No abstract available.
Agglutinins ; Blood Cell Count

No abstract available.
Agglutinins ; Blood Cell Count

Agglutinins ; immunology ; Anemia, Hemolytic, Autoimmune ; Humans ; Immunoglobulin G ; Infant, Newborn

Cold hemagglutinin disease is a form of immune hemolytic anemia caused by cold-reactive immunoglobulins. Cold agglutinins are autoantibodies, usually of the IgM type, that cause red blood cell agglutination at reduced temperatures. When the agglutinated antibody-covered red blood cells return to the central circulation, the classical complement pathway is activated. Complement components combine with the antibody-covered red blood cells, inducing membrane changes that result in intravascular hemolysis. Clinical manifestations of cold hemagglutinin disease, which occur only on cold exposure include acrocyanosis, purpura, Raynauds phenomenon, acral gangrene, immune complex nephritis, and hemolytic anemia. We experienced a case of 66-year-old woman with cold agglutinin disease, gastric cancer and gall bladder stone. Preoperative plasmapheresis and intraoperative forced air convective warming to minimize red blood cell agglutination and hemolysis were performed. The operating room was prewarmed to 31~32degrees C. The patient had her lower body and the upper extremities covered with warming blankets. Inspired gases were humidified at 37degrees C and intravenous fluids were warmed with a blood warmer. Peripheral body temperature was maintained above 36.5degrees C throughout the procedure. Subtotal gastrectomy and cholecystectomy were done successfully without complication. It can be concluded that the maintenance of central and peripheral body temperature above the thermal aetivity of the cold agglutinin is required during the perioperative period.
Aged ; Agglutination ; Agglutinins ; Anemia, Hemolytic ; Anemia, Hemolytic, Autoimmune ; Anesthesia, General* ; Antigen-Antibody Complex ; Autoantibodies ; Body Temperature ; Cholecystectomy ; Complement Pathway, Classical ; Complement System Proteins ; Erythrocytes ; Female ; Gangrene ; Gases ; Gastrectomy ; Hemagglutinins ; Hemolysis ; Humans ; Immunoglobulin M ; Immunoglobulins ; Membranes ; Nephritis ; Operating Rooms ; Perioperative Period ; Plasmapheresis ; Purpura ; Stomach Neoplasms ; Upper Extremity ; Urinary Bladder Calculi

To investigate incidence of acute gastroenteritis (AGE) caused by Yersinia enterocolitica and Y. pseudotuberculosis (referred to as Y. enterocolitica-pseudotuberculosis complex) in children, seropositive rates to major 8 serotypes of Y. enterocolitica-pseudotuberculosis complex antigens among 467 sera of three groups of subjects (298 acute gastroenteritis; AGE, 108 miscellaneous pediatric diseases; MPD, and 61 healthy medical students; HMS) were investigated by bacterial agglutination test using standardized, heat-killed, phenolized, smooth 0 antigens. In addition, cross-reactions between yersinia agglutinins and Widal agglutinins in patients with AGE caused by Y. enterocolitica-pseudotuberculosis complex were examined in paired serum specimens. Seropositive rates to Y. enterocolitica-pseudotuberculosis complex among three groups, AGE, MPD, and HMS, were 36.5%, 13.8%, and 14.7%, respectively. Of 109 seropositive AGE patients, the most common type-specific agglutinin which showed predominating agglutinin titer to one of 8 serotypes of Y. enterocolitica-pseudotuberculosis complex antigens was PO4b (27.5%), followed by PO2a (23.8%), EO3 (16.5%), PO5a (13.7%), PO5b (9.1%), PO3 (4.5%), EO9 (2.7%), and POlb (1.8%), in orders. The Widal agglutinins cross-reacted to Y. pseudotuberculosis PO4b antigen, but the yersinia agglutinins were differentiated from Widal agglutinins by rising agglutinin titers in paired serum specimens taken one to three weeks apart. In conclusion, acute gastroenteritis caused by Y. pseudotuberculosis in children must be regarded as a fairly common enteric disease in children.
Agglutination Tests ; Agglutinins ; Child* ; Gastroenteritis* ; Humans ; Incidence ; Phenol ; Students, Medical ; Yersinia enterocolitica* ; Yersinia*

Pseudothrombocytopenia is an in vitro phenomenon usually associated with anticoagulant (ethylene diaminetetraacetic acid, EDTA)-dependent IgG platelet agglutinins. Two cases of pseudothrombocytopenia due to EDTA-independent agglutinins are reported. The fingerstick blood smear showed platelet clumping as well as EDTA, citrate and heparin samples. In a case with malaria, serum IgM was 985 mg/dL and serum protein immunofixation demonstrated an additional IgM band which disappeared together with platelet clumping a month later. The increased immunoglobulin (especially, IgM) appeared to be associated with platelet agglutinin. Another case had cold reactive agglutinin because the electronic platelet counts were dependent on temperature. These cases illustrate that pseudothrombocytopenia may be caused by more than one type of agglutinin and can be confirmed by using a direct fingerstick, keeping the sample warm, or drawing the blood into another anticoagulant.
Agglutinins* ; Blood Platelets ; Citric Acid ; Edetic Acid ; Heparin ; Immunoglobulin G ; Immunoglobulin M ; Immunoglobulins ; Malaria ; Platelet Count

Cold agglutinins are serum antibodies activated at low temperature to produce red blood cell agglutination and hemolysis. Hypothermic cardiopulmonary bypass has potential danger to patient with positive cold agglutinin titer. We report a successful anesthesia for mitral valve replacement surgery in a patient who has high cold agglutinin titer. To avoid problem, the cold agglutinin titer was reduced by plasmapheresis and hypothermia was maintained above the critical temperature. There was no severe complication except mild hemoglobinuria.
Agglutination ; Agglutinins ; Anesthesia* ; Antibodies ; Cardiopulmonary Bypass ; Erythrocytes ; Heart* ; Hemoglobinuria ; Hemolysis ; Humans ; Hypothermia ; Mitral Valve ; Plasmapheresis ; Thoracic Surgery*

OBJECTIVETo study the correlation of Pinellia ternata agglutinin (PTA) and toxicity of P. ternata raphides and to find out the toxic mechanism of P. ternata.

METHODPTA has obvious effect of pro-inflammation. The model of rats peritonitis was used to study the dose-toxicity and time-toxicity relationship of the effect by detecting the releases of inflammatory mediators PGE2 in the exudates. The model of Draize rabbit eye test was applied to determine the correlation of PTA and toxicity of raphides by pathological examination.

RESULTPTA enhanced the content of PGE2 and protein in rats peritoneal cavities concentration dependently. With PTA concentration increased, PTA enhanced the inflammation induced by raphides to rabbit eyes, but PTA alone had no toxicity response.

CONCLUSIONPTA had obvious effect of pro-inflammation. The toxic mechanism of P. ternata was PTA induced inflammation only when the raphides pierce into the organization.

Agglutinins ; chemistry ; toxicity ; Animals ; Eye ; drug effects ; Inflammation ; chemically induced ; Male ; Pinellia ; chemistry ; Rabbits ; Rats ; Rats, Sprague-Dawley

The present study was carried out to investigate the glycoconjugate properties of the nasal mucosa in the rat after inhalation of formaldehyde. Sprague-Dawley male rats were inhalated 30 ppm formaldehyde for 3 times with 3 hours exposure. The olfactory and respiratory mucosa in the nasal mucosa were taken from the animals on 3, 6,9 days and 2, 3, 4, 5 weeks after inhalation of formaldehyde. The properties of glycoconjugate of the olfactory and respiratory mucosa were investigated using nine biotinylated lectins (PSA, UEA I, PHA-L, BSL I, PNA, MAL I, DBA, BSL II or sWGA). In experimental groups, the degenerative changes of the olfactory epithelium were observed until 3 weeks after inhalation of formaldehyde, but the respiratory epithelium was no change. In control group, the olfactory cells in the olfactory epithelium reacted with PSA, UEA I, PNA, DBA, BSL II, sWGA, and the supporting cells reacted with PSA, PHA-L, PNA, MAL I, DBA, BSL II, sWGA, and Bowman's glands reacted with all the lectins. In experimental groups, the olfactory cells reacted with UEA I, DBA, and the supporting cells reacted with PHA-L, MAL I, DBA, UEA I, and the positive reaction of Bowman's glands was increased. In control group, the goblet cells in the respiratory epithelium reacted with UEA I, MAL I, and the ciliated columnar cells reacted with PSA, UEA I, PHA-L, BSL I, DBA, BSL II, sWGA, and the septal nasal glands reacted with all the lectins except UEA I. In experimental groups, the goblet cells reacted with UEA I, MAL I and PNA. Conclusively, the olfactory mucosa was shown a lot of changes in the properties of glycoconjugates following inhalation of formaldehyde, but respiratory mucosa was shown feeble change. These results suggest that there were different sugar residues of glycoconjugate in the olfactory and respiratory mucosa following inhalation of formaldehyde, respectively.
Animals ; Formaldehyde ; Glycoconjugates ; Goblet Cells ; Humans ; Inhalation ; Lectins ; Male ; Nasal Mucosa ; Olfactory Mucosa ; Phytohemagglutinins ; Rats ; Respiratory Mucosa ; Wheat Germ Agglutinins

This study is undertaken to modify the chitosan nanoparticles (CS-NPs) with wheat germ agglutinin (WGA), and investigate the conjugation between WGA-CS-NPs and N-acetylglucosamine (NAG). CS-NPs were prepared by ionotropic gelation process and then conjugated with WGA under the activation of glutaricdialdehyde. The mean diameter of the CS-NPs was approximately 113.5 nm and the poly-dispersity index (PDI) was 0.18. The binding yield of WGA to CS-NPs was comprised between 27.8% and 87.9% depending mostly on the addition of 0.3% (w/v) glutaraldehyde solution. A competitive inhibition experiment of WGA-CS-NPs to bovine submaxillary gland mucin (BSM) was taken to illuminate the binding activity of WGA-CS-NPs to the sugar of N-acetylglucosamine. After the addition of NAG, the binding rates between CS-NPs and BSM almost didn't change, while the binding rates between WGA-CS-NPs and BSM dropped down significantly, which confirmed the specific binding characteristics of WGA to NAG.
Acetylglucosamine ; chemistry ; metabolism ; Chitosan ; chemistry ; metabolism ; Drug Delivery Systems ; Mucins ; metabolism ; Nanoparticles ; Particle Size ; Protein Binding ; Wheat Germ Agglutinins ; chemistry ; metabolism