PAT1 (SLC36A1) shows nuclear localization and affect growth of smooth muscle cells from rats
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PAT1 (SLC36A1) shows nuclear localization and affect growth of smooth muscle cells from rats. / Jensen, Anne; Figueiredo-Larsen, Evan Manuel; Holm, René; Broberg, Mie Larsen; Brodin, Birger; Nielsen, Carsten Uhd.
In: A J P: Endocrinology and Metabolism (Online), Vol. 306, 01.2014, p. E65-E74.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - PAT1 (SLC36A1) shows nuclear localization and affect growth of smooth muscle cells from rats
AU - Jensen, Anne
AU - Figueiredo-Larsen, Evan Manuel
AU - Holm, René
AU - Broberg, Mie Larsen
AU - Brodin, Birger
AU - Nielsen, Carsten Uhd
PY - 2014/1
Y1 - 2014/1
N2 - The proton-coupled amino acid transporter 1 (PAT1) is a transporter of amino acids in small intestinal enterocytes. PAT1 is, however, also capable of regulating cell growth and sensing the availability of amino acids in other cell types. The aim of the present study was to investigate the localization and function of PAT1 in smooth muscle cells (SMCs). The PAT1 protein was found in smooth muscles from rat intestine and in the embryonic rat aorta cell line A7r5. Immunolocalization and cellular fractionation studies revealed that the majority of the PAT1 protein located within the cell nucleus of A7r5. These results were confirmed in primary SMCs derived from rat aorta and colon. A 3'-untranslated region of the PAT1 transcript directed the nuclear localization. Neither cellular starvation nor cell division altered the nuclear localization. In agreement, uptake studies of L-proline, a PAT1 substrate, in A7r5 cells suggested an alternative role for PAT1 in SMCs than in transport. To shed light on the function of PAT1 in A7r5 cells, experiments with down regulation of the PAT1 level using a siRNA approach were conducted. The growth rates of the cells were evaluated and knock-down of PAT1 lead to induced cellular growth suggesting a role for PAT1 in regulating cellular proliferation of SMCs.
AB - The proton-coupled amino acid transporter 1 (PAT1) is a transporter of amino acids in small intestinal enterocytes. PAT1 is, however, also capable of regulating cell growth and sensing the availability of amino acids in other cell types. The aim of the present study was to investigate the localization and function of PAT1 in smooth muscle cells (SMCs). The PAT1 protein was found in smooth muscles from rat intestine and in the embryonic rat aorta cell line A7r5. Immunolocalization and cellular fractionation studies revealed that the majority of the PAT1 protein located within the cell nucleus of A7r5. These results were confirmed in primary SMCs derived from rat aorta and colon. A 3'-untranslated region of the PAT1 transcript directed the nuclear localization. Neither cellular starvation nor cell division altered the nuclear localization. In agreement, uptake studies of L-proline, a PAT1 substrate, in A7r5 cells suggested an alternative role for PAT1 in SMCs than in transport. To shed light on the function of PAT1 in A7r5 cells, experiments with down regulation of the PAT1 level using a siRNA approach were conducted. The growth rates of the cells were evaluated and knock-down of PAT1 lead to induced cellular growth suggesting a role for PAT1 in regulating cellular proliferation of SMCs.
U2 - 10.1152/ajpendo.00322.2013
DO - 10.1152/ajpendo.00322.2013
M3 - Journal article
C2 - 24222668
VL - 306
SP - E65-E74
JO - A J P: Endocrinology and Metabolism (Online)
JF - A J P: Endocrinology and Metabolism (Online)
SN - 1522-1555
ER -
ID: 75364924