Receptor distribution and the mechanism of enhanced erythrocyte agglutination by soybean agglutinin. 1976

C A Kuettner, and L A Staehelin, and J A Gordon

We have examined the role of receptor clustering in intact erythrocyte membranes exhibiting enhanced lectin-mediated cell agglutination by analyzing freeze-fracture and freeze-etch images of human erythrocytes labeled with ferritin-conjugated soybean agglutinin. We find that trypsinization and fixation of intact erythrocytes, in either order, causes no alteration of the random distribution of ferritin-conjugated soybean agglutinin on the surfaces of these cells as compared to their distribution on the surfaces of fixed erythrocytes and untreated erythrocyte ghosts. Furthermore, clustering of the intramembranous particles in the membrane of intact erythrocytes was not found with any of the cells described above. We conclude that clustering of the soybean agglutinin receptors is not a major factor involved in the enhanced agglutination of intact trypsinized erythrocytes. Caution is necessary in transferring information obtained with erythrocyte ghosts, where clustering can be induced, to intact erythrocytes.

UI MeSH Term Description Entries
D011485 Protein Binding The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments. Plasma Protein Binding Capacity,Binding, Protein
D011955 Receptors, Drug Proteins that bind specific drugs with high affinity and trigger intracellular changes influencing the behavior of cells. Drug receptors are generally thought to be receptors for some endogenous substance not otherwise specified. Drug Receptors,Drug Receptor,Receptor, Drug
D004903 Erythrocyte Aggregation The formation of clumps of RED BLOOD CELLS under low or non-flow conditions, resulting from the attraction forces between the red blood cells. The cells adhere to each other in rouleaux aggregates. Slight mechanical force, such as occurs in the circulation, is enough to disperse these aggregates. Stronger or weaker than normal aggregation may result from a variety of effects in the ERYTHROCYTE MEMBRANE or in BLOOD PLASMA. The degree of aggregation is affected by ERYTHROCYTE DEFORMABILITY, erythrocyte membrane sialylation, masking of negative surface charge by plasma proteins, etc. BLOOD VISCOSITY and the ERYTHROCYTE SEDIMENTATION RATE are affected by the amount of erythrocyte aggregation and are parameters used to measure the aggregation. Erythrocyte Aggregation, Intravascular,Agglutination, Intravascular,Intravascular Agglutination,Intravascular Erythrocyte Aggregation,Rouleaux Formation, Erythrocyte,Agglutinations, Intravascular,Aggregation, Erythrocyte,Aggregation, Intravascular Erythrocyte,Aggregations, Erythrocyte,Aggregations, Intravascular Erythrocyte,Erythrocyte Aggregations,Erythrocyte Aggregations, Intravascular,Erythrocyte Rouleaux Formation,Erythrocyte Rouleaux Formations,Formation, Erythrocyte Rouleaux,Formations, Erythrocyte Rouleaux,Intravascular Agglutinations,Intravascular Erythrocyte Aggregations,Rouleaux Formations, Erythrocyte
D005293 Ferritins Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types. Basic Isoferritin,Ferritin,Isoferritin,Isoferritin, Basic
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000373 Agglutinins A substance that makes particles (such as bacteria or cells) stick together to form a clump or a mass. Agglutinin
D013025 Glycine max An annual legume. The SEEDS of this plant are edible and used to produce a variety of SOY FOODS. Soy Beans,Soybeans,Bean, Soy,Beans, Soy,Soy Bean,Soybean
D014357 Trypsin A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. Tripcellim,Trypure,beta-Trypsin,beta Trypsin

Related Publications

C A Kuettner, and L A Staehelin, and J A Gordon
March 1975, Experimental cell research,
C A Kuettner, and L A Staehelin, and J A Gordon
January 2001, Molecular membrane biology,
C A Kuettner, and L A Staehelin, and J A Gordon
October 1978, Zhurnal mikrobiologii, epidemiologii i immunobiologii,
C A Kuettner, and L A Staehelin, and J A Gordon
May 1976, Experimental cell research,
C A Kuettner, and L A Staehelin, and J A Gordon
April 1948, Japanese journal of medicine,
C A Kuettner, and L A Staehelin, and J A Gordon
November 1983, Proceedings of the National Academy of Sciences of the United States of America,
C A Kuettner, and L A Staehelin, and J A Gordon
August 1971, Rinsho byori. The Japanese journal of clinical pathology,
C A Kuettner, and L A Staehelin, and J A Gordon
January 1978, Biochimica et biophysica acta,
C A Kuettner, and L A Staehelin, and J A Gordon
January 1984, Methods in enzymology,
C A Kuettner, and L A Staehelin, and J A Gordon
May 1968, Journal of immunology (Baltimore, Md. : 1950),
Copied contents to your clipboard!