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Phylogenesis and Biological Characterization of a New Glucose Transporter in the Chicken (Gallus gallus), GLUT12.

Coudert E, Pascal G, Dupont J, Simon J, Cailleau-Audouin E, Crochet S, Duclos MJ, Tesseraud S, Métayer-Coustard S - PLoS ONE (2015)

Bottom Line: Third a physiological characterization was performed: SLC2A12 mRNA levels were significantly lowered in fed chickens subjected to insulin immuno-neutralization.Finally, recruitment of immuno-reactive GLUT12 to the muscle plasma membrane was increased following 1h of intraperitoneal insulin administration (compared to a control fasted state).In conclusion, these results suggest that the facilitative glucose transporter protein GLUT12 could act in chicken muscle as an insulin-sensitive transporter that is qualitatively similar to GLUT4 in mammals.

View Article: PubMed Central - PubMed

Affiliation: UR83 Recherches Avicoles, Institut National de la Recherche Agronomique, Nouzilly, France.

ABSTRACT
In mammals, insulin-sensitive GLUTs, including GLUT4, are recruited to the plasma membrane of adipose and muscle tissues in response to insulin. The GLUT4 gene is absent from the chicken genome, and no functional insulin-sensitive GLUTs have been characterized in chicken tissues to date. A nucleotide sequence is predicted to encode a chicken GLUT12 ortholog and, interestingly, GLUT12 has been described to act as an insulin-sensitive GLUT in mammals. It encodes a 596 amino acid protein exhibiting 71% identity with human GLUT12. First, we present the results of a phylogenetic study showing the stability of this gene during evolution of vertebrates. Second, tissue distribution of chicken SLC2A12 mRNA was characterized by RT-PCR. It was predominantly expressed in skeletal muscle and heart. Protein distribution was analysed by Western blotting using an anti-human GLUT12 antibody directed against a highly conserved region (87% of identity). An immuno-reactive band of the expected size (75kDa) was detected in the same tissues. Third a physiological characterization was performed: SLC2A12 mRNA levels were significantly lowered in fed chickens subjected to insulin immuno-neutralization. Finally, recruitment of immuno-reactive GLUT12 to the muscle plasma membrane was increased following 1h of intraperitoneal insulin administration (compared to a control fasted state). Thus insulin administration elicited membrane GLUT12 recruitment. In conclusion, these results suggest that the facilitative glucose transporter protein GLUT12 could act in chicken muscle as an insulin-sensitive transporter that is qualitatively similar to GLUT4 in mammals.

No MeSH data available.


Phylogenetic tree of multiple alignments of all known chicken GLUT protein sequences.The analysis of chicken GLUTs was performed on the Phylogeny.fr platform (http://www.phylogeny.fr; [20, 21]) using Ensembl protein IDs. The tree was constructed as described in Materials and Methods. Reliability of internal branches was assessed using the aLRT test. The scale represents the substitution rate.
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pone.0139517.g001: Phylogenetic tree of multiple alignments of all known chicken GLUT protein sequences.The analysis of chicken GLUTs was performed on the Phylogeny.fr platform (http://www.phylogeny.fr; [20, 21]) using Ensembl protein IDs. The tree was constructed as described in Materials and Methods. Reliability of internal branches was assessed using the aLRT test. The scale represents the substitution rate.

Mentions: Up to ten predicted and annoted GLUTs were found in the Ensembl chicken database (Ensembl release 75; Table 1). According to the phylogenetic analysis of these chicken GLUTs (Fig 1), we discriminated three main branches corresponding to the three classes of GLUTs described in mammals: Class I (GLUT1, 2, and 3), Class II (GLUT5, 9 and 11) and Class III (GLUT6, 8, 10 and 12). The different chicken GLUTs showed 24 to 69% of identity between the different paralogs, highest percentage of identity being found between GLUT1 and GLUT3 (Table 3).


Phylogenesis and Biological Characterization of a New Glucose Transporter in the Chicken (Gallus gallus), GLUT12.

Coudert E, Pascal G, Dupont J, Simon J, Cailleau-Audouin E, Crochet S, Duclos MJ, Tesseraud S, Métayer-Coustard S - PLoS ONE (2015)

Phylogenetic tree of multiple alignments of all known chicken GLUT protein sequences.The analysis of chicken GLUTs was performed on the Phylogeny.fr platform (http://www.phylogeny.fr; [20, 21]) using Ensembl protein IDs. The tree was constructed as described in Materials and Methods. Reliability of internal branches was assessed using the aLRT test. The scale represents the substitution rate.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4592010&req=5

pone.0139517.g001: Phylogenetic tree of multiple alignments of all known chicken GLUT protein sequences.The analysis of chicken GLUTs was performed on the Phylogeny.fr platform (http://www.phylogeny.fr; [20, 21]) using Ensembl protein IDs. The tree was constructed as described in Materials and Methods. Reliability of internal branches was assessed using the aLRT test. The scale represents the substitution rate.
Mentions: Up to ten predicted and annoted GLUTs were found in the Ensembl chicken database (Ensembl release 75; Table 1). According to the phylogenetic analysis of these chicken GLUTs (Fig 1), we discriminated three main branches corresponding to the three classes of GLUTs described in mammals: Class I (GLUT1, 2, and 3), Class II (GLUT5, 9 and 11) and Class III (GLUT6, 8, 10 and 12). The different chicken GLUTs showed 24 to 69% of identity between the different paralogs, highest percentage of identity being found between GLUT1 and GLUT3 (Table 3).

Bottom Line: Third a physiological characterization was performed: SLC2A12 mRNA levels were significantly lowered in fed chickens subjected to insulin immuno-neutralization.Finally, recruitment of immuno-reactive GLUT12 to the muscle plasma membrane was increased following 1h of intraperitoneal insulin administration (compared to a control fasted state).In conclusion, these results suggest that the facilitative glucose transporter protein GLUT12 could act in chicken muscle as an insulin-sensitive transporter that is qualitatively similar to GLUT4 in mammals.

View Article: PubMed Central - PubMed

Affiliation: UR83 Recherches Avicoles, Institut National de la Recherche Agronomique, Nouzilly, France.

ABSTRACT
In mammals, insulin-sensitive GLUTs, including GLUT4, are recruited to the plasma membrane of adipose and muscle tissues in response to insulin. The GLUT4 gene is absent from the chicken genome, and no functional insulin-sensitive GLUTs have been characterized in chicken tissues to date. A nucleotide sequence is predicted to encode a chicken GLUT12 ortholog and, interestingly, GLUT12 has been described to act as an insulin-sensitive GLUT in mammals. It encodes a 596 amino acid protein exhibiting 71% identity with human GLUT12. First, we present the results of a phylogenetic study showing the stability of this gene during evolution of vertebrates. Second, tissue distribution of chicken SLC2A12 mRNA was characterized by RT-PCR. It was predominantly expressed in skeletal muscle and heart. Protein distribution was analysed by Western blotting using an anti-human GLUT12 antibody directed against a highly conserved region (87% of identity). An immuno-reactive band of the expected size (75kDa) was detected in the same tissues. Third a physiological characterization was performed: SLC2A12 mRNA levels were significantly lowered in fed chickens subjected to insulin immuno-neutralization. Finally, recruitment of immuno-reactive GLUT12 to the muscle plasma membrane was increased following 1h of intraperitoneal insulin administration (compared to a control fasted state). Thus insulin administration elicited membrane GLUT12 recruitment. In conclusion, these results suggest that the facilitative glucose transporter protein GLUT12 could act in chicken muscle as an insulin-sensitive transporter that is qualitatively similar to GLUT4 in mammals.

No MeSH data available.