Rat hepatic sinusoidal endothelial cells in monolayer culture

Eyhorn, S.; Schlayer, H.‐J.; Henninger, Hanspeter; Dieter, Peter; Hermann, R; Woort-Menker, M.; Becker, Heiko; Schaefer, Hans E.; Decker, Karl

doi:10.1016/s0168-8278(88)80459-8

Cited by 141 publications

(66 citation statements)

References 27 publications

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“…Rat Kupffer cells were prepared by collagenase-pronase perfusion and separated by a single Nycodenz gradient and centrifugal elution as described previously [3,16]. Cells were cultured in RPMI 1640 medium supplemented with 10% heat-inactivated fetal calf serum (FCS) for 48 h. The experiments were performed during the following 24 h using Krebs-Henseleit hydrogen carbonate buffer (pH 7.4) containing 10 mmol/l glucose.…”

Section: Isolation and Culture Of Kupffer Cellsmentioning

confidence: 99%

Modulation of phagocytosis by anisoosmolarity and betaine in rat liver macrophages (Kupffer cells) and RAW 264.7 mouse macrophages

1996

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Section: Isolation and Culture Of Kupffer Cellsmentioning

confidence: 99%

Modulation of phagocytosis by anisoosmolarity and betaine in rat liver macrophages (Kupffer cells) and RAW 264.7 mouse macrophages

1996

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“…Non-parenchymal cells were prepared by a combined collagenase/ pronase perfusion [21,22]. Kupffer cells were then purified by Nycodenz density-gradient centrifugation and subsequent centrifugal elutriation using a Beckman JE-6 elutriation rotor in a J-21 Beckman centrifuge.…”

Section: Kupffer Cell Preparationmentioning

confidence: 99%

Stimulation of glycogen phosphorylase in rat hepatocytes via prostanoid release from Kupffer cells by recombinant rat anaphylatoxin C5a but not by native human C5a in hepatocyte/Kupffer cell co‐cultures

Hespeling¹,

Püschel²,

Jungermann³

et al. 1995

FEBS Letters

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Stimulation of glycogen phosphorylase in rat hepatocytes via prostanoid release from Kupffer cells by recombinant rat anaphylatoxin C5a but not by native human C5a in hepatocyte/Kupffer cell co-cultures first published in: FEBS Letters 372 (1995), 1, p. 108-112, DOI 10.1016 . Surprisingly, human C5a, which in most systems elicits much stronger effects than C3a, did not increase glycogenolysis in perfused rat liver [3]. It was assumed that the lack of an effect of human C5a in perfused rat liver was due to a species incompatibility [3].The aim of the current study was to corroborate the apparent species specificity of anaphylatoxin. C5a and, moreover, to demonstrate the C5a-elicited intercellular communication via prostanoids in Kupffer cell/hepatocyte co-cultures. It was found that recombinant rat C5a but not native human C5a increased prostanoid formation in cultured rat Kupffer cells and stimulated glycogen phosphorylase activity in rat Kupffer cell/hepatocyte co-cultures via an aspirin-inhibitable mechanism.

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“…Kupffer cells were prepared as described previously (12,13) by means of combined pronase/collagenase perfusion. They were purified with Nycodenz density-gradient centrifugation and subsequent centrifugal elutriation.…”

Section: Methodsmentioning

confidence: 99%

Increase in prostanoid formation in rat liver macrophages (Kupffer cells) by human anaphylatoxin C3a

Püschel

1993

Hepatology

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Human anaphylatoxin C3a increases glycogenolysis in perfused rat liver. This action is inhibited by prostanoid synthesis inhibitors and prostanoid antagonists. Because prostanoids but not anaphylatoxin C3a can increase glycogenolysis in hepatocytes, it has been proposed that prostanoid formation in nonparenchymal cells represents an important step in the C3a-dependent increase in hepatic glycogenolysis. This study shows that (a) human anaphylatoxin C3a (0.1 to 10 pg/ml) dose-dependently increased prostaglandin D,, thromboxane B, and prostaglandin F,, formation in rat liver macrophages (Kupffer cells); (b) the C3a-mediated increase in prostanoid formation was maximal after 2 min and showed tachyphylaxis; and (c) the C3a-elicited prostanoid formation could be inhibited specifically by preincubation of C3a with carboxypeptidase B to remove the essential C-terminal arginine or by preincubation of C3a with Fab fragments of a neutralizing monoclonal antibody. These data support the hypothesis that the C3a-dependent activation of hepatic glycogenolysis is mediated by way of a C3a-induced prostanoid production in Kupffer cells. (HEPATOLOGY 1993; 18: 1516-1521.)The human anaphylatoxin C3a is generated by the proteolytic cleavage of the third complement component C3. C3a is under the control of serum carboxypeptidase N, which cleaves the C-terminal Arg-77 and thereby inactivates C3a. The classic anaphylatoxic effects of C3a such as smooth muscle contraction and enhanced vascular permeability are only in part due to direct activation of the effector cells by C3a receptors. Other proinflammatory mediators such as histamine and prostanoids may be involved in the signal chains. Thus the C3a-mediated contraction of guinea pig lung parenchymal strips were inhibited by indomethacin (11, and

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Rat hepatic sinusoidal endothelial cells in monolayer culture

Cited by 141 publications

References 27 publications

Modulation of phagocytosis by anisoosmolarity and betaine in rat liver macrophages (Kupffer cells) and RAW 264.7 mouse macrophages

Modulation of phagocytosis by anisoosmolarity and betaine in rat liver macrophages (Kupffer cells) and RAW 264.7 mouse macrophages

Stimulation of glycogen phosphorylase in rat hepatocytes via prostanoid release from Kupffer cells by recombinant rat anaphylatoxin C5a but not by native human C5a in hepatocyte/Kupffer cell co‐cultures

Increase in prostanoid formation in rat liver macrophages (Kupffer cells) by human anaphylatoxin C3a

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