Cell surface laminin-like substances and laminin-related carbohydrates of rat ascites hepatoma AH7974 and its variants with different lung-colonizing potential

1994 ◽  
Vol 12 (3) ◽  
pp. 203-212 ◽  
Author(s):  
Takanori Kawaguchi ◽  
Tomohisa Ono ◽  
Hironao Wakabayashi ◽  
Seiji Igarashi
Keyword(s):  
Cell Surface ◽  
Ascites Hepatoma ◽  
Rat Ascites Hepatoma

Cell surface heparan sulphate and adhesive property of sublines of rat ascites hepatoma AH7974

1988 ◽  
Vol 90 (4) ◽  
pp. 683-689 ◽  
Author(s):  
A. Kimura ◽  
T. Kawaguchi ◽  
T. Ono ◽  
A. Sakuma ◽  
Y. Yokoya ◽  
...  
Keyword(s):  
Cell Surface ◽  
Culture Medium ◽  
Heparan Sulphate ◽  
Soluble Form ◽  
Foetal Calf Serum ◽  
Serum Free Medium ◽  
Free Medium ◽  
Ascites Hepatoma ◽  
Serum Free ◽  
Rat Ascites Hepatoma

Two variants (74AD and 74FL) established from rat ascites hepatoma AH7974 were examined for the production of glycosaminoglycans in culture. There was no difference between the adhesive (74AD) and the floating (74FL) variants in quantity of glycosaminoglycans produced by their cultivation in minimum essential medium supplemented with 10% foetal calf serum. However, they were distinctly different in the distribution patterns of heparan sulphate. In 74FL, about 70% of total heparan sulphate was found in the culture medium in soluble form, whereas in 74AD, only 7% was found in the medium and the rest was in the cell-substratum complex. In a serum-free medium, 74AD cells grew without adhering to the substratum. After cultivation, more than 90% of total heparan sulphate was found in the cell-associated fractions and the rest in the substratum fractions. No heparan sulphate was detected in the culture medium. On the other hand, 74FL cells released heparan sulphate to the serum-free medium as much as to the serum-containing medium. The increase in amount of heparan sulphate in the culture medium of 74FL cells was supposed to be caused by failure of the cells to deposit heparan sulphate at the cell surface and not caused by increased production. Cell-substratum adhesion mechanisms involving cell surface heparan sulphate (heparan sulphate proteoglycan) and some serum intermediate(s) are discussed for 74AD cells.

Roles of calcium in aggregation of rat ascites hepatoma cells by cell surface-associated adhesive factor

1984 ◽  
Vol 66 (1) ◽  
pp. 367-382
Author(s):  
S. Kurano ◽  
M. Ishida ◽  
Y. Ishimaru
Keyword(s):  
Cell Surface ◽  
Single Cells ◽  
Cell Aggregation ◽  
Ascites Hepatoma ◽  
A Cell ◽  
Rat Ascites Hepatoma ◽  
Junctional Complexes ◽  
Adhesive Factor ◽  
Induced Aggregation

Our previous studies have shown that a cell surface-associated adhesive factor (AF), separated from rat ascites hepatoma AH136B cells of a differentiated type and highly purified by chromatography, induces not only aggregation of dissociated AH136B cells or rat ascites hepatoma AH109A cells of an undifferentiated type but also adhesiveness characterized by the development of junctional complexes; the AF-induced aggregation of the cells was Ca2+-dependent. Further analysis of the roles of Ca2+ in cell aggregation was performed using AH109A cells (present as single cells in vivo). (1) AF clearly enhanced 45Ca uptake by the cells; (2) calmodulin was isolated from the cells; (3) calmodulin inhibitor, W-7 (N-(6-amino-hexyl)-5-chloro-1-naphthalenesulphonamide), strongly inhibited aggregation of the cells; (4) W-7 also inhibited the clustering or capping of AF-binding sites on the cell surface; (5) binding of 125I-labelled AF to the cells was independent of Ca2+ concentration; (6) binding of 125I-labelled AF to AF-conjugated beads was not observed, independently of the presence of Ca2+. These findings suggest that Ca2+ and Ca2+-activated calmodulin may play a key role in the process of aggregation of the cells by controlling the microfilament components and that Ca2+ may not be involved either in the interactions between AF and its cellular receptor or in linkages of AF molecules.

An immunoelectron microscopic study on the distribution of a cell surface-associated adhesive glycoprotein synthesized by rat ascites hepatoma cells

1984 ◽  
Vol 71 (1) ◽  
pp. 95-109
Author(s):  
R. Hattori ◽  
Y. Ishimaru ◽  
R. Kurano ◽  
H. Hayashi
Keyword(s):  
Cell Surface ◽  
Contact Region ◽  
Cell Surfaces ◽  
Intercellular Spaces ◽  
Ascites Hepatoma ◽  
A Cell ◽  
Rat Ascites Hepatoma ◽  
Adhesive Factor

As previously described, a cell surface-associated adhesive factor (AF) was separated from differentiated rat ascites hepatoma AH136B cells (forming cell islands in vivo) and highly purified by chromatography. AF synthesis by the cells was investigated by means of ultrastructural immunoperoxidase cytochemistry. Its synthesis and localization in vivo were observed in the perinuclear spaces, the rough endoplasmic reticulum, the Golgi apparatus, the smooth-membranous vesicles, and the contact region of basolateral cell surfaces of the cells in the islands, and also in the intercellular spaces. No AF synthesis was detectable in the nucleus, the free ribosomes, the mitochondria or the apical non-contacting cell surfaces. Similar features of AF synthesis and localization were also induced by dissociated AH136B cells in vitro. Upon adhesion of such recovered cells, AF was also localized at the contact surface of the adjacent cells, but not at the non-contacting free surface.

scholarly journals Inhibition of P-Glycoprotein-Dependent Multidrug Resistance by an Isoquinolinesulfonamide Compound H-87 in Rat Ascites Hepatoma AH66 Cells.

1996 ◽  
Vol 19 (6) ◽  
pp. 886-889 ◽  
Author(s):  
Shigeo NAKAMURA ◽  
Tomoyoshi MINAMINO ◽  
Masaaki NOMURA ◽  
Shinya WAKUSAWA ◽  
Ken-ichi MIYAMOTO ◽  
...  
Keyword(s):  
Multidrug Resistance ◽  
Ascites Hepatoma ◽  
P Glycoprotein ◽  
Rat Ascites Hepatoma

A high-affinity (Ca2+ + Mg2+)-ATPase in plasma membranes of rat ascites hepatoma AH109A cells

1983 ◽  
Vol 731 (2) ◽  
pp. 229-238 ◽  
Author(s):  
Takafumi Iwasa ◽  
Yasushi Iwasa ◽  
Rajabather Krishnaraj
Keyword(s):  
Plasma Membranes ◽  
Ascites Hepatoma ◽  
High Affinity ◽  
Rat Ascites Hepatoma
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