Characterization of the bile acid sensitive methotrexate carrier of rat liver cells

1999 ◽  
Vol 359 (5) ◽  
pp. 411-419 ◽  
Author(s):  
W. Honscha ◽  
Ernst Petzinger
Hepatology ◽  
2000 ◽  
Vol 31 (6) ◽  
pp. 1296-1304 ◽  
Author(s):  
Walther Honscha ◽  
Kerstin U. Dötsch ◽  
Nadine Thomsen ◽  
Ernst Petzinger

1991 ◽  
Vol 273 (1) ◽  
pp. 153-160 ◽  
Author(s):  
J F Coquil ◽  
B Berthon ◽  
N Chomiki ◽  
L Combettes ◽  
P Jourdon ◽  
...  

The monohydroxy bile acid taurolithocholate permeabilizes the endoplasmic reticulum to Ca2+ in rat liver cells. To assess whether this action on the endoplasmic reticulum was restricted to this tissue, the effects of bile acid were investigated in two cell types quite unrelated to rat hepatocyte, namely human platelets and neuronal NG108-15 cell line. The results showed that taurolithocholate (3-100 microM) had no effect on free cytosolic [Ca2+] in human platelets and NG108-15 cells. whereas it increased it from 180 to 520 nM in rat hepatocytes. In contrast, in cells permeabilized by saponin, taurolithocholate initiated a profound release of the stored Ca2+ from the internal Ca2+ pools in the three cell types. The bile acid released 90% of the Ca2+ pools, with rate constants of about 5 min-1 and half-maximal effects at 15-30 microM. The results also showed that, in contrast with liver cells, which displayed an influx of [14C]taurolithocholate of 2 nmol/min per mg, human platelets and the neuronal cell line appeared to be resistant to [14C]taurolithocholate uptake. The influx measured in these latter cells was about 100-fold lower than in rat liver cells. Taken together, these data suggest that human platelets and NG108-15 cells do not possess the transport system for concentrating monohydroxy bile acids into cells. However, they show that human platelets and neuronal NG108-15 possess, in common with liver cells, the intracellular system responsible for taurolithocholate-mediated Ca2+ release from internal stores.


1981 ◽  
Vol 119 (2) ◽  
pp. 409-414 ◽  
Author(s):  
Henk S. GANKEMA ◽  
Elly LAANEN ◽  
Albert K. GROEN ◽  
Joseph M. TAGER

1980 ◽  
Vol 103 (2) ◽  
pp. 299-305 ◽  
Author(s):  
Kathleen M. BOTHAM ◽  
Geoffrey J. BECKETT ◽  
Iain W. PERCY-ROBB ◽  
George S. BOYD

In Vitro ◽  
1984 ◽  
Vol 20 (4) ◽  
pp. 291-301 ◽  
Author(s):  
Ursula I. Heine ◽  
Mary J. Wilson ◽  
Eliana F. Munoz

1977 ◽  
Vol 164 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Åke Oldberg ◽  
Magnus Höök ◽  
Björn Öbrink ◽  
Håkan Pertoft ◽  
Kristofer Rubin

Rat liver cells grown in primary cultures in the presence of [35S]sulphate synthesize a labelled heparan sulphate-like glycosaminoglycan. The characterization of the polysaccharide as heparan sulphate is based on its resistance to digestion with chondroitinase ABC or hyaluronidase and its susceptibility to HNO2 treatment. The sulphate groups (including sulphamino and ester sulphate groups) are distributed along the polymer in the characteristic block fashion. In 3H-labelled heparan sulphate, isolated after incubation of the cells with [3H]galactose, 40% of the radioactive uronic acid units are l-iduronic acid, the remainder being d-glucuronic acid. The location of heparan sulphate at the rat liver cell surface is demonstrated; part of the labelled polysaccharide can be removed from the cells by mild treatment with trypsin or heparitinase. Further, a purified plasma-membrane fraction isolated from rats previously injected with [35S]sulphate contains radioactively labelled heparan sulphate. A proteoglycan macromolecule composed of heparan sulphate chains attached to a protein core can be solubilized from the membrane fraction by extraction with 6m-guanidinium chloride. The proteoglycan structure is degraded by treatment with papain, Pronase or alkali. The production of heparan [35S]sulphate by rat liver cells incubated in the presence of [35S]sulphate was followed. Initially the amount of labelled polysaccharide increased with increasing incubation time. However, after 10h of incubation a steady state was reached where biosynthetic and degradative processes were in balance.


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