scholarly journals The development of the sinusoids of fetal rat liver: localization of endogenous peroxidase in fetal Kupffer cells.

1979 ◽  
Vol 27 (2) ◽  
pp. 643-652 ◽  
Author(s):  
R M Pino ◽  
P W Bankston

Endogenous peroxidase is the cytochemical marker used to identify Kupffer cells in the adult liver. In this study, we show by ultrastructural cytochemistry that Kupffer cells of the fetal rat liver are endogenous peroxidase positive. The reaction product is localized in the endoplasmic reticulum including the perinuclear cisternae and in a few lysosome-like dense bodies. Serial sections of Golgi regions suggest that GERL and not the Golgi stacks, is peroxidase positive. As in the adult liver, peroxidase is not localized in endothelial cells. Kupffer cells do not appear to transform from endothelial or extravascular developing monocytic cells and are present prior to bone marrow formation. The relevance of these observations with respect to the possible origin of the Kupffer cell is discussed.

Author(s):  
Richard M. Pino

This study confirms the presence of endogenous peroxidase in fetal Kupffer cells. In adult hepatic sinusoids Kupffer cells are peroxidase positive; endothelial cells are not.1 The fetal rat liver sinusoidal endothelium during development changes from a lining similar to that found in adult bone marrow to an adult liver type.2 Cells that resemble adult Kupffer cells are evident at 13 days gestation and can endocytize carbon beginning at 14 days.Sixteen day Wistar rat fetuses were exposed in utero after ether anesthesia of their mothers. Colloidal carbon (Pelikan, Gunther Wagner) diluted 1:1 with double strength Tyrode1s solution, or as a control, single strength Tyrode's solution without carbon, was injected (0.01-0,03ml) into the fetal umbilical veins with a 30 gauge needle.2 After allowing one minute for the injected material to circulate, the fetuses were decapitated and the livers were removed and diced into small pieces.


1996 ◽  
Vol 270 (2) ◽  
pp. E244-E250 ◽  
Author(s):  
M. Casado ◽  
L. Bosca ◽  
P. Martin-Sanz

Fetal rat liver expresses a 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/Fru-2,6-Pase2) form that differs from the adult liver enzyme in the inhibition by phosphorylation by the adenosine 3',5'-cyclic monophosphate-dependent protein kinase and in the recognition by an antibody specific for the NH2-terminal domain of the adult liver enzyme. Northern blot analysis shows that fetal hepatocytes contain a species of mRNA that is 2.2 kb in size and that exhibits the maximal levels after delivery. PFK-2/Fru-2,6-Pase2 mRNA analysis using a sensitive ribonuclease protection assay reveals the presence of nearly similar amounts of adult liver-specific and skeletal muscle-specific mRNA in fetal liver and hepatocytes during the last days of gestation, as well as a 233-bp protected fragment present in fetal liver. These results were confirmed by polymerase chain reaction using specific oligonucleotide pairs. Primer extension of fetal liver cDNA suggests the presence of two initiation sites of transcription. Analysis of the adult liver PFK-2/Fru-2,6-Pase2 protein during the perinatal transition using a specific antibody shows a marked accumulation of this form immediately after birth.


Author(s):  
F. G. Zaki

Fetal and neonatal liver injury induced by agents circulating in maternal plasma, even though well recognized, its morphological manifestations are not yet established. As part of our studies of fetal and neonatal liver injury induced by maternal nutritional disorders, metabolic impairment and toxic agents, the effects of two anti-inflammatory steroids have been recently inves tigated.Triamcinolone and methyl prednisolone were injected each in a group of rats during pregnancy at a-dosage level of 2 mgm three times a week. Fetal liver was studied at 18 days of gestation. Litter size and weight markedly decreased than those of control rats. Stillbirths and resorption were of higher incidence in the triamcinolone group than in those given the prednisolone.


Sign in / Sign up

Export Citation Format

Share Document