Genistein suppresses adhesion-induced protein tyrosine phosphorylation and invasion of B16-BL6 melanoma cells

Chunhong Yan, Rui Han

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Protein tyrosine phosphorylation occurs as one of the earlier events in cancer cell-extracellular matrix (ECM) interaction. With immunoblot analysis and immunofluorescence microscopy, genistein was found to suppress the tyrosine phosphorylation of proteins located at the cell periphery, including a 125 kDa protein, when B16-BL6 melanoma cells attached to and interacted with ECM. When accompanied by the suppression of adhesion-induced protein tyrosine phosphorylation, the invasive potential of B16-BL6 cells through reconstituted basement membrane was decreased significantly. However, neither adhesive capability nor cell growth was significantly affected by genistein. Therefore, the interruption of cancer cell-ECM interaction by suppression of protein tyrosine phosphorylation may contribute to invasion prevention of genistein.

Original languageEnglish (US)
Pages (from-to)117-124
Number of pages8
JournalCancer Letters
Volume129
Issue number1
DOIs
StatePublished - Jul 3 1998

Fingerprint

Experimental Melanomas
Genistein
Tyrosine
Phosphorylation
Extracellular Matrix
Proteins
Fluorescence Microscopy
Basement Membrane
Adhesives
Neoplasms
Growth

Keywords

  • Cell-extracellular matrix interaction
  • Genistein
  • Invasion
  • Protein tyrosine phosphorylation

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

Cite this

Genistein suppresses adhesion-induced protein tyrosine phosphorylation and invasion of B16-BL6 melanoma cells. / Yan, Chunhong; Han, Rui.

In: Cancer Letters, Vol. 129, No. 1, 03.07.1998, p. 117-124.

Research output: Contribution to journalArticle

@article{318054cb1f004aa3b2fdb248ec30322f,
title = "Genistein suppresses adhesion-induced protein tyrosine phosphorylation and invasion of B16-BL6 melanoma cells",
abstract = "Protein tyrosine phosphorylation occurs as one of the earlier events in cancer cell-extracellular matrix (ECM) interaction. With immunoblot analysis and immunofluorescence microscopy, genistein was found to suppress the tyrosine phosphorylation of proteins located at the cell periphery, including a 125 kDa protein, when B16-BL6 melanoma cells attached to and interacted with ECM. When accompanied by the suppression of adhesion-induced protein tyrosine phosphorylation, the invasive potential of B16-BL6 cells through reconstituted basement membrane was decreased significantly. However, neither adhesive capability nor cell growth was significantly affected by genistein. Therefore, the interruption of cancer cell-ECM interaction by suppression of protein tyrosine phosphorylation may contribute to invasion prevention of genistein.",
keywords = "Cell-extracellular matrix interaction, Genistein, Invasion, Protein tyrosine phosphorylation",
author = "Chunhong Yan and Rui Han",
year = "1998",
month = "7",
day = "3",
doi = "10.1016/S0304-3835(98)00093-7",
language = "English (US)",
volume = "129",
pages = "117--124",
journal = "Cancer Letters",
issn = "0304-3835",
publisher = "Elsevier Ireland Ltd",
number = "1",

}

TY - JOUR

T1 - Genistein suppresses adhesion-induced protein tyrosine phosphorylation and invasion of B16-BL6 melanoma cells

AU - Yan, Chunhong

AU - Han, Rui

PY - 1998/7/3

Y1 - 1998/7/3

N2 - Protein tyrosine phosphorylation occurs as one of the earlier events in cancer cell-extracellular matrix (ECM) interaction. With immunoblot analysis and immunofluorescence microscopy, genistein was found to suppress the tyrosine phosphorylation of proteins located at the cell periphery, including a 125 kDa protein, when B16-BL6 melanoma cells attached to and interacted with ECM. When accompanied by the suppression of adhesion-induced protein tyrosine phosphorylation, the invasive potential of B16-BL6 cells through reconstituted basement membrane was decreased significantly. However, neither adhesive capability nor cell growth was significantly affected by genistein. Therefore, the interruption of cancer cell-ECM interaction by suppression of protein tyrosine phosphorylation may contribute to invasion prevention of genistein.

AB - Protein tyrosine phosphorylation occurs as one of the earlier events in cancer cell-extracellular matrix (ECM) interaction. With immunoblot analysis and immunofluorescence microscopy, genistein was found to suppress the tyrosine phosphorylation of proteins located at the cell periphery, including a 125 kDa protein, when B16-BL6 melanoma cells attached to and interacted with ECM. When accompanied by the suppression of adhesion-induced protein tyrosine phosphorylation, the invasive potential of B16-BL6 cells through reconstituted basement membrane was decreased significantly. However, neither adhesive capability nor cell growth was significantly affected by genistein. Therefore, the interruption of cancer cell-ECM interaction by suppression of protein tyrosine phosphorylation may contribute to invasion prevention of genistein.

KW - Cell-extracellular matrix interaction

KW - Genistein

KW - Invasion

KW - Protein tyrosine phosphorylation

UR - http://www.scopus.com/inward/record.url?scp=0032479518&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032479518&partnerID=8YFLogxK

U2 - 10.1016/S0304-3835(98)00093-7

DO - 10.1016/S0304-3835(98)00093-7

M3 - Article

C2 - 9714343

AN - SCOPUS:0032479518

VL - 129

SP - 117

EP - 124

JO - Cancer Letters

JF - Cancer Letters

SN - 0304-3835

IS - 1

ER -