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PubMed1963

GROWTH INHIBITORY PROPERTIES OF MYCOPLASMA ANTIBODY.

Bailey, Jack S. (The George Washington University, Washington, D.C.), Harold W. Clark, William R. Felts, and Thomas McP. Brown. Growth inhibitory properties of Mycoplasma antibody. J. Bacteriol. 86:147-150. 1963.-A substance in antiserum responsible for growth inhibition of Mycoplasma was found to be associated with the water-insoluble globulin fraction. This fraction and the agglutinins removed from agglutinated antigen inhibited the growth of Mycoplasma in a similar manner. Sonic oscillation of antiserum broth cultures partially relieved the growth inhibition. The results of this study suggest the existence of neutralized Mycoplasma in a latent phase, which could explain their infrequent detection in tissues and fluids. The application of such techniques as sonic oscillation may improve the recovery and identification of Mycoplasma from these sources.

Antibodies↗
PubMed1997

[An importance of colloid chemical characterization of liposomes for DDS in a large scale production].

Efficacy and safety data of liposomal drugs in a laboratory environment are often not reproduced on an industrial production scale. This is largely due to the fact that the colloid-chemical properties of the liposomes manufactured on a small scale are not reproduced in large scale production. Though the size and the electric charge of liposomes are measured and are adequately specified in relation to the bio-distributions in most developments of liposomes (1), uniformity of lipid components, exposure of bio-chemically important functional groups on the outer surface of liposomes (2), fixed aqueous layer thickness (FALT), number of the lipid bilayers, etc., are dependent upon the scale of production. Nevertheless these properties are not always exactly specified. Uniformity, especially of the functional groups on the membrane surface can be assessed chemically or bio-chemically with fractionated samples, and FALT can be easily determined through electro-chemical means (3). In this review, colloid chemical characterization of liposomes is introduced, FALT as an example, and its importance in a quality control of a liposomal product in an industrial scale production is shown. Methoxy-polyethyleneglycol-diacylglycerol (PEG-DAG) with varying PEG chain length and acyl chains were synthesized, FALT of liposomes coated with PEG-DAG determined and tissue distribution in tumor bearing mice. The higher incorporation ratio of PEG-DAG into liposomal membrane was observed with PEG-DAG with short acyl chains (myristoyl) and a small PEG molecular weight (1000). The easier to incorporate, the easier to be stripped in the serum. The disposition data in the rats well reflected the colloid chemical and in vitro data of the PEG liposomes. Galactosyl-carbonyl-propionyl-polyethyleneglycol-diacylglycerol (Gal-PEG-DAG) with oxyethylene number, n = 10, 20 and 40 were synthesized. The exposure of the galactose residue beyond the fixed aqueous layer of liposomes coated with Gal-PEG-DAG was monitored by a lectin, Ricinus communis agglutinin (RCA) induced agglutination, the half life in the blood after i.v. injection into rats, organ distribution determined and intrahepatic distribution studied. Only the liposomes containing the Gal-PEG10-DAG aggregated with the lectin, indicating that only with this derivative the galactose group was adequately exposed. The Gal-PEG10-DAG liposomes were cleared from the plasma with a half life of 0.3 h. The plasma elimination could be attributed entirely to increased uptake by the liver. The increased liver uptake was almost entirely attributed to increased uptake by the non-parenchymal cell. Incorporation of PEG-DSPE in to the Gal-PEG10-DAG liposomes caused 1) a three-fold increase in blood circulation time, 2) a small but significant decrease in hepatic uptake after 20 h and 3) a significant shift in intrahepatic distribution in favor of the hepatocytes, comparable to that of the control liposomes. In conclusion, therapeutic efficacy and safety of liposomes can be controlled by their colloid chemical, more exactly, surface chemical properties. By setting up reasonable quality control specification of the properties in laboratory and examining the specifications satisfied in upscaling, the efficacy and safety are reproduced in a large scale product.

Animals↗
PubMed1992

Enhancement of T-cell-depleted bone marrow allografts in the absence of graft-versus-host disease is mediated by CD8+ CD4- and not by CD8- CD4+ thymocytes.

Transplantation of T-cell-depleted C57BL/6-Nu/Nu ("nude") bone marrow (BM) into C3H/HeJ recipients, conditioned with 8 Gy total body irradiation plus chemotherapy with the myeloablative drug dimethyl myleran, resulted in poor hematopoietic reconstitution 14 days posttransplant, compared with transplantation with T-cell-depleted BM from normal C57BL/6 donors. Hematopoietic reconstitution of "nude" BM could be improved by the addition of (C57BL/6xC3H/HeJ)F1 thymocytes void of graft-versus-host activity. Enhancement of BM allografting by thymocytes is sensitive to low radiation doses (> or = 5.0 Gy) and can be achieved by transplanting the BM 24 hours before the administration of thymocytes. Fractionation of F1 thymocytes by differential agglutination with peanut agglutinin (PNA) and by fluorescence activated cell sorting showed that this hematopoietic enhancing activity is enriched in the unagglutinated (PNA-) thymocyte fraction and is mediated by PNA- CD8+ and not by PNA- CD4+ thymocytes.

Animals↗
PubMed1990

Evidence that appearance of thymulin in plasma follows lymphoid chimerism and precedes development of immunity in patients with lethal combined immunodeficiency transplanted with T cell-depleted haploidentical marrow.

Thymulin, a peptide secreted by human thymic epithelial cells, circulates in peripheral blood. Levels of plasma thymulin (FTS-Zn) activity were analyzed in 21 patients with lethal combined immunodeficiency disorders who were treated with transplantation of HLA-haplotype-mismatched parental bone marrow depleted of T cells by differential agglutination with soybean agglutinin and E-rosetting (SBA-E-BMT). Among these 21 infants, 15 were patients with severe combined immunodeficiency (SCID) and 6 had combined immunodeficiency (CID) with Omenn's syndrome or CID with T cell predominance (CIDTP). In contrast to normal infants who possess high levels of plasma thymulin activity, 20 of the 21 patients demonstrated undetectable or low plasma thymulin levels for their age at admission prior to transplantation. Following SBA-E-BMT, however, thymulin became detectable in the plasma of 17 of 18 evaluable patients and reached normal or near-normal levels between 21 and 125 days posttransplant. In patients in whom the timing of engraftment could be established by emergence of donor lymphocytes, thymulin appeared in the plasma at approximately the same time as lymphoid chimerism was detected, and in all patients who were engrafted and immunologically reconstituted, the increment in thymulin levels preceded development of immune functions. These studies support the concept that normal marrow-derived cells in the graft can provide a stimulus necessary for induction of thymic epithelial secretory function in patients with thymic dysplasia. Further, immunologic reconstitution in these patients was not seen following SBA-E-BMT unless and until recovery of thymus function had been observed.

Bone Marrow Transplantation↗
PubMed1985

Activity of ecto-ATPase in different populations of mouse and rat lymphocytes.

Mouse and rat lymphocytes showed different activities of ecto-ATPase in dependence on animal species and cell population. Compared with the total thymocyte population glucocorticoid resistant thymocytes exhibited a higher ecto-ATPase activity. The activity of ecto-ATPase was lower in immature mouse thymocytes separated by agglutination with peanut agglutinin than in mature thymocytes. T-lymphocytes of rat mesenteric lymph nodes and glucocorticoid resistant thymocytes showed the same ecto-ATPase activity. These findings indicate that the ecto-ATPase activity in mouse and rat thymocytes is related to the maturation of the cells.

Adenosine Triphosphatases↗
PubMed1987

The generation of infective stage Leishmania major promastigotes is associated with the cell-surface expression and release of a developmentally regulated glycolipid.

A monoclonal antibody, 3F12, was generated which reacted specifically against infective or metacyclic stage Leishmania major promastigotes, but not with noninfective promastigotes obtained from log phase cultures. The antibody recognized a cell surface and released molecule that could be metabolically labeled with [14C]glucose, [3H]mannose, [3H]galactose, and [3H]palmitic acid, but not with [35S]methionine or [3H]leucine. The molecule was the major species surface-labeled by [3H]sodium borohydride after periodate treatment. The glycolipid appeared to be shed primarily as free carbohydrate because 70% of the released material partitioned in the aqueous fraction after phase separation in TX-114. The molecule could be distinguished from the L. major glycolipid which has already been extensively described because its migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis was of higher relative m.w. However, a close relationship between the two molecules was indicated by the finding that another monoclonal antibody, WIC-79.3, recognized both forms of the glycolipid; one produced and released only by log phase promastigotes, and one produced and released only by metacyclic promastigotes. The loss of agglutination with peanut agglutinin which has been shown to accompany metacyclogenesis was found to be caused by the loss of expression of the log form of the glycolipid which in most cases appeared to be the result of the developmental modification of this molecule. A survey of a number of virulent and avirulent. L. major strains and clones reinforced an absolute association between the ability of these promastigotes to initiate infection in BALB/c mice and their expression and release of the 3F12-binding, developmentally regulated form of the glycolipid. Not only does this glycolipid serve as the first well defined molecular marker for infective stage metacyclic promastigotes, but its unique structure is very likely to contribute to the adaptive changes that allow these parasites to survive within the vertebrate host.

Animals↗
PubMed1984

[T-cell lymphomagenesis induced by chemical carcinogens in mice].

Investigations were performed on models of murine leukemogenesis induced by butylnitrosourea or methylnitrosourea in DBA/2, C57B1/6, NMRI, BDF and CBA mice. The latency period in CBA mice was longer than in mice of the other strains. The first transplantable cells appeared mostly in the thymus, and only in two cases in the bone marrow. Methylnitrosourea suppressed the activity of natural killer cells, but not to the same extent as leukemogenic irradiation. Heterogeneity of leukemic T-cell phenotypes with respect to the expression of the ly-1 and ly-2 antigens was detected. At the same time leukemic cells revealed consistent inability to be agglutinated by peanut agglutinine. When hydrocortisone was injected to mice after the carcinogene treatment or within 24 h before it, the leukemogenesis was delayed.

Animals↗
PubMed1984

A novel differentiation antigen on proliferating murine thymocytes identified by a rat monoclonal antibody.

A surface antigen on the mouse lymphoma cell line EL-4 has been identified by a rat monoclonal antibody. The antigen, YE1/7.1, is strongly expressed on at least two other T lymphoma cell lines, BW5147 and MBL-2, but not on several Thy-1-lymphoid cell lines. This antigen is not significantly expressed on normal adult thymocytes, spleen cells, bone marrow cells, or mitogen-activated T and B cells as tested by radioimmunoassay or fluorescence analysis using flow cytometry. Whether a small number (up to 5%) of very weakly positive cells in Con A-stimulated spleen cell populations represent a unique subpopulation is unknown. This antigen is, however, demonstrable on a subpopulation of fetal thymocytes as well as on mitogen-activated adult thymocytes. When adult thymocytes are separated by agglutination with peanut agglutinin (PNA) into PNA+ and PNA-, and stimulated with Con A in the presence of Con A culture supernatant, YE1/7.1 antigen is expressed on the majority of stimulated PNA+ cells but only weakly on a small proportion of PNA- cells. It therefore seems likely that the YE1/7.1 is a differentiation antigen expressed on a population of proliferating immature thymocytes. Immunoprecipitation of the antigen from the surface of iodinated EL-4 cells shows it to have an apparent m.w. of 60,000 under reducing and nonreducing conditions.

Aging↗
PubMed1983

The effect of temperature on the activation of thymocytes by interleukins I and II.

Endogenous pyrogen (EP) and interleukin (IL 1) appear to be closely related or identical. We therefore conducted experiments to test whether the central action of EP (fever) enhanced its local action (potentiation of immune responses). We found that 3H-TdR incorporation by thymocytes stimulated with IL 1 in the presence of 5 micrograms/ml of phytohemagglutinin (PHA) was strongly enhanced by small rises of temperature in the 32 to 38 degrees C range. Responses at 40 degrees C were generally less than those seen at 38 degrees C. Calculated values for the temperature coefficient (Q10) of the PHA-facilitated response to IL 1 varied between 50 and 300 in different experiments. Thymocytes had a variable response to IL 1 in the absence of PHA. However, thymocytes that failed to agglutinate with peanut agglutinin responded consistently to IL 1 alone, and these mitogenic responses were strongly temperature sensitive (Q10, 50 to 100 in different experiments). Thymocyte responses to 5 micrograms/ml PHA were only modestly sensitive to temperature (Q10, 3 to 8), and responses to interleukin 2 gave Q10 values of 3 to 24, with a mean of about 9. The responses of CTL cells to IL 2 were also modestly enhanced by small increases of temperature, and calculated Q10 values were similar to those observed for thymocytes. IL 1 production by macrophages was also not greatly enhanced by temperature (Q10, 2 to 5). These observations suggest that small increases of temperature enhance IL 1 activity to a much greater degree than they enhance the activity of other components of the immune response. This may help to explain the conservation of two such apparently disparate activities as EP and IL 1 in the same molecules.

Animals↗
PubMed1983

Characterization of the target cell for a thymocyte specific growth factor in guinea pigs.

A growth factor prepared from calf thymus has been described previously (Thymus 3, 289, 1981). The factor was shown to stimulate the DNA synthesis in thymic cells but not in peripheral lymphocytes in guinea pigs. We now present a further analysis of the target cell. Thymus cells were fractionated into subpopulations based on their different adherence to plastic, buoyant density and agglutinability by peanut agglutinin (PNA) and the influence of the growth factor on DNA synthesis was studied. The results showed that the responding cell was enriched in the population of non-adherent PNA-positive (PNA +) cells of low buoyant density. This cell population showed high spontaneous DNA synthesis in vitro, but did not contain the phytohemagglutinin-responsive thymocyte, which resided in the PNA-negative (PNA -) population of low density. The results strongly indicated that the target cell of the thymic growth factor is the immunologically immature proliferating thymocyte of the thymic cortex.

Animals↗
PubMed1981

[Relation between the dietary proteins in animal feed and agglutinin formation in chickens infected with Salmonella gallinarum pullorum].

Experiments were carried out with birds of the Leghorn and Cornish breeds, aged 2, 45, and 120 days and divided into two groups: I--birds given standard mixtures, and II--birds fed mixtures with a higher content of proteins. Both groups were infected with Salmonella gallinarum pullorum. At given intervals of time after that the chickens were bled, and their agglutinin titer was determined by the agglutination reaction. It was found that agglutinin production in all birds correlated with the amount of proteins in the feed. Lower amounts of proteins in the diet led to delayed agglutinin production in the infected birds. The agglutinin titers were shown to be considerably lower than those in birds given a normal ration. This was better expressed with Cornish birds. Birds at the age of 45 days proved to particularly sensitive to the fluctuations in the level of dietary proteins.

Agglutinins↗
PubMed1983

Actinomyces viscosus and Actinomyces naeslundii agglutinins in human saliva.

The objectives were to determine the degree of Actinomyces agglutinating activity in human saliva and to begin characterizing the agglutination mechanism. Agglutination titres of whole saliva collected from adults and 6-yr-old children were compared. Titres for A. naeslundii were always higher than for A. viscosus. The mean A. naeslundii titre for the adults' and children's samples were equivalent. The children had a slightly lower mean titre than the adults for A. viscosus. No correlation was found between IgA concentrations and agglutination titre. Agglutinating activity was partially impaired by incubation with anti-IgA serum. Activity in submandibular/sublingual saliva was resistant to heat at 56 degrees C but sensitive to boiling. Boiling the bacteria had no effect. In sugar inhibition tests, only galactosides (beta-Gal) and glucosamine (for A. viscosus) affected Actinomyces agglutination but impairment was only temporary. Agglutinating activity was diminished by incubating saliva with hydroxyapatite. Thus, Actinomyces agglutinins 1) are probably distinct from IgA but may complex with it; 2) may include both beta-Gal and higher affinity sites; and 3) may contribute to salivary pellicle.

Actinomyces↗
PubMed1973

Transformation of neuraminidase-treated lymphocytes by soybean agglutinin.

Transformation of mouse-spleen lymphocytes in the presence of soybean agglutinin is markedly enhanced after their treatment with neuraminidase (EC 3.2.1.18). Incubation of the cells with the enzyme also facilitates their agglutination by the lectin. The soybean agglutinin-induced agglutination and transformation is inhibited specifically by N-acetyl-D-galactosamine. New specific binding sites for soybean agglutinin were shown to appear after neuraminidase treatment. It is postulated that the transformation of neuraminidase-treated mouse-spleen lymphocytes induced by soybean agglutinin is caused by the binding of the lectin to galactosyl residues exposed by the action of neuraminidase on the cell membrane.

Animals↗
PubMedDate not supplied

Binding of lectins to culture and vector forms of Trypanosoma rangeli Tejera, 1920 (Protozoa, Kinetoplastida) and to structures of the vector gut.

Culture forms of Trypanosoma rangeli could be agglutinated with Canavalia ensiformis (Con A) lectin and, less effectively with Pisum sativum agglutinin (PEA), at a concentration of 200 micrograms/ml. Ricinus communis agglutinin I (RCA I) agglutinated trypanosomes only if they were not previously washed with physiological Ringer's solution. Three other lectins did not react with the same parasite forms. Direct or indirect lectin-gold labeling techniques were applied to LR-White embedded thin sections of T. rangeli culture forms and to forms in the gut, hemolymph, and salivary glands of Rhodnius prolixus. Under these conditions, Con A was the only lectin out of 9 that bound to the surface of trypanosomes from culture and from the bug hemolymph. Con A did not react with any midgut or salivary gland forms. The preservation of the biological activity of the lectin-gold complexes that did not bind to the parasite surface was confirmed by reactions with structures of the invertebrate host.

Agglutination Tests↗
PubMed1989

Isolation and partial characterization of the cell membrane of Walker-256 carcinosarcoma ascites cells.

Cell membranes of carcinosarcoma-256 ascites cells were isolated by the Zn++ method. Neutral sugars, sialic acid, fucose and N-Acetylhexosamines were determined in the cell membrane fraction. Cells were agglutinated by wheat germ agglutinin, Concanavalin A, and the lectins from Phaseolus vulgaris and Glycine max. No agglutination was observed with peanut lectin (Arachis hypogaea). Gel electrophoresis under dissociating conditions revealed more than 40 bands in the membrane fraction after silver staining. Only 2 bands were evident with PAS staining.

Animals↗