Nonfunctional epidermal growth factor receptor in cells transformed by Kirsten sarcoma virus

Chu Chang Chua; Deborah E. Geiman; Alain B. Schreiber; Roger L. Ladda

doi:10.1016/0006-291X(84)91336-6

Nonfunctional epidermal growth factor receptor in cells transformed by Kirsten sarcoma virus

Chu Chang Chua, Deborah E. Geiman, Alain B. Schreiber, Roger L. Ladda

Department of Pediatrics

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

12 Scopus citations

Abstract

The cell membrane receptor for epidermal growth factor (EGF) appears to be a glycoprotein of M_r 170,000 and mediates the mitogenic and metabolic responses of cells with EGF receptors (EGF-R). Normal rat kidney (NRK) have about 3 × 10⁵ EGF-R per cell. Upon transformation of NRK cells by Kirsten sarcoma virus, the transformed derivative (KNRK) loses the ability to bind ¹²⁵I-EGF. Membranes from NRK and KNRK cells were included in EGF-dependent phosphorylation reactions to search for evidence of the EGF-R. A phosphorylated protein of M_r 170,000 was detected in both NRK and KNRK membranes. The M_r 170,000 protein was identified to be EGF-R by immunoprecipitation with monoclonal antibody to the receptor. Furthermore, two-dimensional peptide mapping using trypsin and chymotrypsin digestions of the iodinated receptors from both NRK and KNRK cells showed essentially identical patterns. These data indicate that the EGF-R is present in KNRK cells with apparently the same protein structure as the NRK counterpart.

Original language	English (US)
Pages (from-to)	538-547
Number of pages	10
Journal	Biochemical and Biophysical Research Communications
Volume	118
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(84)91336-6
State	Published - Jan 30 1984

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Nonfunctional epidermal growth factor receptor in cells transformed by Kirsten sarcoma virus",

abstract = "The cell membrane receptor for epidermal growth factor (EGF) appears to be a glycoprotein of Mr 170,000 and mediates the mitogenic and metabolic responses of cells with EGF receptors (EGF-R). Normal rat kidney (NRK) have about 3 × 105 EGF-R per cell. Upon transformation of NRK cells by Kirsten sarcoma virus, the transformed derivative (KNRK) loses the ability to bind 125I-EGF. Membranes from NRK and KNRK cells were included in EGF-dependent phosphorylation reactions to search for evidence of the EGF-R. A phosphorylated protein of Mr 170,000 was detected in both NRK and KNRK membranes. The Mr 170,000 protein was identified to be EGF-R by immunoprecipitation with monoclonal antibody to the receptor. Furthermore, two-dimensional peptide mapping using trypsin and chymotrypsin digestions of the iodinated receptors from both NRK and KNRK cells showed essentially identical patterns. These data indicate that the EGF-R is present in KNRK cells with apparently the same protein structure as the NRK counterpart.",

author = "Chua, {Chu Chang} and Geiman, {Deborah E.} and Schreiber, {Alain B.} and Ladda, {Roger L.}",

note = "Funding Information: We are grateful to Dr. Dai-Kee Liu for his helpful discussion. We thank Tina M. Gingrich for typing this manuscript. This work was supported in part Grant AG-00421 from the National Institute on Aging and a Research Career Development Award, AG-00006, to R.L.L.",

year = "1984",

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doi = "10.1016/0006-291X(84)91336-6",

language = "English (US)",

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AU - Chua, Chu Chang

AU - Geiman, Deborah E.

AU - Schreiber, Alain B.

AU - Ladda, Roger L.

N1 - Funding Information: We are grateful to Dr. Dai-Kee Liu for his helpful discussion. We thank Tina M. Gingrich for typing this manuscript. This work was supported in part Grant AG-00421 from the National Institute on Aging and a Research Career Development Award, AG-00006, to R.L.L.

PY - 1984/1/30

Y1 - 1984/1/30

N2 - The cell membrane receptor for epidermal growth factor (EGF) appears to be a glycoprotein of Mr 170,000 and mediates the mitogenic and metabolic responses of cells with EGF receptors (EGF-R). Normal rat kidney (NRK) have about 3 × 105 EGF-R per cell. Upon transformation of NRK cells by Kirsten sarcoma virus, the transformed derivative (KNRK) loses the ability to bind 125I-EGF. Membranes from NRK and KNRK cells were included in EGF-dependent phosphorylation reactions to search for evidence of the EGF-R. A phosphorylated protein of Mr 170,000 was detected in both NRK and KNRK membranes. The Mr 170,000 protein was identified to be EGF-R by immunoprecipitation with monoclonal antibody to the receptor. Furthermore, two-dimensional peptide mapping using trypsin and chymotrypsin digestions of the iodinated receptors from both NRK and KNRK cells showed essentially identical patterns. These data indicate that the EGF-R is present in KNRK cells with apparently the same protein structure as the NRK counterpart.

AB - The cell membrane receptor for epidermal growth factor (EGF) appears to be a glycoprotein of Mr 170,000 and mediates the mitogenic and metabolic responses of cells with EGF receptors (EGF-R). Normal rat kidney (NRK) have about 3 × 105 EGF-R per cell. Upon transformation of NRK cells by Kirsten sarcoma virus, the transformed derivative (KNRK) loses the ability to bind 125I-EGF. Membranes from NRK and KNRK cells were included in EGF-dependent phosphorylation reactions to search for evidence of the EGF-R. A phosphorylated protein of Mr 170,000 was detected in both NRK and KNRK membranes. The Mr 170,000 protein was identified to be EGF-R by immunoprecipitation with monoclonal antibody to the receptor. Furthermore, two-dimensional peptide mapping using trypsin and chymotrypsin digestions of the iodinated receptors from both NRK and KNRK cells showed essentially identical patterns. These data indicate that the EGF-R is present in KNRK cells with apparently the same protein structure as the NRK counterpart.

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Nonfunctional epidermal growth factor receptor in cells transformed by Kirsten sarcoma virus

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