Biomedical subjects

H Komano

Publications and source records attributed to H Komano.

43 records · Page 3Linked to original sources

PubMed1985

Comparison of binding proteins on the surface of murine tumor cells for two lectins active in the lectin-dependent macrophage-mediated cytotoxic reaction.

The binding proteins for Sarcophaga lectin and wheat germ agglutinin on the surface of Ehrlich ascites tumor cells were compared. Studies with antibody against the binding protein for Sarcophaga lectin showed that these two binding proteins are different. Since these two lectins are both active in the lectin-dependent macrophage-mediated cytotoxic reaction with Ehrlich ascites tumor cells as target cells, there must be multiple proteins on the surface of target cells that can trigger cytolytic reaction in response to different lectins in the presence of macrophages.

Animals↗

PubMed1984

Identification of hemagglutinating protein and bactericidal activity in the hemolymph of adult Sarcophaga peregrina on injury of the body wall.

When the body wall of adult Sarcophaga peregrina (flesh-fly) was injured with a hypodermic needle, hemagglutinating activity and antibacterial activity were induced in the hemolymph simultaneously. The hemagglutinating activity was shown to be due to the same lectin that was found previously in the hemolymph of injured larvae. Thus, larval and adult Sarcophaga respond in the same way to injury of the body wall.

Animals↗

PubMed1983

Measurement of Sarcophaga peregrina lectin under various physiological conditions by radioimmunoassay.

Lectin induced in the hemolymph of Sarcophaga peregrina (flesh fly) larvae on injury of the body wall or on pupation was studied further by radioimmunoassay, focusing on the interaction between the lectin and hemocytes. It was found that the amount of lectin on the surface of hemocytes prepared from injured larvae increased with time after injury of the body wall. Radioiodinated lectin could bind to hemocytes prepared from injured larvae more effectively than those from normal larvae, indicating a difference in the affinities to lectin of hemocytes from these two sources. The lectin was found to be synthesized in the fat-body and then secreted into the hemolymph both on injury of the body wall and on pupation. A significant level of lectin was maintained in pupae during the entire pupal stage, but it decreased rapidly before emergence, and no lectin was found in newly emerged flies. Since the lectin greatly activated the activity of mouse bone marrow cells to kill Candida parapsilosis cells, the biological significance of humoral lectin in the defense mechanism was discussed from the ontogenic viewpoint.

Animals↗

PubMed1983

Polymorphonuclear leukocyte-mediated cytolysis induced by animal lectin.

Nine animal lectins, i.e., Sarcophaga peregrina agglutinin, Balanus roseus agglutinin, Aplysia kurodai agglutinin, Balanus balanoides agglutinin, Tetraclita squamosa japonica agglutinin, Misgurnus anguillicaudatus lectin, Asterina pectinifera agglutinin, Helix aspersa agglutinin and Helix pomatia agglutinin, were tested for induction of cytolysis mediated by polymorphonuclear leukocytes. Among them, S. peregrina agglutinin and B. roseus agglutinin lysed murine target cells in co-operation with polymorphonuclear leukocytes (PMNs) from the peritoneal cavity of mice. PMNs can lyse various tumor cells in the presence of S. peregrina agglutinin, although normal spleen cells were also lysed. This lectin-dependent cytolysis by PMNs was inhibited by galactose, a sugar which is specifically recognized by S. peregrina agglutinin. S. peregrina and B. roseus agglutinins were inhibitory to in vivo development of MM46 tumor cells. These results suggest that PMNs can lyse various target cells in the presence of appropriate animal lectins and that some animal lectins participate in tumor rejection.

Acetylgalactosamine↗

PubMed1982

Induction of macrophage-mediated tumor lysis by an animal lectin, Sarcophaga peregrina agglutinin.

Several animal lectins, such as Sarcophaga peregrina agglutinin, Limulus polyhemus agglutinin, Helix pomatia agglutinin and Helix aspersa agglutinin, were tested for induction of tumor lysis mediated by macrophages. Among them, only S. peregrina agglutinin purified from the hemolymph of S. peregrina larvae lysed tumor cells in co-operation with macrophages from the peritoneal cavity of mice. S. peregrina agglutinin alone did not kill target tumor cells. Macrophages in the presence of this lectin could kill other syngeneic tumor cells. This lectin-dependent cytolysis by macrophages was inhibited by galactose, a sugar which is specifically recognized by S. peregrina agglutinin. These findings suggest that the animal lectin S. peregrina agglutinin is a ligand in macrophage-mediated cytolysis, inducing binding of effector macrophages to target cells which in turn triggers off lysis of the target cells.

Agglutinins↗

PubMed1981

A possible mechanism of induction of insect lectin.

Studies were made using antibody against a lectin induced in the hemolymph of Sarcophaga peregrina larvae on injury. The results suggested that the alpha subunit (Mr = 32,000) of the lectin is normally present in the hemolymph. On injury of the body wall, part of the alpha subunit seems to be converted to the beta subunit (Mr = 30,000), probably by partial proteolysis with a protease activated in response to the injury. As a result, an active lectin with the structure alpha 4 beta 2 is formed.

Animals↗

PubMed1980

Purification of lectin induced in the hemolymph of Sarcophaga peregrina larvae on injury.

A lectin was purified from the hemolymph of Sarcophaga peregrina larvae, obtained after injury of their body wall. This lectin agglutinated sheep red blood cells markedly and the hemagglutinating activity was inhibited by galactose and lactose. The active lectin was found to have a molecular weight of 190,000 and to consist of four alpha subunits and two beta subunits, with molecular weights of 32,000 and 30,000, respectively. During the early pupal stage, similar hemagglutinating activity in the hemolymph increased to several times than in larval hemolymph. This activity was completely inhibited by the antibody prepared against the lectin purified from the hemolymph of injured larvae. Thus, the same protein having lectin activity is apparently induced under two different physiological conditions: injury of the body wall of larvae and during pupation. The biological significance of this lectin is discussed.

Animals↗