scholarly journals Transport of taurine and its regulation by protein kinase C in the JAR human placental choriocarcinoma cell line

1991 ◽  
Vol 277 (1) ◽  
pp. 53-58 ◽  
Author(s):  
P Kulanthaivel ◽  
D R Cool ◽  
S Ramamoorthy ◽  
V B Mahesh ◽  
F H Leibach ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Line ◽  
Transport System ◽  
Taurine Transporter ◽  
Taurine Transport ◽  
Kinase C ◽  
Choriocarcinoma Cells ◽  
Choriocarcinoma Cell Line

The JAR human placental choriocarcinoma cell line transports taurine, concentrating it over 1000-fold inside the cell. The transport system is energized by a Na+ gradient and exhibits an absolute requirement for Cl-. Neutral beta-amino acids such as beta-alanine and hypotaurine effectively compete with the system, whereas neutral alpha-amino acids such as alanine, leucine and alpha-aminoisobutyric acid do not. The transport system interacts with gamma-aminobutyric acid to an appreciable extent. Kinetic analysis reveals that the taurine transport system in this cell line is of a high-affinity and low-capacity type (apparent dissociation constant 2.3 +/- 0.3 microM; maximal velocity 88.5 +/- 5.0 pmol/3 min per mg of protein). Pretreatment of the JAR choriocarcinoma cells with phorbol 12-myristate 13-acetate results in the inhibition of the taurine transport system in a dose-dependent manner. The inhibition is blocked by co-treatment of the cells with staurosporine, an inhibitor of protein kinase C. The inactive phorbol ester, 4 alpha-phorbol 12,13-didecanoate, has no effect on the transport system. These data show that the choriocarcinoma cells express a taurine transporter with characteristics similar to those of the taurine transporter described in the normal human placenta, and that the activity of the transporter in these cells is under the regulatory control of protein kinase C.

scholarly journals Expression and protein kinase C-dependent regulation of peptide/H+ co-transport system in the Caco-2 human colon carcinoma cell line

1994 ◽  
Vol 299 (1) ◽  
pp. 253-260 ◽  
Author(s):  
M Brandsch ◽  
Y Miyamoto ◽  
V Ganapathy ◽  
F H Leibach
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Line ◽  
Transport System ◽  
Carcinoma Cell ◽  
Human Colon ◽  
Human Colon Carcinoma Cell ◽  
Colon Carcinoma Cell Line ◽  
Kinase C ◽  
Human Colon Carcinoma

The characteristics of the transport of the dipeptide glycylsarcosine were studied in the human colon carcinoma cell line Caco-2 grown as a monolayer on impermeable plastic support. Transport of glycylsarcosine in these cells was found to be Na(+)-independent, but was stimulated by an inwardly directed H+ gradient. This H(+)-dependent transport of glycylsarcosine was inhibited by di- and tri-peptides and also by the beta-lactam antibiotic cephalexin, but was unaffected by the amino acids glycine and leucine. The transport system exhibited a Michaelis-Menten constant (Kt) of 1.1 +/- 0.1 mM for glycylsarcosine. The specific activity of the transport system in this cell line was found to be maximal when the cultures were confluent. Treatment of the cells with phorbol esters which activate protein kinase C resulted in a significant inhibition of the transport system. This inhibition was specific and could be blocked if treatment was done in the presence of staurosporine, an inhibitor of protein kinase C. Kinetic analysis revealed that the inhibition was associated with a decrease in the maximal velocity, the Kt remaining unaffected. The phorbol-ester-induced inhibition of the peptide-transport system was not prevented by co-treatment with cycloheximide, an inhibitor of cellular protein synthesis. In addition, there was no change in the intracellular pH following treatment with the phorbol ester, suggesting that the effect was not due to alterations in the transmembrane pH gradient. It is concluded that the peptide/H+ co-transport system, which is known to exist in the normal intestine, is expressed in Caco-2 cells and that the function of the transport system is under the regulatory control of protein kinase C.

scholarly journals Regulation of taurine transporter activity in LLC-PK1 cells: role of protein synthesis and protein kinase C activation.

1991 ◽  
Vol 2 (5) ◽  
pp. 1021-1029 ◽  
Author(s):  
D P Jones ◽  
L A Miller ◽  
C Dowling ◽  
R W Chesney
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Free Medium ◽  
Taurine Transporter ◽  
Taurine Transport ◽  
Kinase C ◽  
Taurine Uptake ◽  
Protein Kinase C Activation

Taurine transporter activity increases after exposure of cultured renal epithelial cells to taurine-free medium for 24 h and decreases after incubation in high (500 microM) taurine. This adaptive response mimics that observed in rat kidney after manipulation of dietary taurine. In order to elucidate potential mechanisms involved in the regulation of beta-amino acid transporter activity, the role of RNA transcription, protein synthesis, and protein import (trafficking), as well as protein kinase C activation, on the control of taurine transport was examined in the continuous proximally derived LLC-PK1 renal cell line. Inhibition of RNA transcription with actinomycin D did not alter the up-regulatory and down-regulatory adaptive responses. Inhibition of protein synthesis with cycloheximide prevented the increased taurine transport in response to taurine-free medium as well as the decrease in taurine transport after exposure to high taurine. Colchicine prevented the response to taurine-free medium but had no effect on the response to high-taurine medium. Exposure of confluent cell monolayers to the active phorbol esters, phorbol 12-myristate 13-acetate and phorbol 12,13 dibutyrate, resulted in a reduction in taurine uptake. The effect was seen within minutes of exposure but was not observed in the presence of the inactive phorbol 4-alpha. This inhibitory action was blocked by staurosporin, an inhibitor of protein kinase C (PKC). Treatment of cells with the diacylglycerol kinase inhibitor R59022, which results in increased intracellular diacylglycerol, a natural stimulant of PKC, also inhibited taurine uptake, providing further evidence for a specific effect of PKC activation.(ABSTRACT TRUNCATED AT 250 WORDS)

Heterogeneity of the Ca2+ sensitivity of secretion in a pituitary gonadotrope cell line and its modulation by protein kinase C and Ca2+

2006 ◽  
Vol 207 (3) ◽  
pp. 668-674 ◽  
Author(s):  
Hui-Sheng Liu ◽  
Zhi-Tao Hu ◽  
Ke-Ming Zhou ◽  
Ya-Ming Jiu ◽  
Hua Yang ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Line ◽  
Kinase C

scholarly journals DNA Binding of TEA/ATTS Domain Factors Is Regulated by Protein Kinase C Phosphorylation in Human Choriocarcinoma Cells

2001 ◽  
Vol 276 (26) ◽  
pp. 23464-23470 ◽  
Author(s):  
Shi-Wen Jiang ◽  
Maoqing Dong ◽  
Miguel A. Trujillo ◽  
Laurence J. Miller ◽  
Norman L. Eberhardt
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dna Binding ◽  
Kinase C ◽  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells
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