Induction and activation of latent transforming growth factor-β1 are carried out by two distinct domains of pregnancy-specific glycoprotein 1 (PSG1)

Angela Ballesteros; Margaret M. Mentink-Kane; James Warren; Gerardo G. Kaplan; Gabriela S. Dveksler

doi:10.1074/jbc.M114.597518

Induction and activation of latent transforming growth factor-β₁ are carried out by two distinct domains of pregnancy-specific glycoprotein 1 (PSG1)

Angela Ballesteros
, Margaret M. Mentink-Kane
, James Warren
, Gerardo G. Kaplan
, Gabriela S. Dveksler^*

^*Corresponding author for this work

Pathology

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

31 Scopus citations

Abstract

Background: PSG1 is secreted by placental cells and regulates TGF-β1. Results: The B2 domain of PSG1 activates latent TGF-β1, whereas macrophage induction of latent TGF-β1 relies on the LYHY amino acid sequence within the N-terminal domain. Conclusion: PSG1 exerts bifunctional activity through two distinct domains, resulting in an increase in active TGF-β1. Significance: These data describe a mechanism by which PSG1 modulates TGF-β1 during pregnancy.

Original language	English
Pages (from-to)	4422-4431
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	290
Issue number	7
DOIs	https://doi.org/10.1074/jbc.M114.597518
State	Published - 13 Feb 2015

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title = "Induction and activation of latent transforming growth factor-β1 are carried out by two distinct domains of pregnancy-specific glycoprotein 1 (PSG1)",

abstract = "Background: PSG1 is secreted by placental cells and regulates TGF-β1. Results: The B2 domain of PSG1 activates latent TGF-β1, whereas macrophage induction of latent TGF-β1 relies on the LYHY amino acid sequence within the N-terminal domain. Conclusion: PSG1 exerts bifunctional activity through two distinct domains, resulting in an increase in active TGF-β1. Significance: These data describe a mechanism by which PSG1 modulates TGF-β1 during pregnancy.",

author = "Angela Ballesteros and Mentink-Kane, \{Margaret M.\} and James Warren and Kaplan, \{Gerardo G.\} and Dveksler, \{Gabriela S.\}",

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AU - Ballesteros, Angela

AU - Mentink-Kane, Margaret M.

AU - Warren, James

AU - Kaplan, Gerardo G.

AU - Dveksler, Gabriela S.

PY - 2015/2/13

Y1 - 2015/2/13

N2 - Background: PSG1 is secreted by placental cells and regulates TGF-β1. Results: The B2 domain of PSG1 activates latent TGF-β1, whereas macrophage induction of latent TGF-β1 relies on the LYHY amino acid sequence within the N-terminal domain. Conclusion: PSG1 exerts bifunctional activity through two distinct domains, resulting in an increase in active TGF-β1. Significance: These data describe a mechanism by which PSG1 modulates TGF-β1 during pregnancy.

AB - Background: PSG1 is secreted by placental cells and regulates TGF-β1. Results: The B2 domain of PSG1 activates latent TGF-β1, whereas macrophage induction of latent TGF-β1 relies on the LYHY amino acid sequence within the N-terminal domain. Conclusion: PSG1 exerts bifunctional activity through two distinct domains, resulting in an increase in active TGF-β1. Significance: These data describe a mechanism by which PSG1 modulates TGF-β1 during pregnancy.

UR - https://www.scopus.com/pages/publications/84922787429

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DO - 10.1074/jbc.M114.597518

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JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 7

ER -

Induction and activation of latent transforming growth factor-β1 are carried out by two distinct domains of pregnancy-specific glycoprotein 1 (PSG1)

Abstract

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Induction and activation of latent transforming growth factor-β₁ are carried out by two distinct domains of pregnancy-specific glycoprotein 1 (PSG1)