Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019621 (Langerhans cell histiocytosis)
 3,250 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Examination of human pregnancy tissues with a panel of lectins provides the opportunity to probe different aspects of carbohydrate structure. Nine biotinylated lectins [concanavalin A (con A), wheat germ agglutin (WGA), Lens culinaris A (LCH-A), Pisum sativum (PSA), Phaseolus vulgaris (PHA-E and PHA-L), Ulex europaeus 1 (UEA1), Griffonia simplicifolia (GSI and GSII)] were used to investigate the lectin binding of human trophoblast in normal, tubal, and molar pregnancy. All lectins except UEA1 bound to normal villous syncytiotrophoblast. Binding of lectins to extravillous trophoblast was more restricted than to villous trophoblast, occurring predominantly with con A, PHA-E, PHA-L, WGA, GSI, and GSII. LCH-A reacted with cyto-trophoblastic columns but not with interstitial or endovascular trophoblast. Con A and GSII were the only lectins that bound to trophoblastic giant cells. GSI and GSII bound preferentially to extravillous trophoblast, showing only focal reactivity with villous trophoblast. Lectin binding in ectopic pregnancy was similar to that in normal first-trimester intrauterine pregnancy. Reactivity in molar pregnancy also generally mirrored that observed in normal pregnancy; however, reactivity of GSII with villous trophoblast was more consistent than that observed in normal pregnancy, and GSI showed uniform binding to proliferating syncytial areas. Thus, lectin binding studies allow definition of surface carbohydrates, which may play a role in the controlled trophoblast proliferation and invasion that occurs in normal pregnancy.
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PMID:Further studies of lectin binding by villous and extravillous trophoblast in normal and pathological pregnancy. 191 74

In order to study the localization of Lentil lectin (LCH)-binding glycoresidues in glomeruli from patients with a variety of glomerulopathies, and to elucidate the relationship between LCH-binding sugars and the components of the extracellular matrix, laminin and type IV collagen, investigations of formalin-fixed, paraffin-embedded kidney tissues digested with trypsin were carried out by the direct and indirect immunofluorescence microscopy techniques. The glomerular basement membrane (GBM) and the mesangium reacted well with LCH, whereas areas with sclerotic lesions exhibited a decreased reactivity. The pattern of LCH binding to the GBM in various glomerulopathies was similar to that of laminin but different from that of type IV collagen. The pattern of localization of LCH-reacting sites and of laminin in the GBM included the double linear lines in diabetic nephropathy, inner linear line with outer projections (spikes) in membranous nephropathy, and reduplicated basement membrane in membranoproliferative glomerulonephritis. The results obtained by enzyme-linked immunoadsorbent assay showed that LCH had a stronger reactivity for laminin than for type IV collagen or fibronectin. These findings suggest that LCH is more reactive with laminin than with other components of the glomerular extracellular matrix.
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PMID:Histochemical and immunohistochemical studies of diseased human glomeruli. 203 28

Using a modified method of concanavalin A (Con A), lentil lectin (LCH) or phytohemagglutinin-E (PHA-E) affinity crossed-line immunoelectrophoresis, alpha-fetoprotein (AFP) subfractions were studied in 33 samples of human amniotic fluid obtained between 41 and 287 days of gestation. Fetal tissues (yolk sac, liver, stomach and small intestine) obtained from a fetus of 68 days' gestation were incubated for 24 hours and AFP subfractions in the culture fluid examined. AFP in control amniotic fluids yielded two subfractions (types a and b) with Con A, three subfractions (types A, B and C) with LCH, and four subfractions (types W, X, Y and Z) with PHA-E. Serial changes of AFP subfractions in the amniotic fluid, as well as in the incubation study, indicated that the yolk sac and the gastrointestinal tract were responsible for the production of the Con A non-reactive subfraction (type b), the LCH weakly-reactive subfraction (type B) and the PHA-E reactive subfraction (types W and X), at an early stage of gestation. The Con A reactive subfraction (type a), LCH reactive subfraction (type A), PHA-E weakly-reactive subfraction (type Y) and PHA-E non-reactive subfraction (type Z) were assumed to be produced mainly by yolk sac, liver or gastrointestinal tract. We also found that the LCH non-reactive subfraction (type C) was synthesized either by liver or by the gastrointestinal tract at an early stage of gestation. At term, type a of Con A, type C of LCH and types Y and Z of PHA-E were the main subfractions in amniotic fluid, assumed to be produced by the fetal liver.
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PMID:Alpha-fetoprotein subfractions in amniotic fluid identified by a modification of the method of concanavalin A, lentil lectin or phytohemagglutinin-E affinity crossed-line immunoelectrophoresis. 241 31

Using a modified method of concanavalin A (Con A), lentil lectin (LCH) or phytohemagglutinin-E (PHA-E) affinity crossed-line immunoelectrophoresis (ACIE), we studied alpha-fetoprotein (AFP) subfractions in 69 sera, including 58 from patients with primary liver cancer and 11 from patients with hepatic metastasis of gastric cancer. We found that Con A non-reactive subfraction (type b) or LCH weakly-reactive subfraction (type B) was more frequently detected in metastatic liver cancer, as compared with liver cancer hepatoma. The amount of Con A non-reactive subfraction (type b) or of PHA-E reactive subfraction (type X) was significantly higher in case of metastatic liver cancer than in primary liver cancer. Since different affinities between AFP and lectins are due to the microheterogeneity in AFP sugar chain, our findings suggest that AFP in primary liver cancer and metastatic liver cancer is glycosylated in a different manner. It is also indicated that different patterns of AFP subfractions identified by the combination of Con A, LCH or PHA-E ACIE facilitate a differential diagnosis of these hepatic malignancies.
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PMID:Serum alpha-fetoprotein subfractions in hepatic malignancies identified by different reactivities with concanavalin A, lentil lectin or phytohemagglutinin-E. 242 Oct 34

Using a modified method of lectin affinity crossed-line immunoelectrophoresis, we studied the alpha-fetoprotein (AFP) subfractions in sera from 12 pregnant Japanese women, at 22 and 42 weeks of gestation. The method involves the first dimension electrophoresis in agarose gel containing concanavalin A (Con A) or lentil lectin (LCH), the second dimension immunoelectrophoresis in agarose gel containing polyclonal antibody against AFP, reaction with peroxidase-conjugated Protein A and staining with 4-methoxy-1-naphthol. We found that type a of Con A or type C of LCH was the only subfraction present in maternal circulation at the second or third trimester. These AFP subfractions were assumed to be of fetal liver-origin. The minimum concentration which yielded an immunoprecipitation peak was approximately 100 ng/ml, being twenty times more sensitive than the conventional lectin affinity crossed-line immunoelectrophoresis.
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PMID:Serum alpha-fetoprotein subfractions in pregnant women identified by the modified method of lectin affinity crossed-line immunoelectrophoresis. 242 45

A sensitive new technique for lectin-affinity immunoelectrophoresis was applied to samples from 28 infants and children in order to distinguish the origin of elevated alpha-fetoprotein (AFP) in sera. This new immunoelectrophoresis was successfully performed within 24 hours in sera with AFP as small as 910 ng/mL. With combined use of concanavalin A (Con A) and lentil agglutinin (LCH) binding tests, AFPs were classified into three subtypes: benign hepatic condition type (six patients), hepatocellular carcinoma type (nine patients) and yolk sac type (12 patients). AFP was of hepatocellular carcinoma type in all seven patients with hepatoblastoma, and of benign hepatic condition type in six of seven patients with elevated AFP due to conditions such as hepatitis, biliary atresia, and normal newborn. The question as to whether AFP produced in "hepatoblastoma" is of benign hepatic condition type or hepatocellular carcinoma type was first answered by the information in this present report. The differentiation between yolk sac and general hepatic AFPs was completed with the Con A binding test.
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PMID:Three different types of alpha-fetoprotein in the diagnosis of malignant solid tumors: use of a sensitive lectin-affinity immunoelectrophoresis. 247 22

Alpha-fetoprotein (AFP) subfractions were studied in 38 sera including 34 patients with primary hepatoma and 4 from patients with hepatic metastasis of gastric cancer. Fractionation of AFP was carried out by concanavalin A (Con A) or lentil lectin (LCH) crossed-line affinity immunoelectrophoresis. With use of Con A, fetal-liver-originated subfraction (peak a) was commonly found in both primary hepatoma and metastatic liver cancer, while yolk-sac-originated subfraction (peak b) was detected in 7 of 34 (20.6%) primary hepatomas and 4 of 4 (100%) metastatic liver cancers. With use of LCH, fetal-liver-originated subfractions (peaks A and/or C) were commonly found in both primary hepatoma and hepatic metastasis of gastric cancer, while yolk-sac-originated subfraction (peak B) was found only in metastatic liver cancer. These findings suggest that glycosylation of AFP in primary hepatoma differs from that in hepatic metastasis of gastric cancer. It is also suggested that AFP synthesized in hepatic cancers and fetal liver are differently glycosylated and AFP synthesis of hepatic malignancies are not always retrogenetically expressed, as in case of the fetal liver. Clinically, different patterns of AFP subfraction identified by Con A or LCH crossed-line affinity immunoelectrophoresis facilitate a differential diagnosis of primary hepatoma and hepatic metastasis of gastric cancer, in cases of elevated serum AFP levels. In the current study, attention was also given to the retrogenetic expression of AFP synthesis in hepatic metastasis of gastric cancer.
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PMID:Serum alpha-fetoprotein subfractions in patients with primary hepatoma or hepatic metastasis of gastric cancer. 257 79

The binding of 10 different lectins to the surface of microfilariae of Wuchereria bancrofti has been investigated. Wheat germ agglutinin (WGA) and Helix pomatia lectin (HPA) bound specifically to the sheathed microfilariae indicating the presence of N-acetyl-D-glucosamine and N-acetyl-D-galactosamine respectively on the surface. Exsheathed microfilariae did not react with any of the lectins. Treatment of sheathed microfilariae with proteases resulted in increased binding of WGA and HPA. Such treated microfilariae showed a weak binding of Concanavalin A (Con A), and lectins of lentil (LCH) and of Limulus polyphemus (LPA). Sheathed microfilariae incubated with sera of people living in endemic zones of filariasis but with no apparent evidence of infection (endemic normals), or with sera of chronic elephantiasis patients, or with their respective gamma globulin fractions, bound Con A and LCH. These lectins bound weakly to exsheathed microfilariae under the same conditions. Binding was due to the mannose components of the specific immunoglobulins of the sera which coated the microfilariae. However, microfilariae when incubated with sera or their globulin fractions from non-endemic normals (NEN), or from microfilarial carriers, did not bind Con A and LCH, suggesting that specific immunoglobulins were neither present in NEN sera nor in significant amounts in sera of microfilarial carriers.
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PMID:Lectin-binding characteristics of Wuchereria bancrofti microfilariae. 288 37

The carbohydrate compounds of the mucus of flask cells in the kidney of claw-frogs (Xenopus laevis) were analysed through lectin binding studies. After removing epoxy resin semithin sections were incubated with 7 lectins (WGA, RCA I, PNA, LCH, UEA, LPA) marked by horseradish peroxidase and 2 unmarked lectins (VAA, Con A). The glycosaminoglycans in the canalicular lumen of flask cells showed a strong reaction with WGA and RCA, whereas the binding of PHA, Con A, and LCH was weaker. No reaction was observed with PNA, UEA, LPA, and VAA. The mucus of the flask cells seems to be rich in N-acetyl-glycosamine and -galactosamine. It contains also mannose, glucose, and galactose, but seems to have no fucose or N-acetyl-sialic acid residues.
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PMID:Lectin binding on carbohydrate compounds of the flask cells in the claw-frog kidney. 314 43

The carbohydrate moieties of microfilariae (Mf) and infective larvae (L3) have been investigated by lectin-binding technique. Mf derived from three sources, namely, uteri (in utero), released in vitro from adults and from blood of rodents infected with Litomosoides carinii were examined by using fluoresceinated lectins. Wheat germ agglutinin (WGA) bound to these Mf and the binding was inhibited by N-acetyl glucosamine. In addition to WGA, Concanavalin A (Con A) and lentil lectin (LCH) bound to in vitro-released and in utero-derived Mf showing the presence of mannose moieties on their surface. In utero-derived Mf also showed binding with the agglutinins of Limulus polyphemus (LPA), peanut (PNA), Ricinus communis (RCA), Helix pomatia (HPA), Soyabean (SBA) and Dolichos biflorus (DBA) but not to that of Ulex europaeus (UEA) indicating the presence of additional carbohydrate molecules like sialic acid, galactose and N-acetyl galactosamine on their sheath. None of the lectins bound to the cuticle of exsheathed Mf. Treatment of blood-derived and in vitro-released Mf with certain proteases exposed additional binding sites for SBA, HPA, Con A and LCH. In case of L3, only PNA bound to the larvae isolated from infective mites Bdellonyssus bacoti, and the binding was inhibited by D-galactose. No such binding of the lectins was seen to the larvae that migrated to the pleural cavity of jirds indicating that there is considerable change on the parasite surface during their migration in the vertebrate host. Sheathed Mf and mite-derived L3 when incubated with immune rat sera, bind Con A and LCH lectins possibly due to the mannose components of the specific immunoglobulins that coat onto the Mf and L3.
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PMID:Litomosoides carinii: characterization of surface carbohydrates of microfilariae and infective larvae. 360 35


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