TY  - JOUR
AU  - Robajac, Dragana
AU  - Vanhooren, Valerie
AU  - Masnikosa, Romana
AU  - Miković, Zeljko
AU  - Mandić, Vesna
AU  - Libert, Claude
AU  - Nedić, Olgica
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/934
AB  - Posttranslational modifications (PTM) which accompany pathological conditions affect protein structure, characteristics and modulate its activity. Glycosylation is one of the most frequent PTM influencing protein folding, localisation and function. Hypertension is a common gestational complication, which can lead to foetal growth restriction (IUGR) and even to foetal or maternal death. In this work we focused on the impact of preeclampsia complicated with IUGR on placental membrane N-glycome. Results have shown that preeclampsia reduced fucosylation of placental glycans, increased the appearance of paucimannosidic and mannosidic structures with lower number of mannose residues and decreased the amount of glycans with more mannose residues. Since preeclampsia is tightly connected to IUGR, glycosylation changes were investigated also on the functional membrane receptors responsible for growth: insulin receptor and the type 1 insulin-like growth factor receptor (IR and IGF1R). It was found that IR present in the IUGR placenta contained significantly less alpha 2,6-Sia. Therefore, glycans on placental membranes alter due to preeclampsia, but changes seen at the level of the entire N-glycome may be different from the changes detected at the level of a specific glycoprotein. The difference recorded due to pathology in one membrane molecule (IR) was not found in another homologous molecule (IGF1R). Thus, besides studying the glycosylation pattern of the entire placental membrane due to preeclampsia, it is inevitable to study directly glycoprotein of interest, as no general assumptions or extrapolations can be made. (C) 2015 Elsevier Inc All rights reserved.
PB  - Elsevier
T2  - Experimental and Molecular Pathology
T1  - Preeclampsia transforms membrane N-glycome in human placenta
VL  - 100
IS  - 1
SP  - 26
EP  - 30
DO  - 10.1016/j.yexmp.2015.11.029
ER  - 

@article{
author = "Robajac, Dragana and Vanhooren, Valerie and Masnikosa, Romana and Miković, Zeljko and Mandić, Vesna and Libert, Claude and Nedić, Olgica",
year = "2016",
abstract = "Posttranslational modifications (PTM) which accompany pathological conditions affect protein structure, characteristics and modulate its activity. Glycosylation is one of the most frequent PTM influencing protein folding, localisation and function. Hypertension is a common gestational complication, which can lead to foetal growth restriction (IUGR) and even to foetal or maternal death. In this work we focused on the impact of preeclampsia complicated with IUGR on placental membrane N-glycome. Results have shown that preeclampsia reduced fucosylation of placental glycans, increased the appearance of paucimannosidic and mannosidic structures with lower number of mannose residues and decreased the amount of glycans with more mannose residues. Since preeclampsia is tightly connected to IUGR, glycosylation changes were investigated also on the functional membrane receptors responsible for growth: insulin receptor and the type 1 insulin-like growth factor receptor (IR and IGF1R). It was found that IR present in the IUGR placenta contained significantly less alpha 2,6-Sia. Therefore, glycans on placental membranes alter due to preeclampsia, but changes seen at the level of the entire N-glycome may be different from the changes detected at the level of a specific glycoprotein. The difference recorded due to pathology in one membrane molecule (IR) was not found in another homologous molecule (IGF1R). Thus, besides studying the glycosylation pattern of the entire placental membrane due to preeclampsia, it is inevitable to study directly glycoprotein of interest, as no general assumptions or extrapolations can be made. (C) 2015 Elsevier Inc All rights reserved.",
publisher = "Elsevier",
journal = "Experimental and Molecular Pathology",
title = "Preeclampsia transforms membrane N-glycome in human placenta",
volume = "100",
number = "1",
pages = "26-30",
doi = "10.1016/j.yexmp.2015.11.029"
}

Robajac, D., Vanhooren, V., Masnikosa, R., Miković, Z., Mandić, V., Libert, C.,& Nedić, O.. (2016). Preeclampsia transforms membrane N-glycome in human placenta. in Experimental and Molecular Pathology
Elsevier., 100(1), 26-30.
https://doi.org/10.1016/j.yexmp.2015.11.029

Robajac D, Vanhooren V, Masnikosa R, Miković Z, Mandić V, Libert C, Nedić O. Preeclampsia transforms membrane N-glycome in human placenta. in Experimental and Molecular Pathology. 2016;100(1):26-30.
doi:10.1016/j.yexmp.2015.11.029 .

Robajac, Dragana, Vanhooren, Valerie, Masnikosa, Romana, Miković, Zeljko, Mandić, Vesna, Libert, Claude, Nedić, Olgica, "Preeclampsia transforms membrane N-glycome in human placenta" in Experimental and Molecular Pathology, 100, no. 1 (2016):26-30,
https://doi.org/10.1016/j.yexmp.2015.11.029 . .

TY  - JOUR
AU  - Robajac, Dragana
AU  - Masnikosa, Romana
AU  - Miković, Zeljko
AU  - Nedić, Olgica
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/994
AB  - Introduction: Insulin receptor (IR) and type 1 and type 2 insulin-like growth factor receptors (IGF1 R and IGF2R) play important roles in regulation of placental and foetal growth. All three receptors are abundantly glycosylated. N-glycosylation significantly affects protein conformation and may alter its function. We have recently found that the N-glycome of placental membrane proteins alters during gestation. The aim of the study presented herein was to investigate whether there were gestation-related changes in N-glycan profiles of placental IR and IGFRs. Methods: Placentas from healthy women at first (FTP) and third trimester (TTP) of pregnancy were collected, membrane proteins isolated, solubilised and used as the source of IR and IGFRs. Reactivity of glycoforms of IR and IGFRs with lectins was monitored by measuring radioactivity of I-125-ligands-receptors complexes. Results: Significant differences in the binding pattern of all three receptors to the lectins were observed between FTP and TTP, which suggest gestational changes in N-glycans bound to receptors. These changes include decrease in total fucosylated, core-fucosylated biantennary N-glycan (NA2F) and alpha 2,6-sialo-N-glycans (for IR); decrease in total fucosylated and a2,6-sialo-N-glycans and an increase in NA2F N-glycans (for IGF1R) and an increase in the total fucosylation and NA2F N-glycans (for IGF2R). Discussion: The gestational alterations in N-glycans attached to IR and IGFRs may represent a mechanism by which these receptors acquire new/additional roles as gestation progresses. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Elsevier
T2  - Placenta
T1  - Gestation-associated changes in the glycosylation of placental insulin and insulin-like growth factor receptors
VL  - 39
SP  - 70
EP  - 76
DO  - 10.1016/j.placenta.2016.01.005
ER  - 

@article{
author = "Robajac, Dragana and Masnikosa, Romana and Miković, Zeljko and Nedić, Olgica",
year = "2016",
abstract = "Introduction: Insulin receptor (IR) and type 1 and type 2 insulin-like growth factor receptors (IGF1 R and IGF2R) play important roles in regulation of placental and foetal growth. All three receptors are abundantly glycosylated. N-glycosylation significantly affects protein conformation and may alter its function. We have recently found that the N-glycome of placental membrane proteins alters during gestation. The aim of the study presented herein was to investigate whether there were gestation-related changes in N-glycan profiles of placental IR and IGFRs. Methods: Placentas from healthy women at first (FTP) and third trimester (TTP) of pregnancy were collected, membrane proteins isolated, solubilised and used as the source of IR and IGFRs. Reactivity of glycoforms of IR and IGFRs with lectins was monitored by measuring radioactivity of I-125-ligands-receptors complexes. Results: Significant differences in the binding pattern of all three receptors to the lectins were observed between FTP and TTP, which suggest gestational changes in N-glycans bound to receptors. These changes include decrease in total fucosylated, core-fucosylated biantennary N-glycan (NA2F) and alpha 2,6-sialo-N-glycans (for IR); decrease in total fucosylated and a2,6-sialo-N-glycans and an increase in NA2F N-glycans (for IGF1R) and an increase in the total fucosylation and NA2F N-glycans (for IGF2R). Discussion: The gestational alterations in N-glycans attached to IR and IGFRs may represent a mechanism by which these receptors acquire new/additional roles as gestation progresses. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier",
journal = "Placenta",
title = "Gestation-associated changes in the glycosylation of placental insulin and insulin-like growth factor receptors",
volume = "39",
pages = "70-76",
doi = "10.1016/j.placenta.2016.01.005"
}

Robajac, D., Masnikosa, R., Miković, Z.,& Nedić, O.. (2016). Gestation-associated changes in the glycosylation of placental insulin and insulin-like growth factor receptors. in Placenta
Elsevier., 39, 70-76.
https://doi.org/10.1016/j.placenta.2016.01.005

Robajac D, Masnikosa R, Miković Z, Nedić O. Gestation-associated changes in the glycosylation of placental insulin and insulin-like growth factor receptors. in Placenta. 2016;39:70-76.
doi:10.1016/j.placenta.2016.01.005 .

Robajac, Dragana, Masnikosa, Romana, Miković, Zeljko, Nedić, Olgica, "Gestation-associated changes in the glycosylation of placental insulin and insulin-like growth factor receptors" in Placenta, 39 (2016):70-76,
https://doi.org/10.1016/j.placenta.2016.01.005 . .