Biological activities of a novel lectin derived from silkworm faeces: Characteristic changes of mouse peritoneal macrophages by the lectin

Cell Structure and Function

Volumn 23, Issue 5, 1998, Pages 303-313

  Hirayama, Etsuko ^a   Maekawa, Hisayuki ^a   Hiraki, Akihiro ^a   Kim, Jeman ^a  

^a KYOTO PHARMACEUTICAL UNIVERSITY   (Japan)

Author keywords

Lectin; Macrophages; Podosomes; Projections; Silkworm faeces

Indexed keywords

LECTIN; VINCULIN;

ANIMAL CELL; ARTICLE; CELL ADHESION; CELL GROWTH; CELL SHAPE; FECES; MOUSE; NONHUMAN; PERITONEUM MACROPHAGE; PHAGOCYTOSIS; PHASE CONTRAST MICROSCOPY; PRIORITY JOURNAL; SILKWORM;

ANIMALIA; BOMBYX MORI;

EID: 0032416323     PISSN: 03867196     EISSN: None     Source Type: Journal    
DOI: 10.1247/csf.23.303     Document Type: Article

References (30)

1. AGGELER, J. and WERB, Z. 1982. Initial events during phagocytosis by macrophages viewed from outside and inside the cell: membrane-particle interactions and clathrin. J. Cell Biol., 94: 613-623.
2. AMATO, P.A., UNANUE, E.R., and TAYLOR, D.L. 1983. Distribution of actin in spreading macrophages: a comparative study on living and fixed cells. J. Cell Biol., 96: 750-761.
3. BOYLES, J. and BAINTON, D.F. 1979. Changing pattern of plasma membrane-associated filaments during the initial phases of polymorphonuclear leukocyte adherence. J. Cell Biol., 82: 347-368.
4. ECKHARDT, A.E., MALONE, B.N., and GOLDSTELN, I.J. 1982. Inhibition of Ehrlich ascites tumor cell growth by Grifolonia simplicifolia I lectin in vivo. Cancer Res., 42: 2977-2979.
5. GANGULY, C. and DAS, S. 1994. Plant lectins as inhibitors of tumor growth and modulators of host immune response. Chemotherapy, 40: 272-278.
6. GOLDMAN, R., SHARON, N., and LOTAN, R. 1976. A differential response elicited in macrophages on interaction with lectins. Exp. Cell Res., 99: 408-422.
7. GOLDSTEIN, I.J. and HAYES, C.E. 1979. The lectins: carbohydrate binding protein of plants and animals. Adv. Carbohydrate Chem. Biochem., 35: 127-340.
8. HIRAYAMA, E., ISHIKAWA, N., YANO-INOUE, T., and KIM, J. 1993. Purification and characterization of a lectin-like substance from silkworm faeces. Cell Struct. Funct., 18: 161-171.
9. HIRAYAMA, E., ISHIKAWA, N., and KIM, J. 1994. Further characterization of a novel lectin derived from silkworm faeces; specific binding to immunoglobulins, and activation of immunocytes. Cell Biol. Inter., 18: 257-269.
10. KILPATRICK, D.C. 1995. Lectins in immunology. In Lectins, Biomedical Perspectives (Pusztai, A. and Bardocz, S., eds.). Taylor and Francis Ltd., London, pp.155-182.
11. KIM, J., SAIUCHI, M., and ADACHI, T. 1995. Morphological characters and disturbance of myofibril assembly in avian myoblasts fused with HVJ (Sendai virus). Eur. J. Cell Biol., 66: 94-105.
12. KIM, J., ADACHI, T., HIRAYAMA, E., YABUBAYASHI, T., and OKADA, Y. 1992. Differentiation of quail myoblasts transformed with a temperature sensitive mutant of Rous sarcoma virus. I. Relationship between differentiation and tyrosine kinase of src gene product. Cell Struct. Funct., 17: 237-247.
13. KURISU, M., YAMAZAKI, M., and MIZUNO, O. 1980. Induction of macrophage-mediated tumor lysis by the lectin wheat germ agglutinin. Cancer Res., 40: 3798-3803.
14. LAEMMLI, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227: 680-685.
15. LEHTO, V.P., HOVI, T., VARTIO, R., BADLEY, R.A., and VIRTANEN, I. 1982. Reorganization of cytoskeletal and contractile elements during transition of human monocytes into adherent macrophages. Lab. Invest., 47: 391-399.
16. LIS, H. and SHARON, N. 1986. Lectins as molecules and as tools. Annu. Rev. Biochem., 55: 35-37.
17. LOWRY, O.H., ROSEBROUGH, N.J., FARR, A.L., and RANDALL, R.J. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193: 265-275.
18. MALDONADO, G., PARRAS, F., FERNÁNDES, L., and ZENTENO, E. 1994. Effect of lectins on mouse peritoneal macrophage phagocytic activity. Immu. Inv., 23: 429-436.
19. MARCHISIO, P.C., CIRILLO, D., TETI, A., ZAMBONIN-ZALLONE, A., and TARONE, G. 1987. Rous sarcoma virus-transformed fibroblasts and cells of monocytic origin display a peculiar dotlike organization of cytoskeletal proteins involved in microfilament-membrane interactions. Exp. Cell Res., 169: 202-214.
20. NATHAN, C. and COHN, Z. 1980. Role of oxygen dependent mechanisms in antibody induced lysis of tumor cells by activated macrophages. J. Exp. Med., 152: 198-208.
21. ONO, M., MURAKAMI, T., TOMITA, M., and ISHIKAWA, H. 1993. Association of the actin cytoskeleton with glass-adherent proteins in mouse peritoneal macrophages. Biol. Cell, 77: 219-230.
22. REAVEN, E.P. and AXLINE, S.G. 1973. Subplasmalemmal microfilaments and microtubules in resting and phagocytizing cultivated macrophages. J. Cell Biol., 59: 12-27.
23. SAITO, H. and TOMOI, K.H. 1979. Enhanced hydrogen peroxidase release from macrophages stimulated with streptococcal preparation OK432. Infect. Immun., 26: 779-782.
24. SHARON, N. and LIS, H. 1972. Lectins: cell-agglutinating and sugar-specific proteins. Science, 177: 949-959.
25. SHOHAM, M., INBAR, M., and SACHS, L. 1970. Differential toxicity on normal and transformed cells in vitro and inhibition of tumor development in vivo by concanavalin A. Nature, 227: 1244-1246.
26. TARONE, G., CIRILLO, D., GIANCOTTI, F.G., COMOGLIO, P.M., and MARCHISIO, P.C. 1985. Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res., 159: 141-157.
27. TOMITA, M. and ISHIKAWA, H. 1992. Identification of novel adhesion proteins in mouse peritoneal macrophages. Biol. Cell, 76: 103-109.
28. TROTTER, J.A. 1980. The organization of actin in spreading macrophages. The actin-cytoskeleton of peritoneal macrophages is linked to the substratum via transmembrane connections. Exp. Cell Res., 132: 235-248.
29. WILLIAMS, A.F. and BARCLAY, A.N. 1988. The immunoglobulin superfamily-domains for cell suface recognition. Annu. Rev. Immunol., 6: 381-405.
30. 3 integrin is colocalized with vinculin and talin in the podosomes of osteoclastoma giant cells. Exp. Cell Res., 182: 645-652.