scholarly journals Protein Kinase C Activation Promotes the Internalization of the Human Cationic Amino Acid Transporter hCAT-1

2004 ◽  
Vol 279 (52) ◽  
pp. 54185-54192 ◽  
Author(s):  
Alexander Rotmann ◽  
Dennis Strand ◽  
Ursula Martiné ◽  
Ellen I. Closs
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 Activation

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

scholarly journals Activation of classical protein kinase C reduces the expression of human cationic amino acid transporter 3 (hCAT-3) in the plasma membrane

2006 ◽  
Vol 395 (1) ◽  
pp. 117-123 ◽  
Author(s):  
Alexander Rotmann ◽  
Nicole Vékony ◽  
Davina Gassner ◽  
Günter Niegisch ◽  
Dennis Strand ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Amino Acid ◽  
Protein Kinase ◽  
Amino Acid Transporter ◽  
Cationic Amino Acid Transporter ◽  
Glioblastoma Cells ◽  
Cationic Amino Acid ◽  
Kinase C ◽  
Pkc Isoforms

We have previously shown that activation of PKC (protein kinase C) results in internalization of hCAT-1 [human CAT-1 (cationic amino acid transporter 1)] and a decrease in arginine transport [Rotmann, Strand, Martiné and Closs (2004) J. Biol. Chem. 279, 54185–54192]. However, others found increased transport rates for arginine in response to PKC activation, suggesting a differential effect of PKC on different CAT isoforms. Therefore we investigated the effect of PKC on hCAT-3, an isoform expressed in thymus, brain, ovary, uterus and mammary gland. In Xenopus laevis oocytes and human U373MG glioblastoma cells, hCAT-3-mediated L-arginine transport was significantly reduced upon treatment with compounds that activate classical PKC. In contrast, inactive phorbol esters and an activator of novel PKC isoforms had no effect. PKC inhibitors (including the PKCα-preferring Ro 31-8280) reduced the inhibitory effect of the PKC-activating compounds. Microscopic analyses revealed a PMA-induced reduction in the cell-surface expression of fusion proteins between hCAT-3 and enhanced green fluorescent protein expressed in X. laevis oocytes and glioblastoma cells. Western-blot analysis of biotinylated surface proteins demonstrated a PMA-induced decrease in hCAT-3 in the plasma membrane, but not in total protein lysates. Pretreatment with a PKC inhibitor also reduced this PMA effect. It is concluded that similar to hCAT-1, hCAT-3 activity is decreased by PKC via reduction of transporter molecules in the plasma membrane. Classical PKC isoforms seem to be responsible for this effect.

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.

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

scholarly journals l-Arginine and Cationic Amino Acid Transporter 2B Regulate Growth and Survival of Leishmania amazonensis Amastigotes in Macrophages

2007 ◽  
Vol 75 (6) ◽  
pp. 2802-2810 ◽  
Author(s):  
Nanchaya Wanasen ◽  
Carol L. MacLeod ◽  
Lesley G. Ellies ◽  
Lynn Soong
Keyword(s):  
Amino Acid ◽  
Amino Acid Transporter ◽  
Parasite Growth ◽  
Leishmania Amazonensis ◽  
Growth Enhancement ◽  
Cationic Amino Acid Transporter ◽  
Cationic Amino Acid ◽  
Arginine Transport ◽  
Ifn Γ ◽  
Acid Transporter

ABSTRACT Leishmania spp. are obligate intracellular parasites, requiring a suitable microenvironment for their growth within host cells. We previously reported that the growth of Leishmania amazonensis amastigotes in murine macrophages (Mφs) was enhanced in the presence of gamma interferon (IFN-γ), a Th1 cytokine normally associated with classical Mφ activation and killing of intracellular pathogens. In this study, we provided several lines of evidence suggesting that IFN-γ-mediated parasite growth enhancement was associated with l-arginine transport via mouse cationic amino acid transporter 2B (mCAT-2B). (i) mRNA expression of Slc7A2, the gene encoding for mCAT-2B, as well as l-arginine transport was increased in IFN-γ-treated Mφs. (ii) Supplementation of l-arginine in Mφ cultures increased parasite growth. (iii) Parasite growth enhancement in wild-type Mφs was inhibited in the presence of nonmetabolized l-arginine analogues. (iv) IFN-γ-mediated parasite growth was absent in Mφs derived from mCAT-2B-deficient mice. Although we detected a clear upregulation of mCAT-2B and l-arginine transport, no measurable iNOS or arginase activities were observed in IFN-γ-treated, infected Mφs. Together, these data suggest an involvement of a novel l-arginine usage independent of iNOS and arginase activities during IFN-γ-mediated parasite growth enhancement. A possible role of mCAT-2B in supplying l-arginine directly to the parasites for their proliferation is discussed.

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