Specific binding of the mononuclear phagocyte colony-stimulating factor CSF-1 to the product of the v-fms oncogene

R. Sacca, E. R. Stanley, C. J. Sherr, C. W. Rettenmier

Research output: Contribution to journalArticle

50 Citations (Scopus)

Abstract

Cells transformed by the McDonough strain of feline sarcoma virus (SM-FeSV) express a v-fms-encoded glycoprotein whose expression at the cell surface correlates with the transformed phenotype. The mouse mononuclear phagocyte growth factor CSF-1 specifically binds to SM-FeSV-transformed cells at high-affinity sites indistinguishable from those detected on normal feline macrophages. A monoclonal antibody to a v-fms-encoded epitope competed for CSF-1 binding to SM-FeSV-transformed cells, and chemical cross-linking demonstrated that murine CSF-1 bound to the v-fms gene product at the cell surface. Although SM-FeSV transformed fibroblast lines were found to secrete CSF-1, the growth of transformed cells was not affected by antibodies to the v-fms gene product or to the growth factor. Tyrosine phosphorylation of the v-fms products in membranes was observed in the absence of CSF-1 and was not enhanced by addition of the murine growth factor. The data support the hypothesis that the c-fms protooncogene product is related, and possibly identical, to the CSF-1 receptor and suggest that the v-fms-encoded kinase functions in the absence of an exogenous growth factor.

Original languageEnglish (US)
Pages (from-to)3331-3335
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number10
StatePublished - 1986

Fingerprint

fms Genes
Macrophage Colony-Stimulating Factor
Phagocytes
Intercellular Signaling Peptides and Proteins
Feline Sarcoma Viruses
Macrophage Colony-Stimulating Factor Receptors
Felidae
Tyrosine
Epitopes
Glycoproteins
Phosphotransferases
Fibroblasts
Macrophages
Monoclonal Antibodies
Phosphorylation
Phenotype
Membranes
Antibodies
Growth

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Specific binding of the mononuclear phagocyte colony-stimulating factor CSF-1 to the product of the v-fms oncogene. / Sacca, R.; Stanley, E. R.; Sherr, C. J.; Rettenmier, C. W.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, No. 10, 1986, p. 3331-3335.

Research output: Contribution to journalArticle

@article{4cf9a98e042d40379b7bc74cee976e8e,
title = "Specific binding of the mononuclear phagocyte colony-stimulating factor CSF-1 to the product of the v-fms oncogene",
abstract = "Cells transformed by the McDonough strain of feline sarcoma virus (SM-FeSV) express a v-fms-encoded glycoprotein whose expression at the cell surface correlates with the transformed phenotype. The mouse mononuclear phagocyte growth factor CSF-1 specifically binds to SM-FeSV-transformed cells at high-affinity sites indistinguishable from those detected on normal feline macrophages. A monoclonal antibody to a v-fms-encoded epitope competed for CSF-1 binding to SM-FeSV-transformed cells, and chemical cross-linking demonstrated that murine CSF-1 bound to the v-fms gene product at the cell surface. Although SM-FeSV transformed fibroblast lines were found to secrete CSF-1, the growth of transformed cells was not affected by antibodies to the v-fms gene product or to the growth factor. Tyrosine phosphorylation of the v-fms products in membranes was observed in the absence of CSF-1 and was not enhanced by addition of the murine growth factor. The data support the hypothesis that the c-fms protooncogene product is related, and possibly identical, to the CSF-1 receptor and suggest that the v-fms-encoded kinase functions in the absence of an exogenous growth factor.",
author = "R. Sacca and Stanley, {E. R.} and Sherr, {C. J.} and Rettenmier, {C. W.}",
year = "1986",
language = "English (US)",
volume = "83",
pages = "3331--3335",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "10",

}

TY - JOUR

T1 - Specific binding of the mononuclear phagocyte colony-stimulating factor CSF-1 to the product of the v-fms oncogene

AU - Sacca, R.

AU - Stanley, E. R.

AU - Sherr, C. J.

AU - Rettenmier, C. W.

PY - 1986

Y1 - 1986

N2 - Cells transformed by the McDonough strain of feline sarcoma virus (SM-FeSV) express a v-fms-encoded glycoprotein whose expression at the cell surface correlates with the transformed phenotype. The mouse mononuclear phagocyte growth factor CSF-1 specifically binds to SM-FeSV-transformed cells at high-affinity sites indistinguishable from those detected on normal feline macrophages. A monoclonal antibody to a v-fms-encoded epitope competed for CSF-1 binding to SM-FeSV-transformed cells, and chemical cross-linking demonstrated that murine CSF-1 bound to the v-fms gene product at the cell surface. Although SM-FeSV transformed fibroblast lines were found to secrete CSF-1, the growth of transformed cells was not affected by antibodies to the v-fms gene product or to the growth factor. Tyrosine phosphorylation of the v-fms products in membranes was observed in the absence of CSF-1 and was not enhanced by addition of the murine growth factor. The data support the hypothesis that the c-fms protooncogene product is related, and possibly identical, to the CSF-1 receptor and suggest that the v-fms-encoded kinase functions in the absence of an exogenous growth factor.

AB - Cells transformed by the McDonough strain of feline sarcoma virus (SM-FeSV) express a v-fms-encoded glycoprotein whose expression at the cell surface correlates with the transformed phenotype. The mouse mononuclear phagocyte growth factor CSF-1 specifically binds to SM-FeSV-transformed cells at high-affinity sites indistinguishable from those detected on normal feline macrophages. A monoclonal antibody to a v-fms-encoded epitope competed for CSF-1 binding to SM-FeSV-transformed cells, and chemical cross-linking demonstrated that murine CSF-1 bound to the v-fms gene product at the cell surface. Although SM-FeSV transformed fibroblast lines were found to secrete CSF-1, the growth of transformed cells was not affected by antibodies to the v-fms gene product or to the growth factor. Tyrosine phosphorylation of the v-fms products in membranes was observed in the absence of CSF-1 and was not enhanced by addition of the murine growth factor. The data support the hypothesis that the c-fms protooncogene product is related, and possibly identical, to the CSF-1 receptor and suggest that the v-fms-encoded kinase functions in the absence of an exogenous growth factor.

UR - http://www.scopus.com/inward/record.url?scp=0011080670&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0011080670&partnerID=8YFLogxK

M3 - Article

C2 - 3010289

AN - SCOPUS:0011080670

VL - 83

SP - 3331

EP - 3335

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 10

ER -