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PubMed1984

[Blood groups A and O with a weaker serological reactivity to agglutinins in the serum].

In normal conditions anti-A and anti-B agglutinins are seldom weak and very seldom they are completely absent. Agglutination reaction depends on temperature. It is intensified by treatment of erythrocytes with enzymes (papain) and is also dependent on genotype of the person investigated. Alterations are more frequently observed in anti-B agglutinin. Two cases with defective A and O blood groups are presented, with anti-B agglutinin missing at routine investigation. Treatment of erythrocytes at 4 degrees C with papain indicated the presence of anti-B agglutinin which has a weaker serological expression. Assessment of immunoglobulin concentration by laser nephelometry before and after adsorption and elution, also indicated the presence of this agglutinin.

ABO Blood-Group System↗
PubMed1984

The role of sialic acid in the activation of platelets by wheat germ agglutinin.

Sialic acid is believed to play a critical role in the survival of blood platelets in circulation. Wheat germ agglutinin, which shows specificity for sialic acid, N-acetylglucosamine, and N-acetylgalactosamine, strongly activates platelets. The role of sialic acid in platelet activation by this lectin was studied utilizing neuraminidase-treated platelets and the succinylated lectin that has been reported not to recognize sialic acid. The succinylated lectin had a dimeric structure similar to the native lectin, but migrated more slowly in gel electrophoresis. The modified lectin bound to about 2.8 X 10(5) sites/cell, with an apparent dissociation constant of 2 microM compared to 5 X 10(5) sites/cell and a dissociation constant of 0.4 microM for the native lectin. The succinylated lectin neither aggregated nor agglutinated platelets, but agglutination of red cells in microtiter plates was normal. Aggregation of platelets by either wheat germ agglutinin or ristocetin was not affected by the succinylated lectin. Since the native wheat germ agglutinin is a strong activator of platelets and the succinylated derivative was devoid of all activity, it appears that a sialoprotein acts as the biologic receptor of wheat germ agglutinin in human platelets. This suggestion was strengthened by the observation that platelets treated with different concentrations of neuraminidase had a decreased capacity to bind this lectin. These platelets also showed reduced aggregation and serotonin secretion when activated with the native lectin. Since sialic acid has been implicated in the removal of platelets from circulation, wheat germ agglutinin may prove to be a useful tool to explore those clinical conditions in which platelet survival is shortened.

Agglutination Tests↗
PubMed1982

Sexual agglutinins from the Chlamydomonas flagellar membrane. Partial purification and characterization.

Chlamydomonas sexual agglutinins have been quantitatively extracted from isolated flagella in vitro using the dialyzable nonionic detergent octyl-D-glucopyranoside and from cells in vivo with 12.5 mM EDTA. Both preparations elicit normal sexual responses from gametes of complementary, but not like, mating types. Extracts of vegetative cells and several agglutination-deficient (imp) mutants are totally inactive. Agglutinin activity is sensitive to trypsin, mild periodate oxidation, and heating at 60 degrees C for 1 min. These findings, coupled with the size of the molecule (it is excluded from Sepharose 6B and sediments as a 12 S particle in sucrose gradients) lead us to propose that the Chlamydomonas sexual agglutinins are large glycoproteins or glycoprotein aggregates which associate with the flagellar membrane in an extrinsic fashion. Partial purification of in vivo 125I-surface labeled EDTA extracts rules out several surface polypeptides, including the bulk of material migrating in the region of the major membrane glycoprotein (Mr 350,000), as agglutinin candidates and indicates that the active molecule is a minor component of the flagellar membrane. In addition, in vitro assays suggest a mechanism for in vivo sexual agglutination whereby stable adhesion is achieved by the active redistribution of agglutinins to the flagellar tips.

Agglutinins↗
PubMed1983

Management of patients with cold agglutinins who require open-heart surgery.

Cold agglutinins are commonly found in the sera of healthy persons but rarely become clinically important because most agglutinins exert their greatest reactivity at low temperatures. This report describes a patient who successfully underwent aortic valve replacement in the presence of cold agglutinins; it discusses the management of patients with cold agglutinins who undergo open-heart surgery with core hypothermia. Changes in the cell membrane occur when cold circulating antibody combines with complement and antigen present on the surface of the red cell membrane, causing intravascular hemolysis. Two conditions are necessary for the reaction to occur to any appreciable extent: there must be a high enough titre of cold agglutinin and the reactive thermal range must be attained. To avoid these conditions, the core hypothermia should not reach the reactive thermal range or the titre should be reduced either by the standard hemodilution techniques for cardiopulmonary bypass or by plasmapheresis.

Aged↗
PubMed1995

[Low titer cold agglutinin disease due to anti-HI antibody and a review of this disease in Japan].

A 79 year-old Japanese man was admitted because of brownish urine and Raynaud phenomenon. Laboratory data showed mild anemia with reticulocytosis, positive direct Coombs test against anti-C3, elevated level of lactate dehydrogenase, undetectable level of serum haptoglobin and low titer of cold agglutinin (1:256 at 4 degrees C), the immunoglobulin subclass of which was IgM. Cold agglutinin disease is usually associated with very high levels of cold agglutinins, the specificity of which is anti-I. This case had low titer cold agglutinin disease due to anti-HI cold agglutinin.

Adolescent↗
PubMed1996

[Cold agglutinins and cryoglobulinemia in a patient with hepatitis C].

OBJECTIVES: Cold agglutinins and cryoglobulins are uncommon in the same patient as observed in our case. CASE REPORT: A 74-year-old patient suffered repeated episodes of hemolytic anemia for one year and had hepatitis C anti-virus antibodies. Mixed cryoglobulinemia was found at levels which increased during episodes of acute hemolysis in addition to anti-I cold agglutinins. Two-dimensional electrophoresis revealed identical oligoclonal cold agglutinins and cryoglobulins. DISCUSSION: Unlike mixed cryoglobulinemia, cold agglutinins are not known to occur subsequent to hepatitis C infection. The identical immunoglobulins observed in our patient suggest a common origin. Chronic anti-I cold oligoclonal agglutinins are rarely observed and could be an intermediary step towards monoclonal lymphopathy as has been described in prolonged hepatitis C infection.

Aged↗
PubMed1999

Immunolocalization of anti-agglutinin for spermatozoa in boars.

A boar "anti-agglutinin," which inhibits head-to-head agglutination of spermatozoa, has been identified as a 25-kDa sialoprotein contained in epididymal and seminal plasma. This study was conducted to determine the location of the anti-agglutinin on spermatozoa and in various organs, including epididymides, by indirect immunofluorescence and Western blotting techniques. Ejaculated boar spermatozoa were washed and subjected to immunocytochemical observation. Epididymal plasma was recovered from three different regions of epididymides and subjected to sodium dodecylsulfate (SDS)-polyacrylamide gel electrophoresis (PAGE) and Western blotting. Twelve kinds of organs (testis, epididymis, seminal vesicle, prostate, heart, liver, kidney, spleen, stomach, small intestine, lung, and muscle) were recovered from boars. The unilateral epididymides were fixed, cut into 10-microm frozen sections, and subjected to immunohistochemical observation. The other organs were homogenized and used for SDS-PAGE and Western blotting. Immunocytochemical observations revealed that the antiserum strongly recognized the acrosomal region and equatorial segment on unfixed and methanol-fixed spermatozoa. Immunohistochemical observations revealed that the epithelia of the epididymal ducts were recognized by the antiserum mainly in the corpus epididymides. Moreover, the antiserum reacted with the luminal contents of the corpus and cauda epididymides. However, no specific reaction was detected in the caput epididymides. Western blotting showed that the antiserum selectively recognized a band of the anti-agglutinin in the corpus and cauda epididymal plasma, although no band was detected in the caput epididymal plasma. In the extracts from various organs, the single band was detected in the corpus and cauda epididymides at the same mobility as the anti-agglutinin, but not in the other organs. Based on these results, the following matters concerning the anti-agglutinin are discussed: (1) the importance of its association with the acrosome of spermatozoa in inhibiting sperm head-to-head agglutination; (2) its origin in the epididymis; and (3) its tissue specificity.

Animals↗
PubMed1983

Cytofluorometric quantification of somatopetally transported FITC-labelled lectins: enhanced uptake of concanavalin A and wheat germ agglutinin from the periphery in regenerating facial nerve.

Cytofluorometric quantification of the accumulation of somatopetally transported fluoroisothiocyanate (FITC)-labelled wheat germ agglutinin (WGA) and Concanavalin A (Con A) were performed on sections of the mouse facial nucleus. The lectins were injected bilaterally in the snout region of six-week-old mice eleven days after one of the facial nerves had been crushed. Analysis of variance revealed a significantly higher uptake of both WGA and Con A in the regenerating than in the control nerve. WGA appeared to be taken up to a higher degree than Con A, both in normal and regenerating nerve. After application of the two lectins to the facial nerve immediately after injury, at the site of crushing, both WGA and Con A were taken up and transported to nerve cell bodies of the facial nucleus. The observed difference in uptake between WGA and Con A from injured axons was even more pronounced than that found in intact axons. No accumulation of fluorescent material was seen in the cell bodies of the facial nucleus after injection of four other lectins (dolichos biflorus agglutinin, peanut agglutinin, ulex europeus 1 agglutinin, soybean agglutinin) either into the snout or the area of the nerve crush.

Animals↗
PubMed1984

Sexual agglutinin of mating-type minus gametes in Chlamydomonas reinhardii. I. Loss and recovery of agglutinability of gametes treated with EDTA.

The effect of EDTA on the mating-type-specific agglutinins located on the flagellar surfaces of Chlamydomonas reinhardii gametes was investigated. The mating-type minus (mt-) gametes lost their agglutinability without apparent loss of motility soon after addition of EDTA at low concentrations (1-2 mM). At the same time, the cells released into the medium agglutinins which can elicit agglutinative responses of mating-type plus (mt+) gametes specifically. When EDTA was neutralized with Mg2+ or removed by centrifugation, the mt- cells quickly replaced agglutinins by protein synthesis: the recovery process was sensitive to cycloheximide, but not to tunicamycin. The EDTA-treated mt+ gametes lost their agglutinins much more slowly than the mt- gametes. The replacement of mt+ agglutinins was inhibited by both cycloheximide and tunicamycin.

Agglutination↗
PubMed1987

Serial observations of colonic carcinogenesis in the rat. Premalignant mucosa binds Ulex europeus agglutinin.

We evaluated certain histochemical tests for their ability to detect premalignant mucosa in the dimethylhydrazine model of colonic carcinogenesis. Biweekly colonoscopic biopsies of the descending colon were performed for 29 wk in control and dimethylhydrazine-treated rats. Biopsy specimens of the splenic flexure, rectum, and any visualized tumors were taken. The specimens were stained with periodic acid-Schiff to detect neutral mucins, high-iron diamine alcian blue to detect sialylated and sulfated mucins, fluoresceinated peanut agglutinin, and fluoresceinated Ulex europeus agglutinin. None of the first three tests consistently detected premalignant mucosa. However, Ulex europeus agglutinin, which bound to only 3% of control biopsy specimens throughout the course of the study, bound to increasing numbers of biopsy specimens in the dimethylhydrazine-treated animals, reaching a maximum of 90% positivity by 13-16 wk. Moreover, Ulex europeus agglutinin bound strongly to all biopsy specimens from tissues adjacent to tumors and to 93% of tumors. Mucosal atrophy and focal dysplasia were present more frequently in specimens taken from the rectum (but not the splenic flexure) of dimethylhydrazine-treated animals than of control animals, but there was no correlation between the histochemical markers and either atrophy or dysplasia. We conclude that Ulex europeus agglutinin binding is a consistent feature of premalignant colonic mucosa in dimethylhydrazine-treated rats.

Animals↗
PubMed1982

Identification of the HA-2 agglutinin in the haemolymph of the ascidian Botrylloides leachii as the factor promoting adhesion of sheep erythrocytes to mouse macrophages.

The HA-2 agglutinin purified from B. leachii haemolymph is shown to mediate the binding of sheep erythrocytes to mouse macrophages. This agglutinin appears to be wholly responsible for the adhesive activity of haemolymph, since upon chromatography of the latter through Sephadex G-200, the adhesive activity for both sheep and guinea pig erythrocytes was confined to those fractions containing the HA-2 agglutinin. The HA-1 agglutinin recovered in earlier fractions was unable to promote the adhesion of guinea pig erythrocytes to macrophages. Adsorption experiments indicated that this was due to a lack of ligand sites on the macrophage surface. These data support earlier conclusions that the HA-1 and HA-2 agglutinins have distinct binding specificities.

Animals↗
PubMed1982

The specificity of Centruroides sculpturatus Ewing (Arizona lethal scorpion) hemolymph agglutinins.

C. sculpturatus sera agglutinate human erythrocytes independently of the ABO blood group, enzyme treatment, incubation temperature or sex of the scorpions. Tested with human lymphocytes and reptile and bird erythrocytes, C. sculpturatus serum reacts like an anti-sialic acid agglutinin. With leukemic lymphocytes, titers are higher than with normal lymphocytes. Mammalian erythrocytes show characteristic agglutination patterns for C. sculpturatus for Limulus polyphemus (horseshoe crab) that suggest different receptors for agglutinins of both species. Cross absorption and elution experiments indicate the presence of at least two specific agglutinins in C. sculpturatus serum. Agglutination is inhibited by N-acetylneuraminic acid and N-glycolyneuraminic acid, for all erythrocytes tested. Calcium is required for optimal activity of C. sculpturatus agglutinins. C. sculpturatus agglutinating activity is destroyed at 65% degrees C for 20 minutes. Titers are decreased by 2-mercaptoethanol, and more so after alkylation with iodoacetic acid suggesting that disulfide bonds are present in C. sculpturatus agglutinin molecules.

ABO Blood-Group System↗
PubMed1972

The purification and characterization of wheat-germ agglutinin.

The purification of wheat-germ agglutinin by precipitation with ammonium sulphate and by chromatography on Sephadex G-75, Sepharose-ovomucoid and CM-cellulose is described. This procedure gave agglutinin preparations which were homogeneous on polyacrylamide gels under a variety of conditions. Purified wheat-germ agglutinin formed colourless solutions and was relatively insoluble at neutral pH; maximum solubility in 1mm-tris-HCl buffer, pH7.4, was approx. 1mg/ml. The agglutinin was a glycoprotein containing a single polypeptide chain with an approximate molecular weight of 23000. The N-terminus of the oxidized agglutinin was cysteic acid and the C-terminus was glycine. The amino acid composition showed that the protein was extremely rich in cysteine and cystine; there were 15-17 free SH groups/mol. The absorption maximum for the protein was at 272nm and the molar extinction coefficient at 280nm was 1.09x10(5) litre.mol(-1).cm(-1). Equilibrium dialysis indicated that there was only one binding site per molecule for N-acetylglucosamine.

Amino Acid Sequence↗
PubMed1998

Cutaneous necrosis by cold agglutinins associated with glomeruloid reactive angioendotheliomatosis.

The cold agglutinin syndrome is a haemolytic disorder that can cause skin lesions, mainly on the acral areas, with acrocyanosis being the most frequent manifestation. Cutaneous necrosis due to cold agglutinins is very rare. Reactive angioendotheliomatosis (RAE) is an uncommon condition that exclusively affects the skin, characterized by a hyperplasia of endothelial cells and pericytes that can result in the formation of glomeruloid structures. The association of cold agglutinin syndrome with glomeruloid RAE has not been previously described. We report a 70-year-old man diagnosed as having a B-cell low-grade non-Hodgkin's lymphoma. He had two episodes of cutaneous necrosis in acral areas which were related to exposure to cold and due to IgM anti-I(T) cold agglutinins. Biopsy specimens showed vessel proliferations composed of dilated vascular spaces in the dermis and subcutis. Some vessel lumina were partially occluded by eosinophilic thrombi of fibrin and erythrocytes. Numerous closely packed capillaries were observed within pre-existing dilated vessels. This intravascular proliferation of capillaries displayed a glomeruloid pattern. We emphasize the possible presence of a cold agglutinin syndrome in patients with skin necrosis and findings of RAE with a glomeruloid pattern. Cold agglutinaemia may cause these distinctive histological changes.

Aged↗
PubMed1998

Essential monoclonal gammopathy with an IgM paraprotein that is a cryoglobulin with cold agglutinin and EDTA-dependent platelet antibody properties.

A patient with apparent anaemia and thrombocytopenia caused by a monoclonal paraprotein is described. The patient's serum contained a monoclonal IgM kappa, a cryoglobulin and a cold agglutinin. The cryoglobulin, similar to the serum paraprotein, was a monoclonal IgM kappa. Serum was studied to determine the relationship of the cryoglobulin with the cold agglutinin. The cryoglobulin and cold agglutinin were found to be the same paraprotein. Moreover, with absorption and elution techniques the reactivity of the autoantibody with both erythrocytes and platelets was demonstrated. Reports of cryoprecipitable cold agglutinins are rare and therefore this case is exceptional given that the IgM kappa paraprotein was found to be a cold agglutinin which was also reactive with platelets.

Aged↗
PubMed1999

Changes in epididymal protein anti-agglutinin on ejaculated boar spermatozoa during capacitation in vitro.

This study is a detailed investigation of changes in epididymal protein anti-agglutinin on ejaculated boar spermatozoa during an incubation designed to promote capacitation in vitro. Ejaculated spermatozoa were collected from six mature boars, washed, and incubated to promote capacitation. Sperm samples were subjected to Western blotting-densitometric analyses, flow cytometry after immunostaining and immunocytochemical observation by indirect immunofluorescence. An antiserum to anti-agglutinin was raised in a rabbit by subcutaneous injection of a purified antigen, as described previously (Harayama et al. 1999). Western blotting-densitometric analyses revealed an approximate halving of the amount of sperm-bound anti-agglutinin during the first 45-min incubation, followed by a gradual decrease thereafter. Comparison between immunostained sperm samples by flow cytometry before and after incubation confirmed this decrease in sperm-bound anti-agglutinin during the incubation. Microscopic characterization established that this decrease occurred mainly on the acrosome. Supplementation with seminal plasma (5% or 10%, v/v) attenuated the decrease. These findings are consistent with the conclusion that a large portion of the anti-agglutinin bound to sperm acrosomes is released at an early stage of the capacitation process in vitro.

Acrosome Reaction↗
PubMed1996

Identification of a ligand-binding site in an immunoglobulin fold domain of the Saccharomyces cerevisiae adhesion protein alpha-agglutinin.

The Saccharomyces cerevisiae adhesion protein alpha-agglutinin (Ag alpha 1p) is expressed by alpha cells and binds to the complementary a-agglutinin expressed by a cells. The N-terminal half of alpha-agglutinin is sufficient for ligand binding and has been proposed to contain an immunoglobulin (Ig) fold domain. Based on a structural homology model for this domain and a previously identified critical residue (His292), we made Ag alpha 1p mutations in three discontinuous patches of the domain that are predicted to be in close proximity to His292 in the model. Residues in each of the three patches were identified that are important for activity and therefore define a putative ligand binding site, whereas mutations in distant loops had no effect on activity. This putative binding site is on a different surface of the Ig fold than the defined binding sites of immunoglobulins and other members of the Ig superfamily. Comparison of protein interaction sites by structural and mutational analysis has indicated that the area of surface contact is larger than the functional binding site identified by mutagenesis. The putative alpha-agglutinin binding site is therefore likely to identify residues that contribute to the functional binding site within a larger area that contacts a-agglutinin.

Amino Acid Sequence↗
PubMedDate not supplied

Lens culinaris agglutinin-reactive alpha-fetoprotein as a prognostic marker in patients with hepatocellular carcinoma undergoing transcatheter arterial chemoembolization.

Lens culinaris agglutinin-reactive alpha-fetoprotein (AFP-L3) is known to be a useful marker for the diagnosis of hepatocellular carcinoma (HCC). Recent studies have shown that positive AFP-L3 results after treatment predicts tumor recurrence and poor clinical outcome. This study was to evaluate the role of pretreatment AFP-L3 as a prognostic marker for response to transcatheter arterial chemoembolization (TACE) and survival in patients with HCC. Forty-six patients with HCC who underwent TACE were analyzed. Agglutinin-reactive AFP was measured by lectin-affinity electrophoresis coupled with antibody-affinity blotting. Agglutinin-reactive AFP results larger than 24.4% were considered to be positive. Agglutinin-reactive AFP fractions were positive in 32 patients. Agglutinin-reactive AFP-positive patients had poorer performance status, larger tumors, frequent portal vein thrombosis, and higher levels of serum AFP. The partial response rate to TACE was lower in AFP-L3-positive patients than in AFP-L3-negative ones (37.5% vs. 78.6%, p = 0.01). Tumor size and AFP-L3 were two independent predictive factors for response to TACE. The 2-year survival rate was lower in AFP-L3-positive patients than in AFP-L3-negative ones (21.2% vs. 78.6%, p = 0.01). Child-Pugh class, AFP-L3, the presence of portal vein thrombosis, and response to TACE were independent prognostic factors for survival. In conclusion, pretreatment status of AFP-L3 could be considered a useful marker for predicting clinical outcome in patients with HCC who underwent TACE.

Adult↗