Databases, Protein: Databases containing information about PROTEINS such as AMINO ACID SEQUENCE; PROTEIN CONFORMATION; and other properties.Internet: A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.User-Computer Interface: The portion of an interactive computer program that issues messages to and receives commands from a user.Software: Sequential operating programs and data which instruct the functioning of a digital computer.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Sequence Analysis, Protein: A process that includes the determination of AMINO ACID SEQUENCE of a protein (or peptide, oligopeptide or peptide fragment) and the information analysis of the sequence.Computational Biology: A field of biology concerned with the development of techniques for the collection and manipulation of biological data, and the use of such data to make biological discoveries or predictions. This field encompasses all computational methods and theories for solving biological problems including manipulation of models and datasets.Anemia, Hemolytic, Autoimmune: Acquired hemolytic anemia due to the presence of AUTOANTIBODIES which agglutinate or lyse the patient's own RED BLOOD CELLS.Coombs Test: A test to detect non-agglutinating ANTIBODIES against ERYTHROCYTES by use of anti-antibodies (the Coombs' reagent.) The direct test is applied to freshly drawn blood to detect antibody bound to circulating red cells. The indirect test is applied to serum to detect the presence of antibodies that can bind to red blood cells.Agglutinins: Substances, usually of biological origin, that cause cells or other organic particles to aggregate and stick to each other. They include those ANTIBODIES which cause aggregation or agglutination of particulate or insoluble ANTIGENS.Cryoglobulins: Abnormal immunoglobulins, especially IGG or IGM, that precipitate spontaneously when SERUM is cooled below 37 degrees Celsius. It is characteristic of CRYOGLOBULINEMIA.Anemia, Hemolytic: A condition of inadequate circulating red blood cells (ANEMIA) or insufficient HEMOGLOBIN due to premature destruction of red blood cells (ERYTHROCYTES).Cold Temperature: An absence of warmth or heat or a temperature notably below an accustomed norm.Hemolysis: The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.Peanut Agglutinin: Lectin purified from peanuts (ARACHIS HYPOGAEA). It binds to poorly differentiated cells and terminally differentiated cells and is used in cell separation techniques.MNSs Blood-Group System: A system of universal human blood group isoantigens with many associated subgroups. The M and N traits are codominant and the S and s traits are probably very closely linked alleles, including the U antigen. This system is most frequently used in paternity studies.Lectins: Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.Arachis hypogaea: A plant species of the family FABACEAE that yields edible seeds, the familiar peanuts, which contain protein, oil and lectins.Plant Lectins: Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.Glycoconjugates: Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed)Portal Vein: A short thick vein formed by union of the superior mesenteric vein and the splenic vein.Protein Array Analysis: Ligand-binding assays that measure protein-protein, protein-small molecule, or protein-nucleic acid interactions using a very large set of capturing molecules, i.e., those attached separately on a solid support, to measure the presence or interaction of target molecules in the sample.Hemagglutination Inhibition Tests: Serologic tests in which a known quantity of antigen is added to the serum prior to the addition of a red cell suspension. Reaction result is expressed as the smallest amount of antigen which causes complete inhibition of hemagglutination.Neuraminidase: An enzyme that catalyzes the hydrolysis of alpha-2,3, alpha-2,6-, and alpha-2,8-glycosidic linkages (at a decreasing rate, respectively) of terminal sialic residues in oligosaccharides, glycoproteins, glycolipids, colominic acid, and synthetic substrate. (From Enzyme Nomenclature, 1992)Organisms, Genetically Modified: Organisms whose GENOME has been changed by a GENETIC ENGINEERING technique.Chick Embryo: The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.Dictionaries, MedicalAgglutination Tests: Tests that are dependent on the clumping of cells, microorganisms, or particles when mixed with specific antiserum. (From Stedman, 26th ed)Dictionaries as Topic: Lists of words, usually in alphabetical order, giving information about form, pronunciation, etymology, grammar, and meaning.Wheat Germ Agglutinins: Lectins purified from the germinating seeds of common wheat (Triticum vulgare); these bind to certain carbohydrate moieties on cell surface glycoproteins and are used to identify certain cell populations and inhibit or promote some immunological or physiological activities. There are at least two isoforms of this lectin.Dictionaries, ChemicalTulipa: A plant genus of the family LILIACEAE. Members contain tuliposides and tulipalins and have been associated with allergic contact dermatitis in florists.Saccharomyces: A genus of ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES.Mollusk Venoms: Venoms from mollusks, including CONUS and OCTOPUS species. The venoms contain proteins, enzymes, choline derivatives, slow-reacting substances, and several characterized polypeptide toxins that affect the nervous system. Mollusk venoms include cephalotoxin, venerupin, maculotoxin, surugatoxin, conotoxins, and murexine.Mycoplasma pneumoniae: Short filamentous organism of the genus Mycoplasma, which binds firmly to the cells of the respiratory epithelium. It is one of the etiologic agents of non-viral primary atypical pneumonia in man.Anemia, Hemolytic, Congenital: Hemolytic anemia due to various intrinsic defects of the erythrocyte.Polysaccharides, Bacterial: Polysaccharides found in bacteria and in capsules thereof.Agglutination: The clumping together of suspended material resulting from the action of AGGLUTININS.Streptococcus pneumoniae: A gram-positive organism found in the upper respiratory tract, inflammatory exudates, and various body fluids of normal and/or diseased humans and, rarely, domestic animals.Pneumococcal Infections: Infections with bacteria of the species STREPTOCOCCUS PNEUMONIAE.PolysaccharidesCharities: Social welfare organizations with programs designed to assist individuals in need.Hematology: A subspecialty of internal medicine concerned with morphology, physiology, and pathology of the blood and blood-forming tissues.Lions: Large, chiefly nocturnal mammals of the cat family FELIDAE, species Panthera leo. They are found in Africa and southern Asia.Societies, Medical: Societies whose membership is limited to physicians.Brachyura: An infraorder of chiefly marine, largely carnivorous CRUSTACEA, in the order DECAPODA, including the genera Cancer, Uca, and Callinectes.ThyroglobulinHemolymph: The blood/lymphlike nutrient fluid of some invertebrates.Sialic Acids: A group of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are ubiquitously distributed in many tissues.N-Acetylneuraminic Acid: An N-acyl derivative of neuraminic acid. N-acetylneuraminic acid occurs in many polysaccharides, glycoproteins, and glycolipids in animals and bacteria. (From Dorland, 28th ed, p1518)Neuraminic Acids

Some leptospira agglutinins detected in domestic animals in British Columbia. (1/437)

During a period of six years 7,555 bovine sera, 421 canine sera, 251 porcine sera and 135 equine sera were tested for agglutinins to Leptospira interrogans serotypes canicola, grippotyphosa, hardjo, icterohemorrhagiae, pomona and sejroe. The bovine sera reacted predominantly with hardjo and/or sejroe at a rate of 15% compared to 3.5% with pomona. Breeding or abortion problems were associated with pomona but not with sejroe/hardjo agglutinins. The canine sera reacted to canicola (9.9%y and icterohemorrhagiae (5.4%), tcted predominantly with canicola (8.9%) and icterohemorrhagiae (8.1%).  (+info)

Platelet high affinity low density lipoprotein binding and import of lipoprotein derived phospholipids. (2/437)

The binding of low density lipoprotein (LDL) to the platelet cell membrane could facilitate the transfer of phospholipids from LDL to the platelets. A polyclonal antibody against the platelet glycoproteins IIb/IIIa inhibited the high affinity binding of 125I-LDL by up to 80%. The transfer of pyrene (py)-labeled sphingomyelin (SM), phosphatidylcholine and phosphatidylethanolamine from LDL to the platelets was unaffected by the antibody. The lectin wheat germ agglutinin (WGA) reduced the binding of 125I-LDL to the platelets by approximately 80%. In contrast, the lectin stimulated the transfer of SM from LDL into the platelets by about three-fold. WGA also specifically augmented the transfer of py-SM between lipid vesicles and the platelets, the stimulation being abolished in the presence of N-acetylglucosamine. Dextran sulfate (DS) increased the specific binding of 125I-LDL to the platelets by up to 2.8-fold. On the other hand, the import of LDL-derived py-phospholipids was unaffected by DS. Together, the results indicate that the phospholipid transfer from LDL to the platelets is independent of the high affinity LDL binding to the platelets and is specifically stimulated by WGA. Thus, the interactions of platelets with LDL phospholipids differ markedly from those with the apoprotein components of the lipoproteins.  (+info)

Role of nonagglutinating antibody in the protracted immunity of vaccinated mice to Pseudomonas aeruginosa infection. (3/437)

Effective immunization against infection with Pseudomonas aeruginosa is difficult to evaluate because agglutinin levels decline rapidly. Because fractionation of hyperimmune sera often yields more specific antibody than can be accounted for by direct agglutination tests, an immunoglobulin-specific assay based on antiglobulin augmentation was used to characterize antibody responses of C3H/HeJ mice vaccinated with P. aeruginosa type 2 lipopolysaccharide. Nonagglutinating antibodies, initially detected at 2 weeks post-primary vaccination, were predominantly immunoglobulin G after 5 weeks, and they remained elevated at levels usually 32-fold higher than the direct titer throughout the 4-month study period. The sequential production of immunoglobulin M, then immunoglobulin G, followed that found in orthodox immunological responses. Sera that contained nonagglutinating antibodies but not direct agglutinins (14 to 16 weeks) enhanced phagocytosis of P. aeruginosa type 2 by macrophages from unimmunized mice and passively immunized mice against lethal challenge doses; bactericidal activity of these sera was not demonstrated in the presence or absence of complement. When challenged with 1, 10, and 100 50% lethal doses at 16 weeks, survival rates of actively immunized mice were significantly higher than those of unvaccinated mice (P < 0.001). Thus, at a time when no direct agglutinins were detectable, the augmented system detected nonagglutinating antibodies that could confer protracted resistance in vaccinated mice to pseudomonas infection.  (+info)

Expression of DMBT1, a candidate tumor suppressor gene, is frequently lost in lung cancer. (4/437)

DMBT1 is a candidate tumor suppressor gene located at 10q25.3-26.1. Homozygous deletion of the gene was found in a subset of medulloblastoma and glioblastoma multiforme; lack of expression was noted in the majority of these tumors. In adult tissues, DMBT1 is highly expressed only in lung and small intestine tissues, indicating its important role in these organs. By analyzing lung cancer cell lines and primary lung tumors using reverse transcription-PCR, we found that 100% (20 of 20) of small cell lung cancer (SCLC) cell lines and 43% (6 of 14) of non-small cell lung cancer (NSCLC) cell lines lacked DMBT1 expression. Furthermore, 45% (9 of 20) of the primary NSCLCs exhibited a markedly low level of gene expression compared with corresponding normal lung tissues, indicating that lack of gene expression also occurs in primary lung cancers. To determine the potential mechanisms for lack of DMBT1 expression in lung cancer, we analyzed tumor cell lines for potential intragenic homozygous deletions of the gene and found such homozygous deletions in 10% (4 of 40) of SCLC cell lines but in none of 14 NSCLC cell lines. Moreover, the loss of expression could not be rescued by treatment with a demethylation agent (5-azacytidine) in two NSCLC cell lines lacking DMBT1 expression, suggesting that de novo methylation of the promoter region of the gene is unlikely to play a role in inactivation of the gene. We then sequenced the whole coding region of DMBT1 in 8 NSCLC cell lines that expressed DMBT1 and 20 primary NSCLCs. A potential point mutation at codon 52 was detected in a NSCLC cell line and resulted in an amino acid change from serine to tryptophan. Three common polymorphisms were also detected in tissues analyzed. Our data demonstrate that DMBT1 expression is frequently lost in lung cancer due to gene deletion and to other not yet identified mechanisms, suggesting that inactivation of DMBT1 may play an important role in lung tumorigenesis.  (+info)

Complement receptor 1 (CD35) on human reticulocytes: normal expression in systemic lupus erythematosus and HIV-infected patients. (5/437)

The low levels of complement receptor 1 (CR1) on erythrocytes in autoimmune diseases and AIDS may be due to accelerated loss in the circulation, or to a diminished expression of CR1 on the red cell lineage. Therefore, we analyzed the expression of CR1 on reticulocytes (R) vs erythrocytes (E). Healthy subjects had a significant higher CR1 number per cell on R (919 +/- 99 CR1/cell) than on E (279 +/- 30 CR1/cell, n = 23), which corresponded to a 3. 5- +/- 1.3-fold loss of CR1. This intravascular loss was confirmed by FACS analysis, which showed that all R expressed CR1, whereas a large fraction of E was negative. The systemic lupus erythematosus (SLE), HIV-infected, and cold hemolytic Ab disease (CHAD) patients had a CR1 number on R identical to the healthy subjects, contrasting with a lower CR1 on their E. The data indicated a significantly higher loss of CR1 in the three diseases, i.e., 7.0- +/- 3.8-, 6.1- +/- 2.9-, and 9.6- +/- 5.6-fold, respectively. The intravascular loss was best exemplified in a patient with factor I deficiency whose CR1 dropped from 520 CR1/R to 28 CR1/E, i.e., 18.6-fold loss. In one SLE patient and in the factor I-deficient patient, the FACS data were consistent with a loss of CR1 already on some R. In conclusion, CR1 is lost progressively from normal E during in vivo aging so that old E are almost devoid of CR1. The low CR1 of RBC in autoimmune diseases and HIV-infection is due to a loss occurring in the circulation by an active process that remains to be defined.  (+info)

Hensin, the polarity reversal protein, is encoded by DMBT1, a gene frequently deleted in malignant gliomas. (6/437)

The band 3 anion exchanger is located in the apical membrane of a beta-intercalated clonal cell line, whereas the vacuolar H(+)-ATPase is present in the basolateral membrane. When these cells were seeded at confluent density, they converted to an alpha-phenotype, localizing each of these proteins to the opposite cell membrane domain. The reversal of polarity is induced by hensin, a 230-kDa extracellular matrix protein. Rabbit kidney hensin is a multidomain protein composed of eight SRCR ("scavenger receptor, cysteine rich"), two CUB ("C1r/C1s Uegf Bmp1"), and one ZP ("zona pellucida") domain. Other proteins known to have these domains include CRP-ductin, a cDNA expressed at high levels in mouse intestine (8 SRCR, 5 CUB, 1 ZP), ebnerin, a protein cloned from a rat taste bud library (4 SRCR, 3 CUB, 1 ZP), and DMBT1, a sequence in human chromosome 10q25-26 frequently deleted in malignant gliomas (9 SRCR, 2 CUB, 1 ZP). Rabbit and mouse hensin genomic clones contained a new SRCR that was not found in hensin cDNA but was homologous to the first SRCR domain in DMBT1. Furthermore, the 3'-untranslated regions and the signal peptide of hensin were homologous to those of DMBT1. Mouse genomic hensin was localized to chromosome 7 band F4, which is syntenic to human 10q25-26. These data suggest that hensin and DMBT1 are alternatively spliced forms of the same gene. The analysis of mouse hensin bacterial artificial chromosome (BAC) genomic clone by sequencing and Southern hybridization revealed that the gene also likely encodes CRP-ductin. A new antibody against the mouse SRCR1 domain recognized a protein in the mouse and rabbit brain but not in the immortalized cell line or kidney, whereas an antibody to SRCR6 and SRCR7 domains which are present in all the transcripts, recognized proteins in intestine, kidney, and brain from several species. The most likely interpretation of these data is that one gene produces at least three transcripts, namely, hensin, DMBT1, and CRP-ductin. Hensin may participate in determining the polarized phenotype of other epithelia and brain cells.  (+info)

The extracellular matrix in the mouse brain: its reactions to endo-alpha-N-acetylgalactosaminidase and certain other enzymes. (7/437)

As our previous studies have indicated, the cingulate cortex of the adult mouse brain contains many neurons with rich cell surface glycoproteins which are linked by collagenous ligands to perineuronal proteoglycans. The present study demonstrated that exclusive incubation with endo-alpha-N-acetylgalactosaminidase abolished the lectin Vicia villosa or Wisteria floribunda agglutinin (VVA or WFA) labeling of the nerve cell surface glycoproteins, while it neither interfered with the cationic iron colloid or aldehyde fuchsin stainings of the perineuronal proteoglycans nor abolished the Gomori's ammoniacal silver impregnation of the collagenous ligands. Double incubations with endo-alpha-N-acetylgalactosaminidase and collagenase did not eliminate the lectin VVA or WFA labeling of the nerve cell surface glycoproteins, though they did eliminate the cationic iron colloid and aldehyde fuchsin stainings of the perineuronal proteoglycans as well as the Gomori's ammoniacal silver impregnation of the collagenous ligands. Triple incubations with endo-alpha-N-acetylgalactosaminidase, collagenase, and endo-alpha-N-acetylgalactosaminidase abolished the lectin VVA or WFA labeling of the nerve cell surface glycoproteins, and also eliminated the cationic iron colloid and aldehyde fuchsin stainings of the perineuronal proteoglycans and the Gomori's ammoniacal silver impregnation of the collagenous ligands. These findings indicate that: the nerve cell surface glycoproteins or their terminal N-acetylgalactosamines are digested by endo-alpha-N-acetylgalactosaminidase; these galactosamines associated with the collagenous ligands or perineuronal proteoglycans are not digested by endo-alpha-N-acetylgalactosaminidase; and the terminal N-acetylgalactosamines newly exposed by collagenase incubation are digested by this galactosaminidase. It was further demonstrated that hyaluronidase incubation neither digests the collagenous ligands nor revives the lectin VVA or WFA labeling of the nerve cell surface proteoglycans.  (+info)

Purification and characterization of a natural agglutinin from the serum of the hermit crab Diogenes affinis. (8/437)

A natural agglutinin from the serum of the hermit crab Diogenes affinis was purified to homogeneity by a single-step affinity chromatography using N-acetylglucosamine-coupled Sepharose 6B. The purified serum agglutinin (PSA) showed a strong affinity for rat RBC, and its hemagglutinating (HA) activity was specifically dependent on Ca2+ and reversibly sensitive to EDTA. PSA in active form has a molecular mass estimate of 185 kDa and is composed of four non-identical subunits (51, 49, 42 and 39 kDa) cross-linked by interchain disulfide bonds. The homogeneity of PSA was corroborated by immunodiffusion and immunoelectrophoretic analyses using rabbit antiserum raised against the agglutinin. The antibodies in this antiserum appear to be specific for RBC-binding sites of the agglutinin molecules as revealed by the ability of the antiserum to neutralize HA activities of both whole serum and PSA of D. affinis. In HA-inhibition assays performed with several carbohydrates and glycoproteins, PSA showed a distinct and unique specificity for acetyl group in carbohydrates independently of the presence of this group on C-2 or C-5 and its stereochemical arrangement in the axial or equatorial orientation. Besides, this agglutinin appears to recognize the terminal N- and O- acetyl groups in the oligosaccharide chain of glycoconjugates. The HA activity of D. affinis agglutinin was also susceptible to inhibition by lipopolysaccharides from diverse gram-negative bacteria, which might indicate a significant in vivo role of this humoral agglutinin in the host immune response against bacterial infections.  (+info)

  • Cryoglobulinemia was noted, and the cryoglobulin was identified as IgM-IgG with anti-I cold agglutinin activity. (cmaj.ca)
  • The cold agglutinins possessed potent lymphocytotoxic and monocytotoxic activity and weaker granulocytotoxic activity. (cmaj.ca)
  • Saccharomyces cerevisiae A and alpha cells express the complementary cell surface glycoproteins A-agglutinin and alpha-, respectively, which interact with one another to promote cellular aggregation during mating. (mybiosource.com)
  • Biotinylated Soybean agglutinin has an appropriate number of biotins bound to provide the optimum staining characteristics for this lectin. (vectorlabs.com)
  • In the digital image above, a rat esophagus tissue section is presented that was labeled with the fluorophore Oregon Green 488 conjugated to wheat germ agglutinin, a fluorescent lectin that selectively binds to sialic acid residues. (microscopyu.com)
  • In short, H. cervicornis agglutinin showed important antinociceptive and anti-inflamatory activity via interaction with the lectin carbohydrate-binding site. (springer.com)
  • Wheat germ agglutinin, a C-type lectin and known label for TNTs, unexpectedly caused striking induction of TNTs. (whiterose.ac.uk)
  • Pinellia ternata leaf agglutinin gene ( pta ), encodes an insecticidal lectin, was isolated and cloned under the 35S and rolC promoters in the pGA482 plant transformation vector for Agrobacterium -mediated tobacco transformation. (ejbiotechnology.info)
  • Their binding ability towards wheat germ agglutinin was measured by competitive enzyme-linked lectin assays. (beilstein-journals.org)
  • The full-length cDNA of Arisaema lobatum agglutinin ( ala ) was 1078 bp and contained a 774 bp open reading frame encoding a lectin precursor (proproprotein) of 258 amino acid residues with a 23 aa signal peptide. (bioscirep.org)
  • We have synthesized a series of multivalent N-acetylglucosamine (GlcNAc) derivatives and studied their interaction with the plant lectin wheat germ agglutinin (WGA) by an enzyme-linked lectin assay (ELLA) and X-ray crystallography. (uni-konstanz.de)
  • Glanthus Nivalis Agglutinin (GNA) is a mannose binding lectin which has tendency for specific recognition and reversible binding to the sugar moieties of a wide variety of glycoproteins of enveloped viruses. (elsevier.com)
  • Roelcke D. The Lud cold agglutinin: a further antibody recognizing N-acetylneuraminic acid-determined antigens not fully expressed at birth. (medscape.com)
  • Cold agglutinin disease usually results from the production of a specific IgM antibody directed against the I/i antigens (precursors of the ABH and Lewis blood group substances) on red blood cells (RBCs). (medscape.com)
  • Cold agglutinins commonly have variable heavy-chain regions encoded by VH, with a distinct idiotype identified by the 9G4 rat murine monoclonal antibody. (medscape.com)
  • Other tests to detect cold agglutinin disease include complete blood count ( CBC ) to detect abnormal clumping (agglutination) of red blood cells, a physical examination for spleen or liver enlargement, and antiglobulin test (Coombs test) to detect the presence of a specific type of antibody (immunoglobulin M, or IgM). (rxlist.com)
  • Medical treatments for cold agglutinin disease include rituximab (Rituxan), a drug that is an antibody that selectively reduces specific types of immune cells). (rxlist.com)
  • Cold agglutinin disease (cold antibody hemolytic anemia) is a rare autoimmune disorder characterized by the premature destruction of red blood cells by the body's natural defenses against invading organisms (antibodies). (rarediseases.org)
  • Erythrocytes also may be agglutinated by agglutinins that are naturally present in the blood, such as the presence of anti A antibody in humans with the blood group B erythrocytes, or such agglutinins may also be formed in response to the entrance of noncompatible blood cells into the bloodstream. (thefreedictionary.com)
  • PARIS - November 14, 2020 - The U.S. Food and Drug Administration issued a Complete Response Letter (CRL) regarding the Biologics License Application (BLA) for sutimlimab, an investigational monoclonal antibody for the treatment of hemolysis in adults with cold agglutinin disease. (yahoo.com)
  • Sutimlimab is a humanized anti-C1s IgG4 monoclonal antibody that blocks the classical complement pathway-specific protease C1s and prevents further hemolysis in patients with cold agglutinin disease. (mdedge.com)
  • Several factors play a role in determining the ability of a cold agglutinin to induce a haemolytic anaemia such as antibody concentration and temperature range, in particular the highest temperature at which antibodies interact with red blood cells. (biomedcentral.com)
  • Studies on rats fed SBA had complex changes: With increasing doses of soybean agglutinin, the activities of aspartate aminotransferase linearly increased in plasma and decreased plasma insulin content without decrease in blood glucose levels. (wikipedia.org)
  • Consumption of soybean agglutinin resulted in a depletion of lipid and an overgrowth of small intestine and pancreas in rats. (wikipedia.org)
  • Meanwhile, poor growth of spleen and kidneys and pancreatic hypertrophy was observed in the soybean agglutinin-fed rats. (wikipedia.org)
  • Composed of four subunits of approximately equal size, soybean agglutinin is a family of closely related isolectins. (vectorlabs.com)
  • Abstract: Soybean agglutinin (SBA), is a non-fiber carbohydrate related protein and a major anti-nutritional factor. (mdpi.com)
  • Pan L, Zhao Y, Farouk MH, Bao N, Wang T, Qin G. Integrins Were Involved in Soybean Agglutinin Induced Cell Apoptosis in IPEC-J2. (mdpi.com)
  • Salivary agglutinin is a 300-400kDa salivary glycoprotein that binds to antigen B polypeptides of oral streptococci, thereby playing a role in their colonization and the development of caries. (biochemj.org)
  • It was shown by Western blotting that monoclonal antibodies against gp-340 reacted with salivary agglutinin, and monoclonals against agglutinin reacted with gp-340. (biochemj.org)
  • Leicester Research Archive: Evolution of the rapidly mutating human salivary agglutinin gene (DMBT1) and population subsistence strategy. (le.ac.uk)
  • Salivary agglutinin [SAG, encoded by the deleted in malignant brain tumors 1 (DMBT1) gene] is an innate immune receptor glycoprotein that binds a variety of bacteria and viruses, and mediates attachment of S. mutans to hydroxyapatite on the surface of the tooth. (le.ac.uk)
  • Bikker, F.J.. / Salivary Agglutinin : Structure and function . (vu.nl)
  • Several serological tests including alpha-fetoprotein (AFP), the ratio of lens culinaris agglutinin-reactive alpha-fetoprotein to total AFP (AFP-L3/AFP), des-gamma carboxyprothrombin (DCP), and glypican-3 (GPC-3) have been widely investigated as diagnostic biomarkers for early-stage HCC in at-risk populations. (biomedcentral.com)
  • The selected sdAb were evaluated for their ability to bind to commercial abrin as well as abrax (a recombinant abrin A-chain), purified abrin fractions, Abrus agglutinin (a protein related to abrin but with lower toxicity), ricin, and unrelated proteins. (mdpi.com)
  • 3D Structure of human the para influenza virus (HPIV) type-3 haem agglutinin neuraminidase protein (A) 1V2I, (B) 1V3E, (C) 1V3B, (D) 1V3D, (E) 4MZA). (nih.gov)
  • Results of colorimetric assays of active column fractions indicated that the agglutinin is a glycoprotein composed of protein, hexose and uronic acid. (oregonstate.edu)
  • Agglutinin is active against only live bacteria and requires the divalent cation Mg⁺⁺. In the purest agglutinin preparations obtained less than one ug each of protein, hexose, and uronic acid was required to agglutinate 10⁸ cells of P. putida. (oregonstate.edu)
  • It was demonstrated that gp-340 and agglutinin bound in a similar way to Streptococcus mutans and surfactant protein-D. Histochemically, the distribution of gp-340 in the submandibular salivary glands was identical with the agglutinin distribution, as shown in a previous paper [Takano, Bogert, Malamud, Lally and Hand (1991) Anat. (biochemj.org)
  • We conclude that agglutinin is identical with gp-340, and that this molecule interacts with S. mutans and surfactant protein-D. (biochemj.org)
  • When an agglutinin is added to a uniform suspension of particles such as bacteria or blood, agglutinin binds to the agglutinin-specific structure on the particle causing the particles to aggregate and fall to the bottom leaving a clear suspension. (wikipedia.org)
  • Agglutination, using blood agglutinins known as hemagglutinins, is used diagnostically to identify blood types of human beings based on the reaction between the erythrocyte (Red blood cell) antigens and agglutinins . (wikipedia.org)
  • The potential of the agglutinin in identifying NeuGc containing human tumor associated antigens is discussed. (springer.com)
  • We sought to determine whether a negative DAT using anti-human complement (anti-C3) rules out elevated cold agglutinin (CA) titers and the diagnosis of CAD. (ovid.com)
  • In this report we describe a rare complication caused by the very high concentration in the recipient of cold agglutinins and the activation of the complement system, responsible for red blood cell lysis and consequent fatal cardiovascular shock. (biomedcentral.com)
  • Febrile Agglutinin serologic studies are used to diagnose infectious diseases such as salmonellosis, rickettsial diseases, brucellosis, and tularemia. (wbccount.org)
  • The agglutinin-like sequence (ALS) family of Candida albicans includes eight genes that encode large cell-surface glycoproteins. (nih.gov)
  • [ 21 ] It is found on cold agglutinin-producing malignant lymphoid cells in the bone marrow in persons with lymphoproliferative disorders, on a small proportion of normal lymphoid cells, and in the spleen of a 15-week-old fetus. (medscape.com)