Placental alkaline phosphatase de-phosphorylates insulin-like growth factor (IGF)-binding protein-1

A. L. Solomon; K. W. Siddals; P. N. Baker; J. M. Gibson; John Aplin; M. Westwood

doi:10.1016/j.placenta.2014.04.014

Placental alkaline phosphatase de-phosphorylates insulin-like growth factor (IGF)-binding protein-1

A. L. Solomon, K. W. Siddals, P. N. Baker, J. M. Gibson, John Aplin, M. Westwood

Research output: Contribution to journal › Article › peer-review

Abstract

Background Insulin-like growth factors (IGF) regulate fetal growth through their effects on placenta. Their actions are influenced by IGF binding protein-1. Phosphorylated IGFBP-1 (pIGFBP-1) has high affinity for IGF-I and usually inhibits IGF-I activity but during pregnancy, it is de-phosphorylated to generate lower affinity isoforms and consequently, increased IGF bioavailability. Here we investigate the role of placenta in this process. Results Our data show that term human placental explants, but not their conditioned medium, can de-phosphorylate IGFBP-1 through the action of placental alkaline phosphatase (PLAP). Discussion PLAP-mediated de-phosphorylation of IGFBP-1 may provide a mechanism for controlling IGF-I bioavailability and action at the maternal/fetal interface. © 2014 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	520-522
Number of pages	2
Journal	Placenta
Volume	35
Issue number	7
DOIs	https://doi.org/10.1016/j.placenta.2014.04.014
Publication status	Published - 2014

Keywords

IGF
IGFBP-1
Maternal
PLAP
Trophoblast

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10.1016/j.placenta.2014.04.014

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Cite this

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title = "Placental alkaline phosphatase de-phosphorylates insulin-like growth factor (IGF)-binding protein-1",

abstract = "Background Insulin-like growth factors (IGF) regulate fetal growth through their effects on placenta. Their actions are influenced by IGF binding protein-1. Phosphorylated IGFBP-1 (pIGFBP-1) has high affinity for IGF-I and usually inhibits IGF-I activity but during pregnancy, it is de-phosphorylated to generate lower affinity isoforms and consequently, increased IGF bioavailability. Here we investigate the role of placenta in this process. Results Our data show that term human placental explants, but not their conditioned medium, can de-phosphorylate IGFBP-1 through the action of placental alkaline phosphatase (PLAP). Discussion PLAP-mediated de-phosphorylation of IGFBP-1 may provide a mechanism for controlling IGF-I bioavailability and action at the maternal/fetal interface. {\textcopyright} 2014 Elsevier Ltd. All rights reserved.",

keywords = "IGF, IGFBP-1, Maternal, PLAP, Trophoblast",

author = "Solomon, {A. L.} and Siddals, {K. W.} and Baker, {P. N.} and Gibson, {J. M.} and John Aplin and M. Westwood",

year = "2014",

doi = "10.1016/j.placenta.2014.04.014",

language = "English",

volume = "35",

pages = "520--522",

journal = "Placenta",

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TY - JOUR

T1 - Placental alkaline phosphatase de-phosphorylates insulin-like growth factor (IGF)-binding protein-1

AU - Solomon, A. L.

AU - Siddals, K. W.

AU - Baker, P. N.

AU - Gibson, J. M.

AU - Aplin, John

AU - Westwood, M.

PY - 2014

Y1 - 2014

N2 - Background Insulin-like growth factors (IGF) regulate fetal growth through their effects on placenta. Their actions are influenced by IGF binding protein-1. Phosphorylated IGFBP-1 (pIGFBP-1) has high affinity for IGF-I and usually inhibits IGF-I activity but during pregnancy, it is de-phosphorylated to generate lower affinity isoforms and consequently, increased IGF bioavailability. Here we investigate the role of placenta in this process. Results Our data show that term human placental explants, but not their conditioned medium, can de-phosphorylate IGFBP-1 through the action of placental alkaline phosphatase (PLAP). Discussion PLAP-mediated de-phosphorylation of IGFBP-1 may provide a mechanism for controlling IGF-I bioavailability and action at the maternal/fetal interface. © 2014 Elsevier Ltd. All rights reserved.

AB - Background Insulin-like growth factors (IGF) regulate fetal growth through their effects on placenta. Their actions are influenced by IGF binding protein-1. Phosphorylated IGFBP-1 (pIGFBP-1) has high affinity for IGF-I and usually inhibits IGF-I activity but during pregnancy, it is de-phosphorylated to generate lower affinity isoforms and consequently, increased IGF bioavailability. Here we investigate the role of placenta in this process. Results Our data show that term human placental explants, but not their conditioned medium, can de-phosphorylate IGFBP-1 through the action of placental alkaline phosphatase (PLAP). Discussion PLAP-mediated de-phosphorylation of IGFBP-1 may provide a mechanism for controlling IGF-I bioavailability and action at the maternal/fetal interface. © 2014 Elsevier Ltd. All rights reserved.

KW - IGF

KW - IGFBP-1

KW - Maternal

KW - PLAP

KW - Trophoblast

U2 - 10.1016/j.placenta.2014.04.014

DO - 10.1016/j.placenta.2014.04.014

M3 - Article

C2 - 24856042

SN - 0143-4004

VL - 35

SP - 520

EP - 522

JO - Placenta

JF - Placenta

IS - 7

ER -

Placental alkaline phosphatase de-phosphorylates insulin-like growth factor (IGF)-binding protein-1

Abstract

Keywords

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