Homologous liver parenchymal cell-cell adhesion mediated by an endogenous lectin and its receptor

Cellular and Molecular Biology Letters

Volumn 15, Issue 2, 2010, Pages 356-364

  Banerjee, Saswati ^a   Majumder, Gopal Chandra ^a,b  

^a INDIAN INSTITUTE OF CHEMICAL BIOLOGY   (India)

^b JADAVPUR UNIVERSITY   (India)

Author keywords

Autoagglutination; Homologous cell cell adhesion; Lectin; Lectin receptor; Liver; Parenchymal cell

Indexed keywords

CALCIUM CHLORIDE; CALCIUM ION; FETUIN A; FUCOSE; GALACTOSE; GLUCOSE; LECTIN; MANNOSE; SUCROSE; CALCIUM; LECTIN RECEPTOR;

ARTICLE; BINDING AFFINITY; CARBOHYDRATE ANALYSIS; CELL ADHESION; CELL AGGLUTINATION; CELL INTERACTION; CELL ISOLATION; CELL SURFACE; CONCENTRATION RESPONSE; CONTROLLED STUDY; GOAT; IN VITRO STUDY; LIVER PARENCHYMA; NONHUMAN; PROCESS DEVELOPMENT; PROTEIN BLOOD LEVEL; PROTEIN FUNCTION; PROTEIN INTERACTION; ANIMAL; ANTIGEN ANTIBODY REACTION; CYTOLOGY; DRUG EFFECT; LIVER; METABOLISM;

CAPRA; MAMMALIA;

AGGLUTINATION; ANIMALS; CALCIUM; CELL ADHESION; GALACTOSE; GOATS; LECTINS; LIVER; RECEPTORS, MITOGEN;

EID: 77954587643     PISSN: 14258153     EISSN: 16891392     Source Type: Journal    
DOI: 10.2478/s11658-010-0011-7     Document Type: Article

References (26)

1. Marshall, B. T., Long, M., Piper, J. W., Yago, T., McEver, R. P. and Zhu, C. Direct observation of catch bonds involving cell-adhesion molecules. Nature423 (2003) 190-193.
2. Pokutta, S. and Weis, W. I. Structure and mechanism of cadherins and catenins in cell-cell contacts. Annu. Rev. Cell. Dev. Biol. 23 (2007) 237-261.
3. Schmidmaier, R. and Baumann, P. Anti-adhesion evolves to a promising therapeutic concept in oncology. Curr. Med. Chem. 15 (2008) 978-990.
4. Ogita, H. and Takai, Y. Cross-talk among integrin, cadherin, and growth factor receptor: roles of nectin and nectin-like molecule. Int. Rev. Cytol. 265 (2008) 1-54.
5. Hoffman, S., Sorkin, B. C., White, P. C., Brackenbury, R., Mailhammer, R., Rutishauser, U., Cunningham, B. A. and Edelman, G. M. Chemical characterization of a neural cell adhesion molecule purified from embryonic brain membranes. J. Biol. Chem. 257 (1982) 7720-7729.
6. Gennarini, G., Hirn, M., Deagostini-Bazin, H. and Goridis, C. Studies on the transmembrane disposition of the neural cell adhesion molecule N-CAM. A monoclonal antibody recognizing a cytoplasmic domain and evidence for the presence of phosphoserine residues. Eur. J. Biochem. 142 (1984) 65-73.
7. Edelman, G. M. Surface modulation in cell recognition and cell growth. Science192 (1976) 218-226.
8. Crocker, P. R. and Varki, A. Siglecs in the immune system. Immunology103 (2001) 137-145.
9. Weis, W. I. and Drickamer, K. Structural basis of lectin-carbohydrate recognition. Annu. Rev. Biochem. 65 (1996) 441-473.
10. Nakahara, S. and Raz, A. Biological modulation by lectins and their ligands in tumor progression and metastasis. Anticancer Agents Med. Chem. 8 (2008) 22-36.
11. Yuan, K., Kucik, D., Singh, R. K., Listinsky, C. M., Listinsky, J. J. and Siegal, G. P. Alterations in human breast cancer adhesion-motility in response to changes in cell surface glycoproteins displaying alpha-L-fucose moieties. Int. J. Oncol. 32 (2008) 797-807.
12. Imai, Y., Lasky, L. A. and Rosen, S. D. Sulphation requirement for GlyCAM-1, an endothelial ligand for L-selectin. Nature361 (1993) 555-557.
13. Mannori G., Santoro, D., Carter, L., Corless, C., Nelson, R. N. and Bevilacqua, M. P. Inhibition of colon carcinoma cell lung colony formation by a soluble form of selectin. Am. J. Pathol. 151 (1997) 233-243.
14. Kobayashi, K., Matsumoto, S., Morishima, T., Kawabe, T. and Okamoto, T. Cimetidine inhibits cancer cell adhesion to endothelial cells and prevents metastasis by blocking E-selectin expression. Cancer Res. 60 (2000) 3978-3984.
15. Kolb, H. and Kolb-Bachofen, V. A lectin-like receptor on mammalian macrophages. Biochem. Biophys. Res. Commun. 85 (1978) 678-683.
16. Kolb, H., Schudt, C., Kolb-Bachofen, V. and Kolb, H. A. Cellular recognition by rat liver cells of neuraminidase-treated erythrocytes. Demonstration and analysis of cell contacts. Exp. Cell. Res. 113 (1978) 319-325.
17. Kolb, H., Kriese, A., Kolb-Bachofen, V. and Kolb, H. A. Possible mechanism of entrapment of neuraminidase-treated lymphocytes in the liver. Cell Immunol. 40 (1978) 457-462.
18. Kolb, H., Schlepper-Schafer, J. and Kolb-Bachofen, V. Cell contacts mediated by D- galactose specific lectins on liver cells. Biol. Cell. 36 (1979) 301-308.
19. Schlepper-Schafer, J., Friedrich, E. and Kolb, H. Galactosyl-specific receptor on liver cells: binding sites for tumour cells. Europ. J. Cell. Biol. 25 (1981) 95-102.
20. Spiro, R. G. Studies on fetuin, a glycoprotein of fetal serum. I. Isolation, chemical composition, and physiochemical properties. J. Biol. Chem. 235 (1960) 2860-2869.
21. Seglen, P. O. Preparation of isolated rat liver cells. Methods Cell Biol. 13 (1976) 29-83.
22. Ali, N. and Salahuddin, A. Isolation and some properties of mammalian hepatic membrane lectins. FEBS Lett. 246 (1989) 163-165.
23. Ashwell, G. and Harford, J. Carbohydrate-specific receptors of the liver. Annu. Rev. Biochem. 51 (1982) 531-554.
24. Schwartz, A. L. The hepatic asialoglycoprotein receptor. CRC Crit. Rev. Biochem. 16 (1995) 207-233.
25. Groeber, B. K., Williams, L. G., Pigott, J., Ziska, P. D. S., Franz, H. and Debbage, P. L. Affinities of Ricin 120 and Mistletos lectin 1 for membrane components of liver and nervous tissues. In Lectins: Biology, Biochemistry, Clinical Biochemistry, Vol. III (Bog-Hansen, T. C. and Spengler, G. A. Eds), Walter de Gruyter & Co., Berlin and New York, 1982, 179-187.
26. Banerjee, S., Dungdung, S. R., Das, K. and Majumder, G. C. Synchronous modulation of cell-surface lectin and its receptor in a homologous cell population: a novel mechanism of cellular regulation. Exp. Cell. Res. 312 (2006) 2299-2308.