EGF induces pi 3-kinase association with erbb2 in human airway smooth muscle (hasm) cells

V. P. Krvmskava, R. Hoffman, A. Eszterhas, V. Ciocca, Reynold Panettieri

Research output: Contribution to journalArticle

Abstract

The EGF subfamily of receptor protein tyrosine kinases mediates cellular proliferation, differentiation and transformation. Previously, we demonstrated that EGF is a potent and effective HASM cell mitogen; EGF also markedly enhanced PI 3-kinase activity. In this study, we demonstrate that the effects of EGF on HASM cell growth are mediated by activation of ErbB2 receptors. The addition of 10 ng/ml EGF to HASM cells induces a rapid increase in tyrosine phosphorylated cellular proteins and phosphorylates tyrosine residues on EGF and ErbB2 receptors. The ErbB2 tyrosine phosphorylation occurs within 30 sec and persists for 20 min. In response to EGF stimulation, PI 3-kinase activation is associated with ErbB2, but not with the EGF receptor. No effect on DNA synthesis and no change in phosphotyrosine levels are found in heregulin-treated (100 ng/ml) HASM cells. Heregulin, a specific agonist of ErbB3 and ErbB4, does not induce tyrosine phosphorylation of ErbB2 in HASM cells. ErbB2 activation, therefore, may play a critical role in regulating the mitogenic effects of EGF in non-transformed HASM cells.

Original languageEnglish (US)
JournalFASEB Journal
Volume11
Issue number9
StatePublished - Dec 1 1997
Externally publishedYes

Fingerprint

Epidermal Growth Factor
smooth muscle
myocytes
Smooth Muscle Myocytes
Muscle
phosphotransferases (kinases)
Phosphotransferases
Cells
Association reactions
tyrosine
Tyrosine
Neuregulin-1
phosphatidylinositol 3-kinase
cells
phosphorylation
Phosphatidylinositol 3-Kinases
Epidermal Growth Factor Receptor
receptor protein-tyrosine kinase
Phosphorylation
Chemical activation

All Science Journal Classification (ASJC) codes

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Krvmskava, V. P. ; Hoffman, R. ; Eszterhas, A. ; Ciocca, V. ; Panettieri, Reynold. / EGF induces pi 3-kinase association with erbb2 in human airway smooth muscle (hasm) cells. In: FASEB Journal. 1997 ; Vol. 11, No. 9.
@article{edc0d800c4b2435388f73e2837fa8af7,
title = "EGF induces pi 3-kinase association with erbb2 in human airway smooth muscle (hasm) cells",
abstract = "The EGF subfamily of receptor protein tyrosine kinases mediates cellular proliferation, differentiation and transformation. Previously, we demonstrated that EGF is a potent and effective HASM cell mitogen; EGF also markedly enhanced PI 3-kinase activity. In this study, we demonstrate that the effects of EGF on HASM cell growth are mediated by activation of ErbB2 receptors. The addition of 10 ng/ml EGF to HASM cells induces a rapid increase in tyrosine phosphorylated cellular proteins and phosphorylates tyrosine residues on EGF and ErbB2 receptors. The ErbB2 tyrosine phosphorylation occurs within 30 sec and persists for 20 min. In response to EGF stimulation, PI 3-kinase activation is associated with ErbB2, but not with the EGF receptor. No effect on DNA synthesis and no change in phosphotyrosine levels are found in heregulin-treated (100 ng/ml) HASM cells. Heregulin, a specific agonist of ErbB3 and ErbB4, does not induce tyrosine phosphorylation of ErbB2 in HASM cells. ErbB2 activation, therefore, may play a critical role in regulating the mitogenic effects of EGF in non-transformed HASM cells.",
author = "Krvmskava, {V. P.} and R. Hoffman and A. Eszterhas and V. Ciocca and Reynold Panettieri",
year = "1997",
month = "12",
day = "1",
language = "English (US)",
volume = "11",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "9",

}

EGF induces pi 3-kinase association with erbb2 in human airway smooth muscle (hasm) cells. / Krvmskava, V. P.; Hoffman, R.; Eszterhas, A.; Ciocca, V.; Panettieri, Reynold.

In: FASEB Journal, Vol. 11, No. 9, 01.12.1997.

Research output: Contribution to journalArticle

TY - JOUR

T1 - EGF induces pi 3-kinase association with erbb2 in human airway smooth muscle (hasm) cells

AU - Krvmskava, V. P.

AU - Hoffman, R.

AU - Eszterhas, A.

AU - Ciocca, V.

AU - Panettieri, Reynold

PY - 1997/12/1

Y1 - 1997/12/1

N2 - The EGF subfamily of receptor protein tyrosine kinases mediates cellular proliferation, differentiation and transformation. Previously, we demonstrated that EGF is a potent and effective HASM cell mitogen; EGF also markedly enhanced PI 3-kinase activity. In this study, we demonstrate that the effects of EGF on HASM cell growth are mediated by activation of ErbB2 receptors. The addition of 10 ng/ml EGF to HASM cells induces a rapid increase in tyrosine phosphorylated cellular proteins and phosphorylates tyrosine residues on EGF and ErbB2 receptors. The ErbB2 tyrosine phosphorylation occurs within 30 sec and persists for 20 min. In response to EGF stimulation, PI 3-kinase activation is associated with ErbB2, but not with the EGF receptor. No effect on DNA synthesis and no change in phosphotyrosine levels are found in heregulin-treated (100 ng/ml) HASM cells. Heregulin, a specific agonist of ErbB3 and ErbB4, does not induce tyrosine phosphorylation of ErbB2 in HASM cells. ErbB2 activation, therefore, may play a critical role in regulating the mitogenic effects of EGF in non-transformed HASM cells.

AB - The EGF subfamily of receptor protein tyrosine kinases mediates cellular proliferation, differentiation and transformation. Previously, we demonstrated that EGF is a potent and effective HASM cell mitogen; EGF also markedly enhanced PI 3-kinase activity. In this study, we demonstrate that the effects of EGF on HASM cell growth are mediated by activation of ErbB2 receptors. The addition of 10 ng/ml EGF to HASM cells induces a rapid increase in tyrosine phosphorylated cellular proteins and phosphorylates tyrosine residues on EGF and ErbB2 receptors. The ErbB2 tyrosine phosphorylation occurs within 30 sec and persists for 20 min. In response to EGF stimulation, PI 3-kinase activation is associated with ErbB2, but not with the EGF receptor. No effect on DNA synthesis and no change in phosphotyrosine levels are found in heregulin-treated (100 ng/ml) HASM cells. Heregulin, a specific agonist of ErbB3 and ErbB4, does not induce tyrosine phosphorylation of ErbB2 in HASM cells. ErbB2 activation, therefore, may play a critical role in regulating the mitogenic effects of EGF in non-transformed HASM cells.

UR - http://www.scopus.com/inward/record.url?scp=33750115971&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750115971&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33750115971

VL - 11

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 9

ER -