Gestation-associated changes in the glycosylation of placental insulin and insulin-like growth factor receptors
Само за регистроване кориснике
2016
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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 betwee...n 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.
Кључне речи:
N-glycosylation / Placenta / Gestation / IR / IGF1R / IGF2RИзвор:
Placenta, 2016, 39, 70-76Издавач:
- Elsevier
Финансирање / пројекти:
- Структурне карактеристике везујућих протеина и рецептора за инсулину сличне факторе раста (IGF), њихове интеракције са другим физиолошким молекулима и промене код поремећаја метаболизма (RS-MESTD-Basic Research (BR or ON)-173042)
DOI: 10.1016/j.placenta.2016.01.005
ISSN: 0143-4004; 1532-3102
PubMed: 26992677
WoS: 000373543800011
Scopus: 2-s2.0-84960845391
Колекције
Институција/група
VinčaTY - 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 . .