Regulation of choline kinase activity and phosphatidylcholine biosynthesis by mitogenic growth factors in 3T3 fibroblasts.
نویسندگان
چکیده
The regulation of choline kinase activity by fetal bovine serum and the regulation of phosphatidylcholine biosynthesis by choline kinase have been investigated in 3T3 fibroblasts. Treatment of quiescent 3T3 fibroblasts with serum was shown in previous work to increase phosphocholine pool size and phosphatidylcholine biosynthesis. We now report that treatment of 3T3 cells with serum increased intracellular choline kinase activity by 2-3-fold with a concomitant 2-3-fold decrease of intracellular free choline concentrations. Initial rates of choline transport were the same in quiescent and serum-treated cells, whereas choline kinase activity was 2-3-fold higher in serum-treated cells. As a consequence, free choline concentrations were 2-3-fold lower in serum-stimulated cells than in control quiescent cells. Phosphocholine turnover rates were increased 2-fold by serum treatment both as a consequence of a serum-dependent increase of phosphocholine pools and as a result of a serum-dependent lowering of the phosphocholine half-life. Thus, the overall response of 3T3 cells to serum stimulation included decreased choline pools and increased choline kinase activity, phosphocholine pool size, phosphocholine turnover, and phosphatidylcholine biosynthesis.
منابع مشابه
Phorbol ester stimulates choline uptake in Swiss 3T3 fibroblasts following introduction of the gene encoding protein kinase C alpha.
Phorbol 12-myristate 13-acetate (PMA) stimulated radiolabelled choline uptake and incorporation into phosphatidylcholine (PtdCho) in a time- and concentration-dependent manner in wild-type NIH 3T3 fibroblasts. The accumulation of labelled choline induced by PMA was paralled by an increase in choline mass. The results implicate protein kinase C (PKC) in the regulation of choline uptake. In order...
متن کاملThe cellular mechanism of glucocorticoid acceleration of fetal lung maturation. Fibroblast-pneumonocyte factor stimulates choline-phosphate cytidylyltransferase activity.
The cellular mechanism by which glucocorticoids stimulate phosphatidylcholine biosynthesis has been studied in the fetal rat lung in vivo and in cultured fetal rat lung cells of varying levels of complexity. Administration of dexamethasone to pregnant rats at 18 days gestation resulted in a significant increase in saturated phosphatidylcholine content in fetal lung 24 h after injection. Dexamet...
متن کاملRegulation of Na+/H+exchanger gene expression: mitogenic stimulation increases NHE1 promoter activity.
We examined factors important in regulation of expression of the Na+/H+exchanger gene in NIH/3T3 cells. A stable fibroblast cell line was generated that contained a 1.1-kb proximal fragment of the mouse NHE1 promoter. The addition of serum to serum-starved cells resulted in an increase in activity of the NHE1 promoter. The mitogenic agonists insulin, thrombin, and epidermal growth factor also i...
متن کاملRegulation of phospholipase D by sphingosine involves both protein kinase C-dependent and -independent mechanisms in NIH 3T3 fibroblasts.
Previously, the protein kinase C (PKC) inhibitor sphingosine was found to stimulate phospholipase D (PLD)-mediated hydrolysis of both phosphatidylethanolamine (PtdEtn) and phosphatidylcholine (PtdCho) in NIH 3T3 fibroblasts [Kiss & Anderson (1990) J. Biol. Chem. 265, 7345-7350]. Here we examined the possible relationship between the opposite effects of sphingosine on PKC-mediated protein phosph...
متن کاملA role for Sp1 in transcriptional regulation of phosphatidylethanolamine N-methyltransferase in liver and 3T3-L1 adipocytes.
Phosphatidylcholine is made in all nucleated mammalian cells via the CDP-choline pathway. Another major pathway for phosphatidylcholine biosynthesis in liver is catalyzed by phosphatidylethanolamine N-methyltransferase (PEMT). We have now identified 3T3-L1 adipocytes as a cell culture model that expresses PEMT endogenously. We have found that PEMT mRNA and protein levels increased dramatically ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 260 10 شماره
صفحات -
تاریخ انتشار 1985