Protein tyrosine phosphorylation signaling in the differentiation of human endometrial stromal cells

Tetsuo Maruyama, Yurie Yamamoto, Nozomi Sakai, Aki Shimizu, Asuka Shimoki, Takahiro Masuda, Yasunori Yoshimura

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Reversible protein tyrosine phosphorylation, coordinately controlled by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs), is a critical element in signal transduction pathways regulating cell growth, differentiation, apoptosis, and tumorigenesis. The differentiation of human endometrial stromal cells (decidualization) is crucial for successful embryo implantation and maintenance of pregnancy; however, little is known about the molecular events involving tyrosine phosphorylation, PTKs, and PTPs in the process of decidualization. We have previously reported that the tyrosine kinase activity of c-Src belonging to the Src family kinase is increased together with altered tyrosine phosphorylation of several cellular proteins in the in vitro model of decidualization. Focal adhesion kinase (FAK) and paxillin are known to form a complex with c-Src at the focal contacts and to participate in the integrin-mediated signal transduction as c-Src substrates. Those focal adhesion proteins, however, are not hyperphosphorylated on tyrosine during decidualization. Moreover, the loss of focal adhesions and the disorganization of the actin-based cytoskeleton were observed in decidualized stromal cells, suggesting that the escape from regulation by c-Src may be in part due to the decidualization-induced disruption of the interaction between the focal adhesion proteins and c-Src. These findings collectively indicate that decidual c-Src may activate signaling pathway(s) different from the integrin-mediated signaling cascade involving FAK and paxillin. This review summarizes our recent studies on the tyrosine phosphorylation signaling pathway(s) in decidualization.

Original languageEnglish
Pages (from-to)93-99
Number of pages7
JournalKeio Journal of Medicine
Volume51
Issue number2
Publication statusPublished - 2002 Mar

Fingerprint

Stromal Cells
Focal Adhesions
Tyrosine
Phosphorylation
Paxillin
Focal Adhesion Protein-Tyrosine Kinases
Protein Tyrosine Phosphatases
Proteins
Integrins
Protein-Tyrosine Kinases
Signal Transduction
Pregnancy Maintenance
src-Family Kinases
Actin Cytoskeleton
Cell Differentiation
Carcinogenesis
Apoptosis
Growth

Keywords

  • C-Src
  • Decidualization
  • Endometrium
  • Focal adhesion
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Maruyama, T., Yamamoto, Y., Sakai, N., Shimizu, A., Shimoki, A., Masuda, T., & Yoshimura, Y. (2002). Protein tyrosine phosphorylation signaling in the differentiation of human endometrial stromal cells. Keio Journal of Medicine, 51(2), 93-99.

Protein tyrosine phosphorylation signaling in the differentiation of human endometrial stromal cells. / Maruyama, Tetsuo; Yamamoto, Yurie; Sakai, Nozomi; Shimizu, Aki; Shimoki, Asuka; Masuda, Takahiro; Yoshimura, Yasunori.

In: Keio Journal of Medicine, Vol. 51, No. 2, 03.2002, p. 93-99.

Research output: Contribution to journalArticle

Maruyama, T, Yamamoto, Y, Sakai, N, Shimizu, A, Shimoki, A, Masuda, T & Yoshimura, Y 2002, 'Protein tyrosine phosphorylation signaling in the differentiation of human endometrial stromal cells', Keio Journal of Medicine, vol. 51, no. 2, pp. 93-99.
Maruyama, Tetsuo ; Yamamoto, Yurie ; Sakai, Nozomi ; Shimizu, Aki ; Shimoki, Asuka ; Masuda, Takahiro ; Yoshimura, Yasunori. / Protein tyrosine phosphorylation signaling in the differentiation of human endometrial stromal cells. In: Keio Journal of Medicine. 2002 ; Vol. 51, No. 2. pp. 93-99.
@article{627abf17b22e461cba34efadc0bc06ca,
title = "Protein tyrosine phosphorylation signaling in the differentiation of human endometrial stromal cells",
abstract = "Reversible protein tyrosine phosphorylation, coordinately controlled by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs), is a critical element in signal transduction pathways regulating cell growth, differentiation, apoptosis, and tumorigenesis. The differentiation of human endometrial stromal cells (decidualization) is crucial for successful embryo implantation and maintenance of pregnancy; however, little is known about the molecular events involving tyrosine phosphorylation, PTKs, and PTPs in the process of decidualization. We have previously reported that the tyrosine kinase activity of c-Src belonging to the Src family kinase is increased together with altered tyrosine phosphorylation of several cellular proteins in the in vitro model of decidualization. Focal adhesion kinase (FAK) and paxillin are known to form a complex with c-Src at the focal contacts and to participate in the integrin-mediated signal transduction as c-Src substrates. Those focal adhesion proteins, however, are not hyperphosphorylated on tyrosine during decidualization. Moreover, the loss of focal adhesions and the disorganization of the actin-based cytoskeleton were observed in decidualized stromal cells, suggesting that the escape from regulation by c-Src may be in part due to the decidualization-induced disruption of the interaction between the focal adhesion proteins and c-Src. These findings collectively indicate that decidual c-Src may activate signaling pathway(s) different from the integrin-mediated signaling cascade involving FAK and paxillin. This review summarizes our recent studies on the tyrosine phosphorylation signaling pathway(s) in decidualization.",
keywords = "C-Src, Decidualization, Endometrium, Focal adhesion, Tyrosine phosphorylation",
author = "Tetsuo Maruyama and Yurie Yamamoto and Nozomi Sakai and Aki Shimizu and Asuka Shimoki and Takahiro Masuda and Yasunori Yoshimura",
year = "2002",
month = "3",
language = "English",
volume = "51",
pages = "93--99",
journal = "Keio Journal of Medicine",
issn = "0022-9717",
publisher = "Keio University School of Medicine",
number = "2",

}

TY - JOUR

T1 - Protein tyrosine phosphorylation signaling in the differentiation of human endometrial stromal cells

AU - Maruyama, Tetsuo

AU - Yamamoto, Yurie

AU - Sakai, Nozomi

AU - Shimizu, Aki

AU - Shimoki, Asuka

AU - Masuda, Takahiro

AU - Yoshimura, Yasunori

PY - 2002/3

Y1 - 2002/3

N2 - Reversible protein tyrosine phosphorylation, coordinately controlled by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs), is a critical element in signal transduction pathways regulating cell growth, differentiation, apoptosis, and tumorigenesis. The differentiation of human endometrial stromal cells (decidualization) is crucial for successful embryo implantation and maintenance of pregnancy; however, little is known about the molecular events involving tyrosine phosphorylation, PTKs, and PTPs in the process of decidualization. We have previously reported that the tyrosine kinase activity of c-Src belonging to the Src family kinase is increased together with altered tyrosine phosphorylation of several cellular proteins in the in vitro model of decidualization. Focal adhesion kinase (FAK) and paxillin are known to form a complex with c-Src at the focal contacts and to participate in the integrin-mediated signal transduction as c-Src substrates. Those focal adhesion proteins, however, are not hyperphosphorylated on tyrosine during decidualization. Moreover, the loss of focal adhesions and the disorganization of the actin-based cytoskeleton were observed in decidualized stromal cells, suggesting that the escape from regulation by c-Src may be in part due to the decidualization-induced disruption of the interaction between the focal adhesion proteins and c-Src. These findings collectively indicate that decidual c-Src may activate signaling pathway(s) different from the integrin-mediated signaling cascade involving FAK and paxillin. This review summarizes our recent studies on the tyrosine phosphorylation signaling pathway(s) in decidualization.

AB - Reversible protein tyrosine phosphorylation, coordinately controlled by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs), is a critical element in signal transduction pathways regulating cell growth, differentiation, apoptosis, and tumorigenesis. The differentiation of human endometrial stromal cells (decidualization) is crucial for successful embryo implantation and maintenance of pregnancy; however, little is known about the molecular events involving tyrosine phosphorylation, PTKs, and PTPs in the process of decidualization. We have previously reported that the tyrosine kinase activity of c-Src belonging to the Src family kinase is increased together with altered tyrosine phosphorylation of several cellular proteins in the in vitro model of decidualization. Focal adhesion kinase (FAK) and paxillin are known to form a complex with c-Src at the focal contacts and to participate in the integrin-mediated signal transduction as c-Src substrates. Those focal adhesion proteins, however, are not hyperphosphorylated on tyrosine during decidualization. Moreover, the loss of focal adhesions and the disorganization of the actin-based cytoskeleton were observed in decidualized stromal cells, suggesting that the escape from regulation by c-Src may be in part due to the decidualization-induced disruption of the interaction between the focal adhesion proteins and c-Src. These findings collectively indicate that decidual c-Src may activate signaling pathway(s) different from the integrin-mediated signaling cascade involving FAK and paxillin. This review summarizes our recent studies on the tyrosine phosphorylation signaling pathway(s) in decidualization.

KW - C-Src

KW - Decidualization

KW - Endometrium

KW - Focal adhesion

KW - Tyrosine phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=0036598941&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036598941&partnerID=8YFLogxK

M3 - Article

C2 - 12125911

AN - SCOPUS:0036598941

VL - 51

SP - 93

EP - 99

JO - Keio Journal of Medicine

JF - Keio Journal of Medicine

SN - 0022-9717

IS - 2

ER -