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PubMedDate not supplied

Phosphorylcholine antigens from Nippostrongylus brasiliensis. I.--Anti-phosphorylcholine antibodies in infected rats and location of phosphorylcholine antigens.

The anti-phosphorylcholine (PC) antibody synthesis was investigated in the rat after infection with the nematode Nippostrongylus brasiliensis. Serum IgM and IgG antibodies were demonstrated from day 2 or 3 post-infection. Intestinal IgA-antibody synthesis began shortly after the worms reached the intestine. Antigens containing PC were located with the fluorescent antibody technique in L3 infective larvae, adult worms and eggs of the parasites. They were always found to internal structures such as intestinal tract or gonads. It seems, therefore, that the anti-PC antibody synthesis resulted from the release of PC antigens by the parasite (moulting fluids, excretion, secretion or breakage products).

Animals↗
PubMed2002

Immobilization of L-glyceryl phosphorylcholine: isolation of phosphorylcholine-binding proteins from seminal plasma.

The preparation of an affinity sorbent containing immobilized L-glyceryl phosphorylcholine for affinity chromatography of phosphorylcholine-binding proteins from seminal plasma is described. The ligand was coupled either after its maleinylation to poly(acrylamide-allyl amine) copolymer or directly to divinyl sulfone-activated Sepharose. The prepared phosphorylcholine derivative coupled to Sepharose was used for affinity chromatography of phosphorylcholine-binding proteins from bull and boar seminal plasma. Adsorbed proteins were specifically eluted with phosphorylcholine solution. Isolated phosphorylcholine-binding proteins were characterized by SDS electrophoresis and HPLC with reversed phase. Composition of the boar phosphorylcholine-binding fraction obtained by affinity chromatography on immobilized L-glyceryl phosphorylcholine was compared with that eluted from immobilized heparin by the phosphorylcholine solution. No phosphorylcholine-binding proteins were found in human seminal plasma.

Animals↗
PubMed1989

Stimulation of phosphorylcholine turnover and diacylglycerol production in human polymorphonuclear leukocytes. Novel assay for phosphorylcholine.

Receptor-bypassing stimulants of human polymorphonuclear leukocytes (PMNLs), such as ionomycin or phorbol 12-myristate 13-acetate (PMA), generate an increase in diacylglycerol (DAG) which is independent of a phospholipase C specific for phosphatidylinositol 4,5,-bisphosphate (PIP2). Activation of a phospholipase C specific for phosphatidylcholine (PC) has been implicated as a source of DAG in other cells by measuring the release of radiolabelled phosphorylcholine. However, since PMNLs could not be labelled sufficiently with [3H]choline, we developed an h.p.l.c. assay to quantify mass levels of phosphorylcholine after enzymic conversion to [32P]CDP-choline with CTP-phosphorylcholine (choline phosphate) cytidylyltransferase (EC 2.7.7.15). This assay was linear to at least 20 nmol, and was sensitive to 10 pmol of phosphorylcholine. Baseline phosphorylcholine levels in unstimulated PMNLs were 2300 +/- 510 pmol/10(7) cells and were decreased by pretreatment with PMA (166 nM) or ionomycin (1 microM) for 10 min by 360 +/- 130 and 600 +/- 290 pmol/10(7) cells respectively (P less than 0.05). In contrast, baseline DAG levels were 147.6 +/- 11.7 pmol/10(7) cells in unstimulated PMNLs, and were increased by PMA or ionomycin by 1320 +/- 222 and 1891 +/- 264 pmol/10(7) cells respectively (P less than 0.05). Similarly, the chemoattractant fMet-Leu-Phe raised DAG levels by 731 +/- 111 pmol/10(7) cells and decreased phosphorylcholine levels by 180 +/- 60 pmol/10(7) cells. Activation of PMNLs by PMA, ionophore or fMet-Leu-Phe thus leads to the sustained production of DAG accompanied by the disappearance of phosphorylcholine. This suggests that these stimulants enhance PC turnover via a hydrolytic mechanism which is independent of phospholipase C, with activation of a PC-specific phospholipase D being a plausible mechanism.

Choline↗
PubMed1976

1-Hydroxy-2-tert-butyldimethylsilyl-sn-glycero-3-phosphorylcholine. A useful intermediate in the synthesis of short acyl chain 1-acyl-sn-glycero-3-phosphorylcholines.

The synthesis of 1-acyl-sn-glycero-3-phosphorylcholines in particular those containing short fatty acyl chains are described. The method involves the use of 1-acyl-2-tert-butyl-dimethylsilyl-sn-glycero-3-phosphorylcholines which can be readily prepared by reacting hens' egg yolk 1-acyl-sn-glycero-3-phosphorylcholines with tert-butyldimethylchlorosilane with imidazole as catalyst and dimethylformamide as solvent. Deacylation of the 1-acyl-2-tert-butyldimethylsilyl-sn-glycero-3-phosphorylcholines with saturated anhydrous potassium carbonate in methanol yields the 2-tert-butyldimethylsilyl-sn-glycero-3-phosphorylcholine. Reacylation of the 2-tert-butyldimethylsilyl-sn-glycero-3-phosphorylcholine with fatty acyl anhydride in the presence of 4-dimethylaminopyridine in anhydrous chloroform followed by removal of the tert-butyldimethylsilyl protecting group by treatment with dry hydrogen chloride gas in anhydrous chloroform at 0 degrees yields the desired 1-acyl-sn-glycero-3-phosphorylcholine. Various facets of the reactions involved in developing the synthetic procedures in this study are discussed.

Glycerylphosphorylcholine↗
PubMed1986

Dipetalonema viteae: phosphorylcholine and non-phosphorylcholine antigenic determinants in infective larvae and adult worms.

The humoral immune response of Balb/c mice to live infective larvae or adult worm extract of Dipetalonema viteae is composed of two antibody populations either with or without specificity for phosphorylcholine. Absorption of immune serum on phosphorylcholine-Sepharose and separation of the antibody population demonstrated that anti-larvae serum contains a larger ratio of phosphorylcholine versus non-phosphorylcholine antibodies as compared to anti-adult serum. Immunofluorescence on crossections of female worms revealed that antigen expressing phosphorylcholine determinants were mainly found on certain internal structures, like egg, uterine, and intestinal membranes, but not on the cuticle. Immunoblotting using an adult worm extract demonstrated that protein bands reacted with either one or both populations of antibodies. The patterns were heterogeneous and moreover differed between the anti-larvae serum and the anti-adult serum.

Animals↗
PubMed1989

The binding of phosphorylcholine-carrying antigens to the anti-phosphorylcholine monoclonal antibody TEPC 15. A fluorescence spectroscopic study.

The intrinsic fluorescence of the anti-phosphorylcholine monoclonal antibody TEPC 15 has been used to study its interaction with the hapten phosphorylcholine and some phosphorylcholine-carrying lipids. Spectral conditions were selected so as to obtain fluorescence emission attributable mainly to tryptophan residues. Upon addition of the hapten, the fluorescence intensity increases, and the emission maximum is shifted towards lower wavelengths, in a hyperbolic and saturable process. These effects seem to be specific for phosphorylcholine, since they are not produced by the analogue phosphorylethanolamine. The quenching results suggest that a conformational change occurs in the protein upon interaction with the hapten. Upon addition of a variety of phosphorylcholine-carrying lipids, it is shown that the antibody interacts with the hapten when the lipid exists in the form of micelles, but not when it is present in the lamellar phase.

Animals↗
PubMedDate not supplied

Phosphorylcholine antigens from Nippostrongylus brasiliensis. II.--Isolation and partial characterization of phosphorylcholine antigens from adult worm.

The phosphorylcholine antigens (C substance) were specifically isolated from Nippostrongglus brasiliensis adult worms. They formed a gorup of fairly closely related molecules, but it was not possible to evidence that the carrier molecule was unique. An indirect immunoenzymatic test using immobilized lectins (concanavalin A, phytohaemagglutinin Els, wheat germ agglutinin, recin types I and II, peanut agglutinin) gave some light on the carbohydrate composition of the carrier molecules, whereas the amino acid part of these molecules seemed to indicate an unique oligopeptide, the composition of which would be: Asx (4), Thr (2), Ser (4), Glux (6), Gly (6) Ala (3), Val (2), Ile (1), Leu (2), Phe (8), Lys (2), Arg (1). An epitope of the carrier molecules was demonstrated with anti-N. brasiliensis egg antisera. It was shared with various pathogens including Haemonchus contortus, Schistosoma mansoni and Dipetalonema vitae. It was also found on the purified pneumococcal C. polysaccharide. The C. substance from a variety of parasites can now be isolated by a combination of specific reactions using both anti-phosphorylcholine and anti-carrier molecule antibodies.

Amino Acids↗
PubMed1984

Phosphorylcholine on isologous red blood cells induces polyclonal but not anti-phosphorylcholine plaque-forming cells in mice.

It has been demonstrated in the preceding report (Bach, M. A., Beckmann, E. and Levitt, D., Eur. J. Immunol. 1984. 14: 589) that phosphorylcholine (PC) on the bacterium Streptococcus pneumoniae R36a stimulated polyclonal as well as anti-PC plaque-forming cells (PFC) in mouse spleen in vivo. In this study, red blood cells from BALB/c mice (MRBC) were either conjugated with PC, 2,4,6-trinitrophenyl (TNP) or treated with phospholipase A2 (PLA2) to expose PC on the cell membrane (determined by hemagglutination with the anti-PC myeloma HOPC8). When BALB/c mice were immunized i.v. with the conjugated or enzyme-treated MRBC, a significant polyclonal antibody response occurred (p less than 0.05) using PC-MRBC or PLA2-treated MRBC, but not with TNP-MRBC or sham-treated MRBC. No anti-PC or anti-MRBC immunoglobulin-secreting cells developed after immunization. Repeated immunization with PC-MRBC resulted in similar levels of protein A PFC after each immunization but no anti-PC, anti-MRBC or anti-PC-MRBC PFC. Thus, PC on R36a or isologous RBC stimulated increased numbers of splenic plaque-forming cells. In the case of R36a, 10-25% of these PFC produced antibodies directed towards PC. In contrast, PC-MRBC or PLA2-treated MRBC, failed to evoke any anti-PC antibody responses.

Animals↗
PubMed1995

Ultrastructural colocalization of phosphorylcholine and a phosphorylcholine-associated epitope in first-stage larvae of Trichinella spiralis.

Although the presence of phosphorylcholine (PC) in Trichinella is well established, the structures of the TSL-4 antigens that bear this epitope are unknown. A subset of TSL-4 antigens (TSL-8 antigens) has been reported to be absent from the surface of first-stage T. spiralis larvae. We report experiments with a monoclonal antibody (mAb US2) developed in mice with a relative inability to produce antibodies to PC. In immunoblotting, mAb US2 and anti-PC mAb (BH8) showed apparently identical binding patterns. In addition, we used an immunogold double-labeling technique to study the anatomical distribution of the epitopes recognized by these mAbs; the results obtained indicate close colocalization of epitopes for BH8 and US2 in tissues of T. spiralis first-stage larvae. On the basis of these results, we suggest that US2 probably binds to all T. spiralis TSL-4 antigens, including TSL-8 antigens. We also clarify some conflicting previous reports on the distribution of PC immunoreactivity in first-stage larvae of T. spiralis.

Animals↗
PubMed1974

Clonal nature of the immune response to phosphorylcholine. I. Specificity, class, and idiotype of phosphorylcholine-binding receptors on lymphoid cells.

The relationship between receptor molecules on antigen-binding lymphocytes (ABC) and antibody produced by antibody-secreting cells was studied in inbred strains of mice using the immune response to phosphorylcholine (PC) as a model system. Splenic and lymph node lymphocytes of nonimmune mice possess rare lymphocytes which bind (125)I-labeled PC-bovine serum albumin. The frequency of PC-ABC increases after immunization and is paralleled by a rise in the frequency of PC-specific antibody-producing cells. Both of these responses are thymus independent. The receptors on these ABC display specificity for PC and are exclusively of the IgM class. In one of the strains, BALB/c, the receptors possess the same idiotype and fine degree of specificity for PC and two of its analogues, glycerophosphorylcholine and choline, that are characteristic of a PC-binding myeloma, HOPC 8. Furthermore, the idiotype and class of the receptor in these mice do not change during the course of the immune response. These data provide more direct evidence for the immunelogic relevance of receptor-bearing lymphocytes.

Animals↗
PubMed1991

Interaction between phospholipids and biocompatible polymers containing a phosphorylcholine moiety.

Random and block copolymers containing a phospholipid polar group in their side chain were synthesized by the copolymerization between 2-methacryloyloxyethyl phosphorylcholine and styrene. These copolymers showed amphiphilic character, especially poly(methacryloyloxyethyl phosphorylcholine-block-styrene) formed stable polymer micelles in water. The interaction between natural phospholipid, dipalmitoylphosphatidylcholine and methacryloyloxyethyl phosphorylcholine copolymers was investigated. The amount absorbed of dipalmitoylphosphatidylcholine from its liposomal solution on to the poly(methacryloyloxyethyl phosphorylcholine-co-styrene) surface increased with increase of methacryloyloxyethyl phosphorylcholine composition. Moreover, when poly(methacryloyloxyethyl phosphorylcholine-block-styrene) was added to dipalmitoylphosphatidylcholine solution, organization of dipalmitoylphosphatidylcholine molecules and stabilization of bilayer structure of dipalmitoylphosphatidylcholine liposome were found. This means that methacryloyloxyethyl phosphorylcholine moieties in the copolymer have a strong affinity to dipalmitoylphosphatidylcholine molecules. The blood compatibility of methacryloyloxyethyl phosphorylcholine copolymers was also investigated with particular attention to the aggregation ability of platelets after contacting methacryloyloxyethyl phosphorylcholine copolymers; this ability decreased when platelets were put in contact with polymers without a methacryloyloxyethyl phosphorylcholine moiety. On the other hand, aggregation ability remained at almost the same level to that of original platelets after contact with methacryloyloxyethyl phosphorylcholine copolymers. From these findings, we concluded that methacryloyloxyethyl phosphorylcholine copolymers show excellent blood compatibility due to adsorption of lipids from plasma and the formation of an organized adsorption layer of lipids on the surface of the methacryloyloxyethyl phosphorylcholine copolymers.

1,2-Dipalmitoylphosphatidylcholine↗
PubMed1998

Atypical phosphorylcholine-reactive protein from Atlantic salmon, Salmo salar L.

A phosphorylcholine-reactive protein was isolated from serum of Atlantic salmon (Salmo salar L.) by affinity chromatography on a phosphorylcholine-conjugated Sepharose column followed by elution with phosphorylcholine. Based on the method used we describe the isolated protein as salmon phosphorylcholine-reactive protein (salmon PRP). Salmon PRP has calcium-independent binding to phosphorylcholine. The protein exists in a monomeric and dimeric form with molecular weight of approximately 80 and 160 kD, respectively. Separation of the protein preparation on SDS-PAGE under reducing conditions resulted in disappearance of the 80 and 160 kD bands and appearance of a major protein band of approximately 100 kD. The N-terminal amino acid sequences of the non-reduced 80 and 160 kD bands and the reduced 100 kD band were identical. Apart from the dimeric form, the molecular weight of salmon PRP and its appearance on SDS-PAGE is similar to human plasminogen. Comparison of the sequence in a protein database resulted in approximately 50% identity with human and bovine plasminogen. In addition, cross-reactivity between antibodies to human plasminogen and salmon PRP was demonstrated. Thus, salmon PRP appears to be different from other phosphorylcholine-reactive proteins which are mostly reported to be CRP-like proteins with calcium-dependent binding to phosphorylcholine, pentameric ring-structure and sequence homology between species. Whether salmon PRP is a new type of phosphorylcholine-binding protein with an unknown function or a plasminogen-like protein with binding specificity for phosphorylcholine calls for further investigation.

Amino Acid Sequence↗
PubMed1990

High anti-phosphorylcholine antibody levels and mortality associated with pneumonia.

Phosphorylcholine is an immunodominant determinant of pneumococcal teichoic acids. Antibodies to phosphorylcholine are naturally occurring in man and decline in amount with age. Since antibodies to phosphorylcholine are markers of the immune responsiveness to polysaccharides and since anti-polysaccharide antibodies are highly protective against most bacterial pneumonia we expected a higher rate of pneumonia in elderly individuals with low levels of antibodies to phosphorylcholine. The relationship between the levels of antibodies to phosphorylcholine and mortality was analyzed prospectively in a representative sample of elderly individuals. A significant anti-phosphorylcholine antibody response occurred in a subgroup of the probands. There was a strong association (p less than 0.0001) between high levels of antibodies to phosphorylcholine in the serum at 70 years of age and pneumonia related death up to 14 years later. A similarly strong association was not observed between mortality and the antibody titer to another naturally occurring polysaccharide antigen: the blood group B antigen. Furthermore, there was no association between mortality due to diseases other than pneumonia and the levels of antibodies to phosphorylcholine. The association between antibody levels and subsequent fatal pneumonia provides a means of detecting individuals at risk for pneumonia-related death.

Age Factors↗
PubMed1984

Acetyl glyceryl ether phosphorylcholine (AGEPC). A putative mediator of cardiac anaphylaxis in the guinea pig.

Platelet-activating factor is a novel phospholipid that has been implicated as an important mediator of acute allergic reactions. The intravenous administration of acetyl glyceryl ether phosphorylcholine, a pure, synthetic platelet-activating factor, causes electrocardiographic changes in the rabbit similar to those which are characteristic manifestations of systemic anaphylaxis. To determine whether platelet-activating factor contributes to anaphylactic cardiac dysfunction, we measured platelet-activating factor release from the sensitized guinea pig heart challenged in vitro with specific antigen and compared the resulting cardiac dysfunction with that induced by the injection of acetyl glyceryl ether phosphorylcholine into nonsensitized hearts. The results of these studies document that, during anaphylaxis in the isolated guinea pig heart, a platelet-activating factor is released into the coronary effluent that has physicochemical and functional properties similar to those of acetyl glyceryl ether phosphorylcholine. The intracardiac administration of acetyl glyceryl ether phosphorylcholine (10(-14) to 3 X 10(-9) mol) induced dose-related decreases in left ventricular contractile force (-5 to -85%) and coronary flow (-5 to -85%), as well as impaired atrioventricular conduction. The negative inotropic effect of acetyl glyceryl ether phosphorylcholine also was present in hearts perfused at constant flow. Although, in these hearts, acetyl glyceryl ether phosphorylcholine increased coronary resistance, which may have caused regional shunting and ischemia, it is unlikely that the negative inotropic effect of acetyl glyceryl ether phosphorylcholine was secondary to changes in coronary flow, since acetyl glyceryl ether phosphorylcholine also caused a dose-dependent negative inotropic effect in the electrically paced, noncoronary-perfused left atrium and right ventricular papillary muscle.(ABSTRACT TRUNCATED AT 250 WORDS)

Anaphylaxis↗