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Recognition of activated CSF-1 receptor in breast carcinomas by a tyrosine 723 phosphospecific antibody.
Oncogene. 1997 May 29; 14(21):2553-61.O

Abstract

The macrophage colony stimulating factor receptor (CSF-1R), the product of the c-fms proto-oncogene, plays an important role in regulating the normal proliferation and differentiation of macrophages and trophoblasts. However, the abnormal expression of CSF-1R transcripts and protein by human breast carcinomas has been shown to correlate with advanced stage and poor prognosis. Ligand activated CSF-1R dimers transphosphorylate several tyrosines in their cytoplasmic domains which provide recognition sites for various effector proteins in multiple signal transduction pathways. In cells transformed by the c-fms oncogene, one of the major CSF-1R phosphotyrosines, pTyr723 is important for phenotypic expression of anchorage-independent growth and metastasis. In order to investigate the relationship between receptor activation/phosphorylation and cellular phenotypes in vitro and in vivo, we prepared a CSF-1R phosphorylation-state specific antibody raised against a specific phosphopeptide of CSF-1R, which included phosphorylated tyrosine 723. On immunoblots of lysates from cells expressing CSF-1R, this antibody recognizes phosphorylated CSF-IR in CSF-1 stimulated cells but not in unstimulated cells. As an immunohistochemical reagent, this antibody stained 52% of invasive human breast tumors (72% of CSF-1R positive cases) in a sample of 114 cases and 38% of carcinoma in situ. This data represents the first direct evidence of in vivo phosphorylation of CSF-1R in human breast carcinomas.

Authors+Show Affiliations

Flick MB
Department of Therapeutic Radiology, Yale University School of Medicine, New Haven, Connecticut 06520-8040, USA.
Sapi E
No affiliation info available
Perrotta PL
No affiliation info available
Maher MG
No affiliation info available
Halaban R
No affiliation info available
Carter D
No affiliation info available
Kacinski BM
No affiliation info available

MeSH

Amino Acid SequenceAnimalsAntibodiesAntibody SpecificityBreast NeoplasmsCarcinoma in SituCells, CulturedCross ReactionsEpitopesFibroblastsGenes, fmsHumansImmunohistochemistryMacrophagesMiceMice, Inbred BALB CPhosphopeptidesPhosphorylationPhosphotyrosineReceptor, Macrophage Colony-Stimulating FactorTumor Cells, Cultured

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

9191055

Citation

Flick, M B., et al. "Recognition of Activated CSF-1 Receptor in Breast Carcinomas By a Tyrosine 723 Phosphospecific Antibody." Oncogene, vol. 14, no. 21, 1997, pp. 2553-61.
Flick MB, Sapi E, Perrotta PL, et al. Recognition of activated CSF-1 receptor in breast carcinomas by a tyrosine 723 phosphospecific antibody. Oncogene. 1997;14(21):2553-61.
Flick, M. B., Sapi, E., Perrotta, P. L., Maher, M. G., Halaban, R., Carter, D., & Kacinski, B. M. (1997). Recognition of activated CSF-1 receptor in breast carcinomas by a tyrosine 723 phosphospecific antibody. Oncogene, 14(21), 2553-61.
Flick MB, et al. Recognition of Activated CSF-1 Receptor in Breast Carcinomas By a Tyrosine 723 Phosphospecific Antibody. Oncogene. 1997 May 29;14(21):2553-61. PubMed PMID: 9191055.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Recognition of activated CSF-1 receptor in breast carcinomas by a tyrosine 723 phosphospecific antibody. AU - Flick,M B, AU - Sapi,E, AU - Perrotta,P L, AU - Maher,M G, AU - Halaban,R, AU - Carter,D, AU - Kacinski,B M, PY - 1997/5/29/pubmed PY - 1997/5/29/medline PY - 1997/5/29/entrez SP - 2553 EP - 61 JF - Oncogene JO - Oncogene VL - 14 IS - 21 N2 - The macrophage colony stimulating factor receptor (CSF-1R), the product of the c-fms proto-oncogene, plays an important role in regulating the normal proliferation and differentiation of macrophages and trophoblasts. However, the abnormal expression of CSF-1R transcripts and protein by human breast carcinomas has been shown to correlate with advanced stage and poor prognosis. Ligand activated CSF-1R dimers transphosphorylate several tyrosines in their cytoplasmic domains which provide recognition sites for various effector proteins in multiple signal transduction pathways. In cells transformed by the c-fms oncogene, one of the major CSF-1R phosphotyrosines, pTyr723 is important for phenotypic expression of anchorage-independent growth and metastasis. In order to investigate the relationship between receptor activation/phosphorylation and cellular phenotypes in vitro and in vivo, we prepared a CSF-1R phosphorylation-state specific antibody raised against a specific phosphopeptide of CSF-1R, which included phosphorylated tyrosine 723. On immunoblots of lysates from cells expressing CSF-1R, this antibody recognizes phosphorylated CSF-IR in CSF-1 stimulated cells but not in unstimulated cells. As an immunohistochemical reagent, this antibody stained 52% of invasive human breast tumors (72% of CSF-1R positive cases) in a sample of 114 cases and 38% of carcinoma in situ. This data represents the first direct evidence of in vivo phosphorylation of CSF-1R in human breast carcinomas. SN - 0950-9232 UR - https://www.unboundmedicine.com/medline/citation/9191055/Recognition_of_activated_CSF_1_receptor_in_breast_carcinomas_by_a_tyrosine_723_phosphospecific_antibody_ L2 - https://doi.org/10.1038/sj.onc.1201092 DB - PRIME DP - Unbound Medicine ER -