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- Primary bone marrow lymphoma presenting with cold-type autoimmune hemolytic anemia. [Journal Article]
- Indian J Hematol Blood Transfus 2014 Sep; 30(Suppl 1):271-4.
We report a rare case of primary bone marrow lymphoma with cold-type autoimmune hemolytic anemia (AIHA). A 70-year-old Japanese woman with suspected liver disorder presented to our hospital with palpitation. On physical examination, she had jaundice and signs of anemia. No lymphadenopathy or hepatosplenomegaly was noted. A direct antiglobulin test was positive for complement C3b and C3d. Anti-IgG testing was negative. Cold agglutinin was positive with a titer of 1:≥8,192, and haptoglobin was absent. A diagnosis of cold-type AIHA was made. Bone marrow biopsy revealed involvement with a population of lymphocytes that were positive for CD20 (L-26), CD79a, and Bcl-2. No lymphoma lesion was detected on computerized tomography or on upper and lower endoscopy. The patient was diagnosed with diffuse large B cell lymphoma (DLBCL) presenting with cold-type AIHA. She was treated with rituximab, cyclophosphamide, doxorubicin, vincristine, and prednisolone, resulting in complete remission after six cycles. As of 22 months after presentation, no signs of cold-type AIHA or lymphoma were present.
- Anti-m antibody in solid tumors-two case reports. [Journal Article]
- Indian J Hematol Blood Transfus 2014 Sep; 30(Suppl 1):49-53.
Anti-M antibodies are usually of IgM, appear as cold agglutinins and are clinically insignificant. We are reporting two cases of anti-M in cases of solid tumors where the anti-M caused discrepancy in blood grouping, reacted in coombs phase of crossmatching. Anti-M in first case showed dosage effect. These antibodies can be clinical significant when detected in coombs phase, making M antigen negative coombs compatible unit transfusion imperative.
- A Model for Cell Wall Dissolution in Mating Yeast Cells: Polarized Secretion and Restricted Diffusion of Cell Wall Remodeling Enzymes Induces Local Dissolution. [JOURNAL ARTICLE]
- PLoS One 2014; 9(10):e109780.
Mating of the budding yeast, Saccharomyces cerevisiae, occurs when two haploid cells of opposite mating types signal using reciprocal pheromones and receptors, grow towards each other, and fuse to form a single diploid cell. To fuse, both cells dissolve their cell walls at the point of contact. This event must be carefully controlled because the osmotic pressure differential between the cytoplasm and extracellular environment causes cells with unprotected plasma membranes to lyse. If the cell wall-degrading enzymes diffuse through the cell wall, their concentration would rise when two cells touched each other, such as when two pheromone-stimulated cells adhere to each other via mating agglutinins. At the surfaces that touch, the enzymes must diffuse laterally through the wall before they can escape into the medium, increasing the time the enzymes spend in the cell wall, and thus raising their concentration at the point of attachment and restricting cell wall dissolution to points where cells touch each other. We tested this hypothesis by studying pheromone treated cells confined between two solid, impermeable surfaces. This confinement increases the frequency of pheromone-induced cell death, and this effect is diminished by reducing the osmotic pressure difference across the cell wall or by deleting putative cell wall glucanases and other genes necessary for efficient cell wall fusion. Our results support the model that pheromone-induced cell death is the result of a contact-driven increase in the local concentration of cell wall remodeling enzymes and suggest that this process plays an important role in regulating cell wall dissolution and fusion in mating cells.
- Lectin purification from fruiting bodies of brown roll-rim fungus, Paxillus involutus (Fr.) Fr., and its application in histochemistry. [JOURNAL ARTICLE]
- Rom J Morphol Embryol 2014; 55(3):787-796.
A lectin (agglutinin) from fresh fruit bodies of the brown roll-rim fungus [Paxillus involutus (Fr.) Fr.] has been purified with output approx. 60 mg÷kg of raw material. Method of purification included the sedimentation of viscous polysaccharide by ethanol, removal of ethanol by dialysis, ion-exchange chromatography on DEAE-Toyopearl and affinity chromatography on Sepharose 6B column with immobilized mannose-specific Polygonatum multiflorum lectin. The obtained lectin preparation (abbreviated PIFA) is a glycoprotein with 6.5±1% carbohydrates, molecular mass of 64 kDa, consisting of four identical subunits. Lectin interacted only with N-acetyl-lactosamine and glycoproteins that contained Galβ1-4GlcNAc disaccharide moieties; agglutinated erythrocytes of dog, sheep and horse, but not of humans. The specificity of PIFA binding to tissue samples of the rat has been investigated. Lectin selectively reacted with gastric parietal cells, submandibular salivary gland duct cells. In the kidney, PIFA labeled epithelial cells of renal tubules, collecting ducts, nuclei of podocytes and mesangiocytes. It was also revealed selective lectin binding to Purkinje cells of cerebellum. Brush border of absorptive cells in small intestine was also strongly reactive, while goblet cells both in small and large intestine were completely negative. Considering similarities in carbohydrate specificity of Paxillus involutus (PIFA) and Ricinus communis agglutinin (RCA-120), histochemical reactivity of these two lectins was compared. It was similar, yet not identical: differences included absence of PIFA binding to the brush border of renal tubules, higher interaction with absorptive cells of the small intestine, lower background staining of cerebellar cortex and renal corpuscles. A conclusion was made that due to the unique carbohydrate specificity PIFA lectin can cover prospective position in experimental histochemistry and diagnostic histopathology comparable to PNA (Peanut agglutinin) and SNA (Sambucus nigra agglutinin).
- Peanut agglutinin appearance in the blood circulation after peanut ingestion mimics the action of endogenous galactin-3 to promote metastasis by interaction with cancer-associated MUC1. [JOURNAL ARTICLE]
- Carcinogenesis 2014 Oct 17.
Peanut agglutinin (PNA), which accounts for about 0.15% of the weight of the common peanut, is a carbohydrate-binding protein that binds the oncofetal Thomsen-Friedenreich disaccharide (galactoseβ1,3N-acetylgalactosamine-, TF) that is over-expressed by about 90% of human cancers. Previous studies have shown that PNA is highly resistant to cooking and digestion and rapidly enters the human blood circulation after peanut ingestion. This study investigates the hypothesis that PNA appearance in the circulation after peanut ingestion may mimic the actions of endogenous TF-binding human galectin-3 in metastasis promotion. It shows that PNA at concentrations similar to those found in blood circulation after peanut ingestion increases cancer cell heterotypic adhesion to the blood vascular endothelium and enhances the formation of tumour cell homotypic aggregates, two important steps in the metastasis cascade, and enhances metastasis in a mouse metastasis model. These effects of PNA are shown to result from its interaction with the cancer-associated TF disaccharide on the transmembrane mucin protein MUC1, causing MUC1 cell surface polarization that reveals underlying cell surface adhesion molecules. Thus, PNA appearance in the blood circulation after peanut ingestion mimics the actions of endogenous galectin-3 and promotes cancer cell metastatic spread by interaction with cancer-associated TF/MUC1. As metastasis accounts for the majority of cancer-associated fatality, regular consumption of peanuts by cancer patients would therefore be expected to have an adverse effect on cancer survival.
- Association between Wisteria floribunda agglutinin-positive Mac-2 binding protein and the fibrosis stage of non-alcoholic fatty liver disease. [JOURNAL ARTICLE]
- J Gastroenterol 2014 Oct 18.
Accurately evaluating liver fibrosis in patients with non-alcoholic fatty liver disease (NAFLD) is important for identifying those who may develop complications. The aims of this study were (1) to measure serum Wisteria floribunda agglutinin-positive Mac-2 binding protein (WFA(+)-M2BP) using the glycan sugar chain-based immunoassay and (2) to compare the results with clinical assessments of fibrosis.Serum WFA(+)-M2BP values were retrospectively evaluated in 289 patients with NAFLD who had undergone liver biopsy. Histological findings were evaluated by three blinded, experienced liver-specific pathologists.For stages 0 (n = 35), 1 (n = 113), 2 (n = 49), 3 (n = 41), and 4 (n = 51) of liver fibrosis, the serum WFA(+)-M2BP cutoff indexes were 0.57, 0.70, 1.02, 1.57, and 2.96, respectively. Multivariate regression analysis showed that serum WFA(+)-M2BP values were associated with the stage of fibrosis (≥stage 2). The areas under the receiver operating characteristic curve (AUROC), sensitivity, and specificity of serum WFA(+)-M2BP were 0.876, 85.9, and 74.6 %, respectively, for severe fibrosis (≥stage 3) and were 0.879, 74.6, and 87.0 %, respectively, for cirrhosis. When compared with six non-invasive conventional markers, serum WFA(+)-M2BP had the greatest AUROC for diagnosing severe fibrosis and cirrhosis.Serum WFA(+)-M2BP values are useful for assessing the stage of liver fibrosis in patients with NAFLD.
- The Salivary Scavenger and Agglutinin in Early Life: Diverse Roles in Amniotic Fluid and in the Infant Intestine. [JOURNAL ARTICLE]
- J Immunol 2014 Oct 15.
The salivary scavenger and agglutinin (SALSA), also known as gp340 and dmbt1, is an antimicrobial and inflammation-regulating molecule located at the mucosal surfaces. The present study revealed that SALSA was present in the amniotic fluid (AF) and exceptionally enriched in both meconium and feces of infants. Based on immunological and mass spectrometric analysis, SALSA was estimated to constitute up to 4-10% of the total protein amount in meconium, making it one of the most abundant proteins. SALSA proteins in the AF and intestinal samples were polymorphic and exhibited varying polypeptide compositions. In particular, a different abundance of peptides corresponding to functionally important structures was found in the AF and intestinal SALSA. The AF form of SALSA had a more intact structure and contained peptides from the zona pellucida domain, which is involved in cell differentiation and oligomerization. In contrast, the intestinal SALSA was more enriched with the scavenger receptor cysteine-rich domains. The AF, but not the meconium SALSA, bound to Streptococcus pyogenes, S. agalactiae, S. gordonii, and Escherichia coli. Furthermore, differential binding was observed also to known endogenous ligands C1q, mannose-binding lectin, and secretory IgA. Our results have thus identified mucosal body compartments, where SALSA is particularly abundant, and suggest that SALSA exhibits varying functions in the different mucosal locations. The high levels of SALSA in AF and the infant intestine suggest a robust and important function for SALSA during the fetal development and in the mucosal innate immune defense of infants.
- Salivary Glyco-sialylation changes monitors oral carcinogenesis. [JOURNAL ARTICLE]
- Glycoconj J 2014 Oct 16.
Alterations in cell membrane glycosylation play important role in oral carcinogenesis. The present study evaluated salivary sialylation changes i.e. total sialic acid (TSA), sialidase activity, linkage specific (α2-3 and α2-6) sialoproteins and sialyl transferase (ST) activity in controls, patients with oral precancerous conditions (OPC) and oral cancer. Subjects enrolled included 100 controls, 50 patients with OPC, 100 oral cancer patients, and 30 post treatment follow-ups. TSA was estimated by spectrophotometric method, sialidase activity by spectrofluorometric assay and linkage specific biotinylated lectins (α2-3: sambucus nigra agglutinin and α2-6: maackia amurensis agglutinin) were used to detect α-2,3 and α-2,6 STs and sialoproteins by ELISA and dot blot respectively. An increasing trend of salivary TSA/TP ratio, sialidase activity, α2-3 sialoproteins, α-2,3 and α-2,6 ST activities was observed from controls to patients with OPC to oral cancer patients and levels were significantly elevated in oral cancer patients as compared to the controls. Sialidase activity exhibited significant association with metastasis and infiltration. Sialidase activity, TSA/TP ratio, α-2,3 and α-2,6 ST activities were found to be higher in patients with metastasis as compared to patients without metastasis. A progressive increase in TSA/TP ratio, sialidase activity, α2-3 and α2-6 sialoproteins was observed from controls to early to advanced stage of the disease. Sialidase activity, α2-3 and α2-6 sialoproteins and ST activities were found to be decreased in complete responders; while levels were elevated in non-responders. The results documented utility of salivary sialylation endpoints, a non invasive tool in monitoring of oral carcinogenesis.
- Determination of Multivalent Protein-Ligand Binding Kinetics Using Second Harmonic Correlation Spectroscopy. [JOURNAL ARTICLE]
- Anal Chem 2014 Oct 14.
The binding kinetics and thermodynamics of the multivalent proteins, peanut agglutinin (PnA) and cholera toxin subunit b (CTb), to a GM1 doped 1,2-dioleoyl-sn-glycero-3-phosphocoline (DOPC) lipid bilayer were investigated using both second harmonic correlation spectroscopy (SHCS) and a traditional equilibrium binding isotherm. The adsorption and desorption rates, as well as the binding affinity and binding free energy, for 3 bulk protein concentrations were determined using SHCS. This is the first study to extend SHCS to the examination of multivalent protein-ligand interactions at a surface. For PnA binding to GM1, the measured adsorption rate decreased with increasing bulk PnA concentration from 3.9 ± 0.7 × 106 M-1s-1 at 0.43 μM PnA to 1.2 ± 0.1 × 105 M-1s-1 at 12 μM PnA. CTb-GM1 exhibited a similar trend decreasing from 1.0 ± 0.1 × 109 M-1s-1 at 0.5 nM CTb to 4.0 ± 0.3 × 106 M-1s-1 at 240 nM CTb. The measured desorption rates in both studies did not exhibit any dependence on initial protein concentration. As such, 0.43 μM PnA and 0.5 nM CTb had the strongest measured binding affinities, 2.2 ± 0.7 × 109 M-1 and 5.9 ± 1.4 × 1013 M-1, respectively. Analysis of the binding isotherm data suggests there is electrostatic repulsion between protein molecules when PnA binds GM1, while CTb-GM1 demonstrates positive ligand cooperativity. This study provides additional insight into the complex interactions between multivalent proteins and their ligands, and showcases SHCS for examining these complex yet technologically important protein-ligand complexes used in biosensors, immunoassays, and other biomedical diagnostics.
- A chromophore-containing agglutinin from Haliclona manglaris: purification and biochemical characterization. [JOURNAL ARTICLE]
- Int J Biol Macromol 2014 Oct 10.
A new chromophore-containing agglutinin (Haliclona manglaris agglutinin (HMA)) was isolated from the tropical sponge Haliclona manglaris. HMA was purified by a combination of hydrophobic interaction chromatography and ion exchange chromatography. Native HMA is a heterotrimer formed by two β-chains (15kDa) and one α-chain (22kDa). HMA is a glycoprotein and possesses three intrachain disulfide bonds. Hemagglutinating activity of HMA was stable at neutral pH and temperatures up to 60°C. HMA was only inhibited by thyroglobulin. Mass spectrometry sequencing and Edman degradation revealed a unique amino acid sequence of about 30%. Moreover, HMA has an organic chromophore of 581Da, and this characteristic seems to be important to its antioxidant activity. Interestingly, while HMA showed no toxicity against Artemia nauplii and was unable to agglutinate bacterial cells, it did show a high capacity to protect β-carotene against oxidation. Thus, our findings suggest the putative involvement of HMA in the protection of the sponge against oxidation.