Role of phospholipase C-γ1 in insulin-like growth factor I-induced muscle differentiation of H9c2 cardiac myoblasts

Feng Hong; Keun ai Moon; Sam Soo Kim; Young Seol Kim; Young Kil Choi; Yun Soo Bae; Pann Ghill Suh; Sung Ho Ryu; Eui Ju Choi; Joohun Ha; Sung Soo Kim

doi:10.1006/bbrc.2001.4644

Role of phospholipase C-γ1 in insulin-like growth factor I-induced muscle differentiation of H9c2 cardiac myoblasts

Feng Hong
, Keun ai Moon
, Sam Soo Kim^*
, Young Seol Kim
, Young Kil Choi
, Yun Soo Bae
, Pann Ghill Suh
, Sung Ho Ryu
, Eui Ju Choi
, Joohun Ha
, Sung Soo Kim^*

^*Corresponding author for this work

Department of Life Sciences

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

20 Citations (Scopus)

Abstract

Insulin-like growth factor-I (IGF-I) regulates muscle differentiation through phosphatidylinositol 3-kinase (PI 3-kinase). Also it was recently reported that PI 3-kinase is involved in the activation of phospholipase C-γ1 (PLC-γ1). We investigated whether PLC-γ1 therefore plays a role in IGF-I-induced muscle differentiation using H9c2 rat cardiac myoblasts as a model. IGF-I was able to activate PLC-γ1 via both PI 3-kinase-dependent and tyrosine phosphorylation-dependent mechanisms in this model. However, PI 3-kinase appeared to play a more important role than tyrosine phosphorylation in IGF-I activation of PLC-γ1. In addition, PLC-γ1 activation was independent of Akt/protein kinase B (Akt/PKB). Importantly, PLC-γ1 was involved in IGF-I-induced muscle differentiation in parallel with Akt/PKB. Taken together, these results suggest that IGF-I regulation of muscle differentiation is dependent on the activation of PLC-γ1 and Akt/PKB, both of which are downstream mediators of PI 3-kinase.

Original language	English
Pages (from-to)	816-822
Number of pages	7
Journal	Biochemical and biophysical research communications
Volume	282
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.2001.4644
Publication status	Published - 2001

Bibliographical note

Funding Information:
We are very grateful to Dr. Julian Downward at the Imperial Cancer Research Fund Laboratory, United Kingdom, and Dr. Masato Kasuga at Kobe University, Japan, for providing us with vectors encoding a constitutively active (p110*) and a dominant negative (Δp85) form of PI3-kinase. Dr. Feng Hong is a recipient of fellowship provided by Korea United Pharmaceutical Inc.

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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@article{ad5ec60bba9a40f4ad0db95c0ea44eb1,

title = "Role of phospholipase C-γ1 in insulin-like growth factor I-induced muscle differentiation of H9c2 cardiac myoblasts",

abstract = "Insulin-like growth factor-I (IGF-I) regulates muscle differentiation through phosphatidylinositol 3-kinase (PI 3-kinase). Also it was recently reported that PI 3-kinase is involved in the activation of phospholipase C-γ1 (PLC-γ1). We investigated whether PLC-γ1 therefore plays a role in IGF-I-induced muscle differentiation using H9c2 rat cardiac myoblasts as a model. IGF-I was able to activate PLC-γ1 via both PI 3-kinase-dependent and tyrosine phosphorylation-dependent mechanisms in this model. However, PI 3-kinase appeared to play a more important role than tyrosine phosphorylation in IGF-I activation of PLC-γ1. In addition, PLC-γ1 activation was independent of Akt/protein kinase B (Akt/PKB). Importantly, PLC-γ1 was involved in IGF-I-induced muscle differentiation in parallel with Akt/PKB. Taken together, these results suggest that IGF-I regulation of muscle differentiation is dependent on the activation of PLC-γ1 and Akt/PKB, both of which are downstream mediators of PI 3-kinase.",

author = "Feng Hong and Moon, \{Keun ai\} and Kim, \{Sam Soo\} and Kim, \{Young Seol\} and Choi, \{Young Kil\} and Bae, \{Yun Soo\} and Suh, \{Pann Ghill\} and Ryu, \{Sung Ho\} and Choi, \{Eui Ju\} and Joohun Ha and Kim, \{Sung Soo\}",

note = "Funding Information: We are very grateful to Dr. Julian Downward at the Imperial Cancer Research Fund Laboratory, United Kingdom, and Dr. Masato Kasuga at Kobe University, Japan, for providing us with vectors encoding a constitutively active (p110*) and a dominant negative (Δp85) form of PI3-kinase. Dr. Feng Hong is a recipient of fellowship provided by Korea United Pharmaceutical Inc.",

year = "2001",

doi = "10.1006/bbrc.2001.4644",

language = "English",

volume = "282",

pages = "816--822",

journal = "Biochemical and biophysical research communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "3",

}

TY - JOUR

T1 - Role of phospholipase C-γ1 in insulin-like growth factor I-induced muscle differentiation of H9c2 cardiac myoblasts

AU - Hong, Feng

AU - Moon, Keun ai

AU - Kim, Sam Soo

AU - Kim, Young Seol

AU - Choi, Young Kil

AU - Bae, Yun Soo

AU - Suh, Pann Ghill

AU - Ryu, Sung Ho

AU - Choi, Eui Ju

AU - Ha, Joohun

AU - Kim, Sung Soo

N1 - Funding Information: We are very grateful to Dr. Julian Downward at the Imperial Cancer Research Fund Laboratory, United Kingdom, and Dr. Masato Kasuga at Kobe University, Japan, for providing us with vectors encoding a constitutively active (p110*) and a dominant negative (Δp85) form of PI3-kinase. Dr. Feng Hong is a recipient of fellowship provided by Korea United Pharmaceutical Inc.

PY - 2001

Y1 - 2001

N2 - Insulin-like growth factor-I (IGF-I) regulates muscle differentiation through phosphatidylinositol 3-kinase (PI 3-kinase). Also it was recently reported that PI 3-kinase is involved in the activation of phospholipase C-γ1 (PLC-γ1). We investigated whether PLC-γ1 therefore plays a role in IGF-I-induced muscle differentiation using H9c2 rat cardiac myoblasts as a model. IGF-I was able to activate PLC-γ1 via both PI 3-kinase-dependent and tyrosine phosphorylation-dependent mechanisms in this model. However, PI 3-kinase appeared to play a more important role than tyrosine phosphorylation in IGF-I activation of PLC-γ1. In addition, PLC-γ1 activation was independent of Akt/protein kinase B (Akt/PKB). Importantly, PLC-γ1 was involved in IGF-I-induced muscle differentiation in parallel with Akt/PKB. Taken together, these results suggest that IGF-I regulation of muscle differentiation is dependent on the activation of PLC-γ1 and Akt/PKB, both of which are downstream mediators of PI 3-kinase.

AB - Insulin-like growth factor-I (IGF-I) regulates muscle differentiation through phosphatidylinositol 3-kinase (PI 3-kinase). Also it was recently reported that PI 3-kinase is involved in the activation of phospholipase C-γ1 (PLC-γ1). We investigated whether PLC-γ1 therefore plays a role in IGF-I-induced muscle differentiation using H9c2 rat cardiac myoblasts as a model. IGF-I was able to activate PLC-γ1 via both PI 3-kinase-dependent and tyrosine phosphorylation-dependent mechanisms in this model. However, PI 3-kinase appeared to play a more important role than tyrosine phosphorylation in IGF-I activation of PLC-γ1. In addition, PLC-γ1 activation was independent of Akt/protein kinase B (Akt/PKB). Importantly, PLC-γ1 was involved in IGF-I-induced muscle differentiation in parallel with Akt/PKB. Taken together, these results suggest that IGF-I regulation of muscle differentiation is dependent on the activation of PLC-γ1 and Akt/PKB, both of which are downstream mediators of PI 3-kinase.

UR - https://www.scopus.com/pages/publications/0034814451

U2 - 10.1006/bbrc.2001.4644

DO - 10.1006/bbrc.2001.4644

M3 - Article

C2 - 11401537

AN - SCOPUS:0034814451

SN - 0006-291X

VL - 282

SP - 816

EP - 822

JO - Biochemical and biophysical research communications

JF - Biochemical and biophysical research communications

IS - 3

ER -

Role of phospholipase C-γ1 in insulin-like growth factor I-induced muscle differentiation of H9c2 cardiac myoblasts

Abstract

Bibliographical note

ASJC Scopus subject areas

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