalin A or after opsonization of the bacteria with immune serum. In both types of attachment, between 40 and 100 bacteria bound per amoeba, and considerable ingestion of bacteria into amoeba vacuoles was observed at 37 degrees C. The attachment of opsonized bacteria to the amoebae does not appear to be mediated by Fc receptors since Fab' dimers obtained after pepsin digestion of immunoglobulin were capable of mediating adherence. Furthermore, preincubation of the amoebae with aggregated human immunoglobulin G or with heat-inactivated immune serum and EDTA did not inhibit the attachment of opsonized bacteria. The attachment of opsonized bacteria was markedly inhibited by N-acetylglucosamine-containing glycoconjugates, such as peptidoglycan and chitin oligosaccharides, as well as by N-acetylgalactosamine. These results indicate that amoebae can attach and ingest bacteria either by using their membrane-associated carbohydrate-binding protein or by having their mannose-containing cell surface components serve as receptors.

Animals↗
PubMed1985

Lysosomal enzyme phosphorylation in human fibroblasts. Kinetic parameters offer a biochemical rationale for two distinct defects in the uridine diphospho-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase.

The primary genetic defect in the lysosomal storage disease mucolipidosis III (ML III) is in the enzyme uridine diphospho-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase. This enzyme has two well-defined functions: specific recognition of lysosomal enzymes (recognition function) and phosphorylation of their oligosaccharides (catalytic function). Using fibroblasts from patients with ML III as the source of enzyme, and alpha-methylmannoside and two lysosomal enzymes as the substrates, we have identified defects in both of these functions. In one group of fibroblasts, the catalytic activity of the N-acetylglucosaminylphosphotransferase is decreased while the ability to recognize lysosomal enzymes as specific substrates remains intact. In the second group of fibroblasts, the ability to recognize lysosomal enzymes is impaired while the catalytic activity of the enzyme is normal. These data provide a biochemical rationale for the previously described genetic heterogeneity among patients with ML III (Honey, N. K., O. T. Mueller, L. E. Little, A. L. Miller, and T. B. Shows, 1982, Proc. Natl. Acad. Sci. USA., 79:7420-7424).

Acid Phosphatase↗
PubMed1975

[Adherence of pathogenic Escherichia coli to epithelial cells isolated from the intestinal mucosa of the rabbit, inhibiting effect of hyperimmune bovine colostrum and of various carbohydrates (author's transl)].

In order to study the mode of action of a bovine anti-Escherichia coli lactoserum (BLS), we have used a new test measuring the adherence of pathogenic E. coli on epithelial cells isolated from the small intestine of rabbit. A mixed suspension of E. coli and of epithelial cells is incubated for 15 min and the number of bacteria adhering to the cells counted under the microscope. The BLS at a concentration of 3.5 mg/ml IgG is able to reduce this number by a factor of 3-5. After absorption of the BLS with formaldehyde-treated bacteria, this factor is smaller than 2. At a concentration of 5 mg/ml, D-mannose and alpha-methylmannoside are as efficient inhibitors of adherence as BLS; at the same concentration, L-mannose is ineffective. The cultures of E. coli strongly agglutinating guinea pig erythrocytes, adhere to a larger extent to the epithelial cells. The last two observations confirm the important role played by fimbriae for the adhesive properties of E. coli. The presence of fimbrial antibodies would partially explain the inhibiting effect of BLS on adherence.

Animals↗