Identification and Characterization of Vitamin A-Storing Cells in Fetal Liver: Implications for Functional Importance of Hepatic Stellate Cells in Liver Development and Hematopoiesis

Stem Cells ◽  
2007 ◽  
Vol 25 (9) ◽  
pp. 2339-2349 ◽  
Author(s):  
Hiroshi Kubota ◽  
Hsin-lei Yao ◽  
Lola M. Reid
Keyword(s):  
Vitamin A ◽  
Hepatic Stellate Cells ◽  
Fetal Liver ◽  
Stellate Cells ◽  
Liver Development ◽  
Functional Importance ◽  
Identification And Characterization

scholarly journals Characterization of a stellate cell activation-associated protein (STAP) with peroxidase activity found in rat hepatic stellate cells.

2001 ◽  
Vol 276 (50) ◽  
pp. 47744
Author(s):  
Norifumi Kawada ◽  
Dan Bach Kristensen ◽  
Kinji Asahina ◽  
Kazuki Nakatani ◽  
Yukiko Minamiyama ◽  
...  
Keyword(s):  
Peroxidase Activity ◽  
Hepatic Stellate Cells ◽  
Cell Activation ◽  
Stellate Cell ◽  
Stellate Cells

Characterization and activation of vitamin A-sorted rat hepatic stellate cells

2006 ◽  
Vol 38 ◽  
pp. S6
Author(s):  
T. Mello ◽  
S.P. Sanghani ◽  
W.I. Davis ◽  
C. Surrenti ◽  
A. Casini ◽  
...  
Keyword(s):  
Vitamin A ◽  
Hepatic Stellate Cells ◽  
Stellate Cells

scholarly journals N-glycan chitobiose core biosynthesis by Agl24 strengthens the hypothesis of an archaeal origin of the eukaryal N-glycosylation

2021 ◽  
Author(s):  
Benjamin H. Meyer ◽  
Ben A. Wagstaff ◽  
Panagiotis S. Adam ◽  
Sonja-Verena Albers ◽  
Helge C. Dorfmueller
Keyword(s):  
Posttranslational Modifications ◽  
Biochemical Characterization ◽  
Similar Process ◽  
List Type ◽  
Histidine Residue ◽  
Functional Importance ◽  
Domains Of Life ◽  
Distant Relation ◽  
Identification And Characterization

AbstractProtein N-glycosylation is the most common posttranslational modifications found in all three domains of life. The crenarchaeal N-glycosylation begins with the synthesis of a lipid-linked chitobiose core structure, identical to that in eukaryotes. Here, we report the identification of a thermostable archaeal beta-1,4-N-acetylglucosaminyltransferase, named archaeal glycosylation enzyme 24 (Agl24), responsible for the synthesis of the N-glycan chitobiose core. Biochemical characterization confirmed the function as an inverting β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol glycosyltransferase. Substitution of a conserved histidine residue, found also in the eukaryotic and bacterial homologs, demonstrated its functional importance for Agl24. Furthermore, bioinformatics and structural modeling revealed strong similarities between Agl24 and both the eukaryotic Alg14/13 and a distant relation to the bacterial MurG, which catalyze the identical or a similar process, respectively. Our data, complemented by phylogenetic analysis of Alg13 and Alg14, revealed similar sequences in Asgardarchaeota, further supporting the hypothesis that the Alg13/14 homologs in eukaryotes have been acquired during eukaryogenesis.HighlightsFirst identification and characterization of a thermostable β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphosphodolichol glycosyltransferase (GT family 28) in Archaea.A highly conserved histidine, within a GGH motif in Agl24, Alg14, and MurG, is essential for function of Agl24.Agl24-like homologs are broadly distributed among Archaea.The eukaryotic Alg13 and Alg14 are closely related to the Asgard homologs, suggesting their acquisition during eukaryogenesis.

Vitamin A-coupled liposome system targeting free cholesterol accumulation in hepatic stellate cells offers a beneficial therapeutic strategy for liver fibrosis

2018 ◽  
Vol 48 (5) ◽  
pp. 397-407 ◽  
Author(s):  
Hirotaka Furuhashi ◽  
Kengo Tomita ◽  
Toshiaki Teratani ◽  
Motonori Shimizu ◽  
Makoto Nishikawa ◽  
...  
Keyword(s):  
Liver Fibrosis ◽  
Vitamin A ◽  
Hepatic Stellate Cells ◽  
Free Cholesterol ◽  
Therapeutic Strategy ◽  
Stellate Cells ◽  
Cholesterol Accumulation ◽  
Liposome System

Characterization of ion transport mechanisms regulating intracellular pH in hepatic stellate cells

1997 ◽  
Vol 273 (1) ◽  
pp. G39-G48 ◽  
Author(s):  
A. Di Sario ◽  
G. S. Baroni ◽  
E. Bendia ◽  
L. D'Ambrosio ◽  
F. Ridolfi ◽  
...  
Keyword(s):  
Intracellular Ph ◽  
Hepatic Stellate Cells ◽  
Stellate Cells ◽  
Platelet Derived Growth Factor ◽  
Disulfonic Acid ◽  
Transport Mechanisms ◽  
Independent Manner ◽  
Acid Load ◽  
Acid Loading

The aim of this study was to evaluate intracellular pH (pHi) regulation in nonactivated and activated rat hepatic stellate cells (HSC). The fluorescent pHi indicator 2',7'-bis(carboxyethyl)-5(6)-carboxyfluorescein was used to measure pHi in the presence and absence of HCO3-. In the absence of HCO3-, baseline pHi was significantly higher (P < 0.001) in activated than in nonactivated HSC (7.1 +/- 0.1 vs. 6.9 +/- 0.2) and decreased, in both groups, after amiloride administration and after Na+ removal. After an acid-loading maneuver, pHi recovery was significantly higher (P < 0.03) in activated than in nonactivated HSC (H+ flux = 11.0 +/- 3.8 vs. 7.7 +/- 2.9 mM/min at pHi 6.6) and was inhibited by amiloride and Na+ removal. In the presence of HCO3-, baseline pHi was higher in both groups and decreased after amiloride administration. Amiloride and Na+ removal inhibited pHi recovery after an intracellular acid load by 77 and 93%, respectively, in nonactivated and by 82 and 92%, respectively, in activated HSC, whereas 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid inhibited pHi recovery by only 27%. Acute Cl- removal increased pHi by 0.07 +/- 0.01 pH unit/min in the absence but not in the presence of 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid in nonactivated and activated HSC in an Na(+)-independent manner. In activated HSC, 24 h of incubation with 25 ng/ml platelet-derived growth factor (PDGF)-BB (in 0.5% serum) did not modify baseline pHi (7.07 +/- 0.1 vs. 7.08 +/- 0.1 in HSC cultured in 0.5% serum only) but significantly (P < 0.02) increased, with respect to controls, pHi recovery after an acute acid load. Incubation with PDGF for 24 h induced a fivefold increase in HSC proliferation expressed as percentage of bromodeoxyuridine-positive cells (30.8 +/- 6.7 vs. 6.1 +/- 1.9% in controls). When amiloride (0.1 mM) was present, PDGF-induced HSC proliferation was significantly inhibited (8.1 +/- 0.4%, P < 0.001). Our results show that 1) the Na+/H+ exchanger is the main pHi regulator in rat HSC, 2) activation of HSC is associated with an increase in pHi and in the activity of the Na+/H+ exchanger, 3) PDGF increases the activity of this exchanger, and 4) amiloride is able to inhibit HSC proliferation induced by PDGF.

Characterization of hepatocyte-derived mitogenic activity on hepatic stellate cells

2000 ◽  
Vol 20 (2) ◽  
pp. 157-164 ◽  
Author(s):  
Stanko Skrtic ◽  
Kristina Wallenius ◽  
Axel M. Gressner ◽  
John-Olov Jansson
Keyword(s):  
Hepatic Stellate Cells ◽  
Stellate Cells ◽  
Mitogenic Activity

scholarly journals Characterization of vitamin A-storing cells in mouse fibrous kidneys using Cygb/STAP as a marker of activated stellate cells

2007 ◽  
Vol 70 (2) ◽  
pp. 95-106 ◽  
Author(s):  
Yujiro Kida ◽  
Kinji Asahina ◽  
Kouji Inoue ◽  
Norifumi Kawada ◽  
Katsutoshi Yoshizato ◽  
...  
Keyword(s):  
Vitamin A ◽  
Stellate Cells

scholarly journals Characterization of hepatic stellate cells, portal fibroblasts, and mesothelial cells in normal and fibrotic livers

2016 ◽  
Vol 64 (5) ◽  
pp. 1137-1146 ◽  
Author(s):  
Ingrid Lua ◽  
Yuchang Li ◽  
Jessica A. Zagory ◽  
Kasper S. Wang ◽  
Samuel W. French ◽  
...  
Keyword(s):  
Hepatic Stellate Cells ◽  
Stellate Cells ◽  
Mesothelial Cells ◽  
Portal Fibroblasts
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