Glucose-mediated inactivation of AMP-activated protein kinase reduces the levels of L-type amino acid transporter 1 mRNA in C2C12 cells

2017 ◽  
Vol 47 ◽  
pp. 13-20 ◽  
Author(s):  
Yu Yamamoto ◽  
Ran Sawa ◽  
Ikumi Wake ◽  
Ayaka Morimoto ◽  
Yasuhiko Okimura
Keyword(s):  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Transporter ◽  
C2c12 Cells ◽  
Acid Transporter ◽  
Amp Activated Protein Kinase

Protein kinase C restricts transport of carnitine by amino acid transporter ATB0,+ apically localized in the blood–brain barrier

2014 ◽  
Vol 554 ◽  
pp. 28-35 ◽  
Author(s):  
Katarzyna Michalec ◽  
Caroline Mysiorek ◽  
Mélanie Kuntz ◽  
Vincent Bérézowski ◽  
Andrzej A. Szczepankiewicz ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Blood Brain Barrier ◽  
Amino Acid Transporter ◽  
Brain Barrier ◽  
Kinase C ◽  
Blood Brain ◽  
Acid Transporter

Effects of Volatile Anesthetics on Glutamate Transporter, Excitatory Amino Acid Transporter Type 3

2002 ◽  
Vol 96 (6) ◽  
pp. 1492-1497 ◽  
Author(s):  
Sang-Hwan Do ◽  
Ganesan L. Kamatchi ◽  
Jacqueline M. Washington ◽  
Zhiyi Zuo
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Excitatory Amino Acid ◽  
Volatile Anesthetics ◽  
Amino Acid Transporter ◽  
Excitatory Amino Acid Transporter ◽  
Kinase C ◽  
Acid Transporter ◽  
Type 3

Background Glutamate transporters play an important role in maintaining extracellular glutamate homeostasis. The authors studied the effects of volatile anesthetics on one type of glutamate transporters, excitatory amino acid transporter type 3 (EAAT3), and the role of protein kinase C in mediating these effects. Methods Excitatory amino acid transporter type 3 was expressed in Xenopus oocytes by injection of EAAT3 mRNA. Using two-electrode voltage clamp, membrane currents were recorded before, during, and after application of L-glutamate. Responses were quantified by integrating the current trace and are reported as microcoulombs. Data are mean +/- SEM. Results L-Glutamate-induced responses were increased gradually with the increased concentrations of isoflurane, a volatile anesthetic. At 0.52 and 0.70 mm isoflurane, the inward current was significantly increased compared with control. Isoflurane (0.70 mm) significantly increased Vmax (maximum velocity) (3.6 +/- 0.4 to 5.1 +/- 0.4 microC; P < 0.05) but not Km (Michoelis-Menten Constant) (55.4 +/- 17.0 vs. 61.7 +/- 13.6 microm; P > 0.05) of EAAT3 for glutamate compared with control. Treatment of the oocytes with phorbol-12-myrisate-13-acetate, a protein kinase C activator, caused a significant increase in transporter current (1.7 +/- 0.2 to 2.5 +/- 0.2 microC; P < 0.05). Responses in the presence of the combination of phorbol-12-myrisate-13-acetate and volatile anesthetics (isoflurane, halothane, or sevoflurane) were not greater than those when volatile anesthetic was present alone. Oocytes pretreated with any of the three protein kinase C inhibitors alone (chelerythrine, staurosporine, or calphostin C) did not affect basal transporter current. Although chelerythrine did not change the anesthetic effects on the activity of EAAT3, staurosporine or calphostin C abolished the anesthetic-induced increase of EAAT3 activity. Conclusions These data suggest that volatile anesthetics enhance EAAT3 activity and that protein kinase C is involved in mediating these anesthetic effects.

scholarly journals Protein kinase C activation upregulates human L-type amino acid transporter 2 function

2021 ◽  
Vol 71 (1) ◽  
Author(s):  
Hanae Morio ◽  
Yoshie Reien ◽  
Yuri Hirayama ◽  
Hirofumi Hashimoto ◽  
Naohiko Anzai
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
De Novo ◽  
Amino Acid Transporter ◽  
Regulation System ◽  
Membrane Insertion ◽  
Kinase C ◽  
Acid Transporter ◽  
Pkc Activation

AbstractL-type amino acid transporter 2 (LAT2) is a Na+-independent neutral amino acid transporter, whose function regulation system remains unclarified. Since protein kinase C (PKC) is known to regulate the functions of various transporters, we investigated whether human LAT2 (hLAT2) function is regulated by PKC. In mouse proximal tubule S2 cells, hLAT2 transport activity was upregulated by PKC activation. However, we found that the mRNA and protein expression of hLAT2 was not affected by PKC activation and that the upregulation was independent of the three potential PKC consensus sites in the hLAT2 amino acid sequence. Moreover, we found that PKC activation upregulated the Vmax value for hLAT2-mediated alanine transport, which was not accompanied by the induction of hLAT2 membrane insertion. In conclusion, we showed that hLAT2 function is upregulated by PKC activation, which is not related to either the de novo synthesis, the phosphorylation or the membrane insertion of hLAT2.

scholarly journals Protein Kinase C-dependent Ubiquitination and Clathrin-mediated Endocytosis of the Cationic Amino Acid Transporter CAT-1

2011 ◽  
Vol 286 (10) ◽  
pp. 8697-8706 ◽  
Author(s):  
Arnau Vina-Vilaseca ◽  
Julia Bender-Sigel ◽  
Tatiana Sorkina ◽  
Ellen Ildicho Closs ◽  
Alexander Sorkin
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Transporter ◽  
Cationic Amino Acid Transporter ◽  
Cationic Amino Acid ◽  
Kinase C ◽  
Acid Transporter

Protein kinase C regulates amino acid transporter ATB0,+

2012 ◽  
Vol 422 (1) ◽  
pp. 64-69 ◽  
Author(s):  
Łukasz Samluk ◽  
Magdalena Czeredys ◽  
Krzysztof Skowronek ◽  
Katarzyna A. Nałęcz
Keyword(s):  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Transporter ◽  
Kinase C ◽  
Acid Transporter
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