276 Side population cells derived from non-parenchymal liver cells and splenocytes are capable of differentiating into hepatocytes in vitro

Hepatology ◽  
2003 ◽  
Vol 38 ◽  
pp. 289-289
Author(s):  
S INOKUCHI ◽  
T AZUMA ◽  
T NISHIMURA ◽  
K TOMITA ◽  
N KITAMURA ◽  
...  
Keyword(s):  
Side Population ◽  
Liver Cells ◽  
Side Population Cells ◽  
Parenchymal Liver

scholarly journals Combination of quantification and observation methods for study of “Side Population” cells in their “in vitro” microenvironment

2007 ◽  
Vol 71A (4) ◽  
pp. 251-257 ◽  
Author(s):  
Rachid Benchaouir ◽  
Julien Picot ◽  
Nicolas Greppo ◽  
Philippe Rameau ◽  
Daniel Stockholm ◽  
...  
Keyword(s):  
Side Population ◽  
Side Population Cells ◽  
Observation Methods

scholarly journals Carrier-Mediated Delivery of 9-(2-Phosphonylmethoxyethyl)Adenine to Parenchymal Liver Cells: a Novel Therapeutic Approach for Hepatitis B

2000 ◽  
Vol 44 (3) ◽  
pp. 477-483 ◽  
Author(s):  
Remco L. A. de Vrueh ◽  
Erik T. Rump ◽  
Erika van de Bilt ◽  
Richard van Veghel ◽  
Jan Balzarini ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Lithocholic Acid ◽  
Hepatic Uptake ◽  
Liver Cells ◽  
Asialoglycoprotein Receptor ◽  
Parenchymal Liver ◽  
Lipophilic Prodrug ◽  
Acid Labile

ABSTRACT Our aim is to selectively deliver 9-(2-phosphonylmethoxyethyl)adenine (PMEA) to parenchymal liver cells, the primary site of hepatitis B virus (HBV) infection. Selective delivery is necessary because PMEA, which is effective against HBV in vitro, is hardly taken up by the liver in vivo. Lactosylated reconstituted high-density lipoprotein (LacNeoHDL), a lipid particle that is specifically internalized by parenchymal liver cells via the asialoglycoprotein receptor, was used as the carrier. PMEA could be incorporated into the lipid moiety of LacNeoHDL by attaching, via an acid-labile bond, lithocholic acid-3α-oleate to the drug. The uptake of the lipophilic prodrug (PMEA-LO) by the liver was substantially increased after incorporation into LacNeoHDL. Thirty minutes after injection of [3H]PMEA-LO-loaded LacNeoHDL into rats, the liver contained 68.9% ± 7.7% of the dose (free [3H]PMEA, <5%). Concomitantly, the uptake by the kidney was reduced to <2% of the dose (free [3H]PMEA, >45%). The hepatic uptake of PMEA-LO-loaded LacNeoHDL occurred mainly by parenchymal cells (88.5% ± 8.2% of the hepatic uptake). Moreover, asialofetuin inhibited the liver association by >75%, indicating uptake via the asialoglycoprotein receptor. The acid-labile linkage in PMEA-LO, designed to release PMEA during lysosomal processing of the prodrug-loaded carrier, was stable at physiological pH but was hydrolyzed at lysosomal pH (half-life, 60 to 70 min). Finally, subcellular fractionation indicates that the released PMEA is translocated to the cytosol, where it is converted into its active diphosphorylated metabolite. In conclusion, lipophilic modification and incorporation of PMEA into LacNeoHDL improves the biological fate of the drug and may lead to an enhanced therapeutic efficacy against chronic hepatitis B.

scholarly journals Uptake and degradation of filamentous actin and vitamin D-binding protein in the rat

1991 ◽  
Vol 274 (1) ◽  
pp. 237-241 ◽  
Author(s):  
S Dueland ◽  
M S Nenseter ◽  
C A Drevon
Keyword(s):  
Vitamin D ◽  
Binding Protein ◽  
Total Radioactivity ◽  
Liver Cells ◽  
Tissue Uptake ◽  
Rapid Rate ◽  
Vitamin D Binding Protein ◽  
Filamentous Actin ◽  
Parenchymal Liver

Tissue uptake and degradation of 125I-tyramine-cellobiose-labelled filamentous actin, vitamin D-binding protein (DBP) and actin-DBP complex were studied in the rat. Actin and actin-DBP complex were cleared from plasma at a faster rate than was DBP. About 40% of injected actin was recovered in the liver between 10 and 30 min after administration. Of the total radioactivity recovered in the liver, about 35% and 40% was detected in parenchymal and endothelial cells respectively when labelled actin or DBP-actin complex was injected intravenously. When labelled DBP alone was injected, approx. 55% of the radioactivity recovered in liver was in the Kupffer cells. These results suggest that actin is targeting the DBP-actin complex to the endothelial and parenchymal liver cells. Filamentous actin was also taken up in large amounts and at a rapid rate in parenchymal as well as non-parenchymal liver cells in vitro. Our data indicate that the rat has a mechanism to clear actin and the DBP-actin complex from plasma and that both parenchymal and non-parenchymal liver cells are involved in this process.

scholarly journals Side Population Cells Derived from Adult Human Liver Generate Hepatocyte-like Cells In Vitro

2005 ◽  
Vol 50 (10) ◽  
pp. 1755-1763 ◽  
Author(s):  
Sunny Zaheed Hussain ◽  
Stephen C. Strom ◽  
Martha R. Kirby ◽  
Sean Burns ◽  
Saskia Langemeijer ◽  
...  
Keyword(s):  
Human Liver ◽  
Side Population ◽  
Side Population Cells ◽  
Adult Human

In vitro maintenance of liver function in hierarchical co-culture of hepatocytes and non-parenchymal liver cells

1995 ◽  
Vol 80 (6) ◽  
pp. 575-579 ◽  
Author(s):  
Kiyohito Yagi ◽  
Nobuaki Sumiyoshi ◽  
Chikaomi Yamada ◽  
Nobuyasu Michibayashi ◽  
Yumiko Nakashima ◽  
...  
Keyword(s):  
Liver Function ◽  
Liver Cells ◽  
Parenchymal Liver ◽  
In Vitro Maintenance ◽  
Culture Of Hepatocytes

scholarly journals Proliferation, differentiation and migration of SCA1−/CD31− cardiac side population cells in vitro and in vivo

2017 ◽  
Vol 227 ◽  
pp. 378-386 ◽  
Author(s):  
Xue-zhe Wang ◽  
Rui-lan Gao ◽  
Ping Sun ◽  
Shengyi Liu ◽  
Yang Xu ◽  
...  
Keyword(s):  
Side Population ◽  
Side Population Cells ◽  
And Migration

Cofilin is a marker of myofibroblast differentiation in cells from porcine aortic cardiac valves

2008 ◽  
Vol 294 (4) ◽  
pp. H1767-H1778 ◽  
Author(s):  
M. Pho ◽  
W. Lee ◽  
D. R. Watt ◽  
C. Laschinger ◽  
C. A. Simmons ◽  
...  
Keyword(s):  
Stem Cells ◽  
Side Population ◽  
Smooth Muscle Actin ◽  
Tensile Force ◽  
Type I ◽  
Myofibroblast Differentiation ◽  
Side Population Cells ◽  
Isolated Cells ◽  
Color Flow

The formation of myofibroblasts in valve interstitial cell (VIC) populations contributes to fibrotic valvular disease. We examined myofibroblast differentiation in VICs from porcine aortic valves. In normal valves, cells immunostained for α-smooth muscle actin (α-SMA, a myofibroblast marker) were rare (0.69 ± 0.48%), but in sclerotic valves of animals fed an atherogenic diet, myofibroblasts were spatially clustered and abundant (31.2 ± 6.3%). In cultured VIC populations from normal valves, SMA-positive myofibroblasts were also spatially clustered, abundant (21% positive cells after 1 passage), and stained for collagen type I and vimentin but not desmin. For an analysis of stem cells, two-color flow cytometry of isolated cells stained with Hoechst 33342 demonstrated that 0.5% of VICs were side population cells; none stained for SMA. Upon culture, sorted side population cells generated ∼85% SMA-positive cells, indicating that some myofibroblasts originate from a rare population with stem cell characteristics. Plating cells on rigid collagen substrates enabled the formation of myofibroblasts after 5 days in culture, which was completely blocked by culture of cells on compliant collagen substrates. Exogenous tensile force also significantly increased SMA expression in VICs. Isotope-coded affinity tags and mass spectrometry were used to identify differentially expressed proteins in myofibroblast differentiation of VICs. Of the nine proteins that were identified, cofilin expression and phospho-cofilin were strongly increased by conditions favoring myofibroblast differentiation. Knockdown of cofilin with small-interfering RNA inhibited collagen gel contraction and reduced myofibroblast differentiation as assessed by the SMA incorporation into stress fibers. When compared with normal valves, diseased valves showed strong immunostaining for cofilin that colocalized with SMA in clustered cells. We conclude that in VICs, cofilin is a marker for myofibroblasts in vivo and in vitro that arise from a rare population of stem cells and require a rigid matrix for formation.

scholarly journals Interaction of mutants of tissue-type plasminogen activator with liver cells: effect of domain deletions

1996 ◽  
Vol 313 (3) ◽  
pp. 775-780 ◽  
Author(s):  
Johan KUIPER ◽  
Anita VAN'T HOF ◽  
Marlies OTTER ◽  
Erik A. L. BIESSEN ◽  
Dingeman C. RIJKEN ◽  
...  
Keyword(s):  
Plasminogen Activator ◽  
Plasma Clearance ◽  
Specific Binding ◽  
Liver Cells ◽  
Tissue Type ◽  
Tissue Type Plasminogen Activator ◽  
Type Plasminogen Activator ◽  
Parenchymal Liver

The fibrin-specific thrombolyticum tissue-type plasminogen activator (t-PA) has proven to be a potent drug in several clinical trials, but its clinical application is complicated by the rapid clearance of t-PA from the circulation. The rapid plasma clearance of t-PA results from the uptake of t-PA in the liver. t-PA consists of several domains which may be involved in the interaction with the liver. Three domain-deletion mutants, which were produced by the use of a cassette gene system, were studied in vivo and in vitro for their capacity to bind to the various types of rat liver cells. The three mutants lacked, in comparison to control t-PA, the epidermal growth factor (G) domain, the finger (F) domain or the G domain plus the first kringle (K1). The plasma clearance of the three mutants was slower than that of control t-PA. The slower plasma clearance resulted from a decreased liver uptake: 50 and 80% for t-PA mutants and control t-PA respectively. It was found that the K1 domain was of major importance for the uptake of t-PA by liver endothelial cells in vivo and in vitro. The high-affinity binding of t-PA (and t-PA mutants) to parenchymal liver cells depended largely on the presence of the G domain. Other domain(s), like the F, K2 or protease domain, may be responsible for low-affinity, t-PA-specific binding to rat parenchymal liver cells.

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