L-alanine uptake by rat liver parenchymal and haematopoietic cells during the perinatal period.
نویسندگان
چکیده
Alanine disposal by liver parenchymal and haematopoietic cells from 21-day fetuses, newborns and adult rats was studied. Preparations selectively enriched in either haematopoietic cells or hepatocytes were obtained by direct perfusion of fetal- and neonatal-rat livers. L-Alanine transport into liver parenchymal cells was best fitted to two Na(+)-dependent saturable systems. The high-affinity system showed a much higher activity (Vmax.) in hepatocytes from fetuses and newborns than in those from adult rats (2.4, 4.3 and 0.3 nmol/8 min per 10(6) cells for fetuses, newborns and adults respectively). Vmax. for the low-affinity component was slightly lower during the perinatal period than in the adult (about 30 nmol/8 min per 10(6) cells for hepatocytes from fetuses and newborns, versus 48 nmol/8 min per 10(6) cells for adult rat parenchymal cells). Haematopoietic cells from fetal-rat livers showed significant Na(+)-dependent L-alanine uptake which was completely abolished after birth. These results show that the transport systems involved in L-alanine uptake by liver parenchymal cells are fully developed before birth. This probably contributes to fulfilling the high requirement for neutral amino acids for protein synthesis during development. Haematopoietic cells may play an important role in liver amino acid metabolism during fetal life.
منابع مشابه
THE CYTOTOXIC EFFEC T OF CHELIDONIUM ALKALOIDS ON CELLS ISOLATED FROM ADULT RAT LIVER
Alkaloids of the aerial parts of chelidonium were extracted in the salt form, and their aqueous solutions were prepared in different concentrations. Rat hepatocytes were obtained by liver perfusion. The alkaloidal solutions were added to suspensions of hepatocytes in petri dishes and the mixtures were incubated. Two types of controls have been used in one type. no alkaloidal extract was ad...
متن کاملEndocytosis of lysosomal enzymes by non-parenchymal rat liver cells. Comparative study of lysosomal-enzyme uptake by hepatocytes and non-parenchymal liver cells.
Cultured non-parenchymal rat liver cells internalize human urine alpha-N-acetylglucosaminidase, human skin beta-N-acetylglucosaminidase and pig kidney alpha-mannosidase. Different heat-stabilities of endocytosed and endogenous alpha-mannosidase activity provided indirect evidence that the increase in intracellular activity resulted from uptake. The high efficiency and the saturation kinetics of...
متن کاملCytoslic and mitochondrial isoenzymes of branched-chain amino acid aminotransferase during development of the rat
The isoenzymic forms of branched-chain amino acid aminotransferase in mitochondria of rat tissues were compared with the better-known cytosolic forms in order to find any regular pattern of expression of these isoenzymes during development. Mitochondria of all tissues examined except brain contained only a type-I isoenzyme differing from the cytosolic type-I isoenzyme in heat stability and acti...
متن کاملAnticoagulants prevent monocrotaline-induced hepatic parenchymal cell injury but not endothelial cell injury in the rat.
Monocrotaline (MCT) is a pyrrolizidine alkaloid plant toxin that produces hepatotoxicity in humans and animals. Human exposure to MCT occurs through consumption of contaminated grains and herbal medicines. Administration of MCT to rats stimulates activation of the coagulation system and fibrin deposition in the liver. Fibrin deposition occurs simultaneously with endothelial cell damage and prio...
متن کاملMetabolic interactions of parenchymal hepatocytes and dividing epithelial cells in co-culture.
When parenchymal hepatocytes isolated from adult liver are co-cultured with other epithelial cells, the production of various plasma proteins by the hepatocytes is preserved for much longer than in conventional culture. This study examines some of the metabolic interactions between parenchymal hepatocytes and epithelial cells maintained in co-culture. The leakage of lactate dehydrogenase by hep...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- The Biochemical journal
دوره 293 ( Pt 3) شماره
صفحات -
تاریخ انتشار 1993