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Protein kinase C-mediated impairment of glutamine outward transport and SN1 transporter distribution by ammonia in mouse cortical astrocytes.

Abstract：

:SN1, a system N amino acid transporter specific for astrocytes, is mainly responsible for export of newly synthesized L-glutamine from the cells. Astrocytic retention of L-glutamine which plays a critical role in ammonia-induced astrocytic swelling resulting in brain edema, could be tentatively attributed to the impaired L-glutamine export from astrocytes. The present study demonstrates that treatment of cultured mouse cortical astrocytes for 24 h with 5 mM ammonium chloride ("ammonia") inhibits the system N-mediated L-glutamine transport out of the cell, and that this inhibition is related to the reduced presence of the SN1 transporter on the cell membrane. Ammonia decreased total protein kinase C (PKC) activity in the absence but not in the presence of PKC activator, phorbol 12-myristate 13-acetate (PMA), and activation of PKC by PMA reversed both the ammonia-induced decrease of system N-mediated L-glutamine release and ammonia-induced SN1 deficit in the membrane fraction. However, while ammonia did not change the protein level of PKCα isoform, it decreased the protein content of PKCδ. Moreover, ammonia treatment increased the cell surface expression of SN1 in cells with silenced PKCα and PKCδ. Silencing of PKCδ abrogated the decrease of system N (SN1)-mediated L-glutamine release by ammonia. The results implicate the involvement of PKCδ in the inhibition of SN1 membrane expression and activity by ammonia.

journal_name

Neurochem Int

journal_title

Neurochemistry international

authors

Dąbrowska K,Albrecht J,Zielińska M

doi

10.1016/j.neuint.2018.07.001

subject

Has Abstract

pub_date

2018-09-01 00:00:00

pages

225-232

eissn

0197-0186

issn

1872-9754

pii

S0197-0186(18)30037-8

journal_volume

118

pub_type

杂志文章

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