Ganglioside GD1a Activates the Phosphorylation of EGFR in Porcine Oocytes Maturation in vitro

Ganglioside GD1a is specifically formed by the addition of sialic acid to ganglioside GM1a by ST3 β- galactoside α -2,3-sialyltransferase 2 (ST3GAL2). Above all, GD1a are known to be related with the functional regulation of several growth factor receptors, including activation and dimerization of e...

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Main Authors: Hyo-Jin Park, Jin-Woo Kim, Jae-Young Park, Seul-Gi Yang, Jae-Min Jung, Min-Ji Kim, Deog-Bon Koo
Format: Article
Language:English
Published: The Korean Society of Animal Reproduction and Biotechnology 2017-03-01
Series:Journal of Animal Reproduction and Biotechnology
Subjects:
Online Access:http://www.e-jarb.org/journal/view.html?uid=12&vmd=Full
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spelling doaj-5f96ec49e1c04d2dade12f504cbe3bdf2021-01-10T05:54:49ZengThe Korean Society of Animal Reproduction and BiotechnologyJournal of Animal Reproduction and Biotechnology2671-46392671-46632017-03-01321172410.12750/JET.2017.32.1.17Ganglioside GD1a Activates the Phosphorylation of EGFR in Porcine Oocytes Maturation in vitroHyo-Jin Park0Jin-Woo Kim1Jae-Young Park2Seul-Gi Yang3Jae-Min Jung4Min-Ji Kim5Deog-Bon Koo6Department of Biotechnology, College of Engineering, Daegu University, 201 Daegudae-ro, Jillyang, Gyeongsan, Gyeongbuk 38453, Republic of KoreaDepartment of Biotechnology, College of Engineering, Daegu University, 201 Daegudae-ro, Jillyang, Gyeongsan, Gyeongbuk 38453, Republic of KoreaDepartment of Biotechnology, College of Engineering, Daegu University, 201 Daegudae-ro, Jillyang, Gyeongsan, Gyeongbuk 38453, Republic of KoreaDepartment of Biotechnology, College of Engineering, Daegu University, 201 Daegudae-ro, Jillyang, Gyeongsan, Gyeongbuk 38453, Republic of KoreaDepartment of Biotechnology, College of Engineering, Daegu University, 201 Daegudae-ro, Jillyang, Gyeongsan, Gyeongbuk 38453, Republic of KoreaDepartment of Biotechnology, College of Engineering, Daegu University, 201 Daegudae-ro, Jillyang, Gyeongsan, Gyeongbuk 38453, Republic of KoreaDepartment of Biotechnology, College of Engineering, Daegu University, 201 Daegudae-ro, Jillyang, Gyeongsan, Gyeongbuk 38453, Republic of KoreaGanglioside GD1a is specifically formed by the addition of sialic acid to ganglioside GM1a by ST3 β- galactoside α -2,3-sialyltransferase 2 (ST3GAL2). Above all, GD1a are known to be related with the functional regulation of several growth factor receptors, including activation and dimerization of epidermal growth factor receptor (EGFR) in tumor cells. The activity of EGF and EGFR is known to be a very important factor for meiotic and cytoplasmic maturation during in vitro maturation (IVM) of mammalian oocytes. However, the role of gangliosides GD1a for EGFR-related signaling pathways in porcine oocyte is not yet clearly understood. Here, we investigated that the effect of ST3GAL2 as synthesizing enzyme GD1a for EGFR activation and phosphorylation during meiotic maturation. To investigate the expression of ST3GAL2 according to the EGF treatment (0, 10 and 50 ng/ml), we observed the patterns of ST3GAL2 genes expression by immunofluorescence staining in denuded oocyte (DO) and cumulus cell-oocyte-complex (COC) during IVM process (22 and 44 h), respectively. Expression levels of ST3GAL2 significantly decreased (p<0.01) in an EGF concentration (10 and 50 ng/ml) dependent manner. And fluorescence expression of ST3GAL2 increased (p<0.01) in the matured COCs for 44 h. Under high EGF concentration (50 ng/ml), ST3GAL2 protein levels was decreased (p<0.01), and their shown opposite expression pattern of phosphorylation-EGFR in COCs of 44 h. Phosphorylation of EGFR significantly increased (p<0.01) in matured COCs treated with GD1a for 44 h. In addition, ST3GAL2 protein levels significantly decreased (p<0.01) in GD1a (10 μM) treated COCs without reference to EGF pre-treatment. These results suggest that treatment of exogenous ganglioside GD1a may play an important role such as EGF in EGFR-related activation and phosphorylation in porcine oocyte maturation of in vitro.http://www.e-jarb.org/journal/view.html?uid=12&vmd=Fullganglioside gd1ast3gal2egfr phosphorylationoocyte maturationporcine
collection DOAJ
language English
format Article
sources DOAJ
author Hyo-Jin Park
Jin-Woo Kim
Jae-Young Park
Seul-Gi Yang
Jae-Min Jung
Min-Ji Kim
Deog-Bon Koo
spellingShingle Hyo-Jin Park
Jin-Woo Kim
Jae-Young Park
Seul-Gi Yang
Jae-Min Jung
Min-Ji Kim
Deog-Bon Koo
Ganglioside GD1a Activates the Phosphorylation of EGFR in Porcine Oocytes Maturation in vitro
Journal of Animal Reproduction and Biotechnology
ganglioside gd1a
st3gal2
egfr phosphorylation
oocyte maturation
porcine
author_facet Hyo-Jin Park
Jin-Woo Kim
Jae-Young Park
Seul-Gi Yang
Jae-Min Jung
Min-Ji Kim
Deog-Bon Koo
author_sort Hyo-Jin Park
title Ganglioside GD1a Activates the Phosphorylation of EGFR in Porcine Oocytes Maturation in vitro
title_short Ganglioside GD1a Activates the Phosphorylation of EGFR in Porcine Oocytes Maturation in vitro
title_full Ganglioside GD1a Activates the Phosphorylation of EGFR in Porcine Oocytes Maturation in vitro
title_fullStr Ganglioside GD1a Activates the Phosphorylation of EGFR in Porcine Oocytes Maturation in vitro
title_full_unstemmed Ganglioside GD1a Activates the Phosphorylation of EGFR in Porcine Oocytes Maturation in vitro
title_sort ganglioside gd1a activates the phosphorylation of egfr in porcine oocytes maturation in vitro
publisher The Korean Society of Animal Reproduction and Biotechnology
series Journal of Animal Reproduction and Biotechnology
issn 2671-4639
2671-4663
publishDate 2017-03-01
description Ganglioside GD1a is specifically formed by the addition of sialic acid to ganglioside GM1a by ST3 β- galactoside α -2,3-sialyltransferase 2 (ST3GAL2). Above all, GD1a are known to be related with the functional regulation of several growth factor receptors, including activation and dimerization of epidermal growth factor receptor (EGFR) in tumor cells. The activity of EGF and EGFR is known to be a very important factor for meiotic and cytoplasmic maturation during in vitro maturation (IVM) of mammalian oocytes. However, the role of gangliosides GD1a for EGFR-related signaling pathways in porcine oocyte is not yet clearly understood. Here, we investigated that the effect of ST3GAL2 as synthesizing enzyme GD1a for EGFR activation and phosphorylation during meiotic maturation. To investigate the expression of ST3GAL2 according to the EGF treatment (0, 10 and 50 ng/ml), we observed the patterns of ST3GAL2 genes expression by immunofluorescence staining in denuded oocyte (DO) and cumulus cell-oocyte-complex (COC) during IVM process (22 and 44 h), respectively. Expression levels of ST3GAL2 significantly decreased (p<0.01) in an EGF concentration (10 and 50 ng/ml) dependent manner. And fluorescence expression of ST3GAL2 increased (p<0.01) in the matured COCs for 44 h. Under high EGF concentration (50 ng/ml), ST3GAL2 protein levels was decreased (p<0.01), and their shown opposite expression pattern of phosphorylation-EGFR in COCs of 44 h. Phosphorylation of EGFR significantly increased (p<0.01) in matured COCs treated with GD1a for 44 h. In addition, ST3GAL2 protein levels significantly decreased (p<0.01) in GD1a (10 μM) treated COCs without reference to EGF pre-treatment. These results suggest that treatment of exogenous ganglioside GD1a may play an important role such as EGF in EGFR-related activation and phosphorylation in porcine oocyte maturation of in vitro.
topic ganglioside gd1a
st3gal2
egfr phosphorylation
oocyte maturation
porcine
url http://www.e-jarb.org/journal/view.html?uid=12&vmd=Full
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