Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)

H. I. Chen; D. G. Fernig; P. S. Rudland; A. Sparks; Mark Wilkinson; R. Barraclough

doi:10.1006/bbrc.2001.5517

Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)

H. I. Chen, D. G. Fernig, P. S. Rudland, A. Sparks, Mark Wilkinson, R. Barraclough

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

78 Citations (Scopus)

Abstract

Experimentally elevated levels of S100A4 induce a metastatic phenotype in benign mammary tumour cells in vivo. In humans, the presence of S100A4 in breast cancer cells correlates strongly with reduced patient survival. Potential interacting binding partners for S100A4 have now been examined using an optical biosensor. There was significant interaction of S100A4 with non-muscle myosin and p53, but not with actin, tropomyosin or tubulin. The results suggest that myosin and p53 are likely to be intracellular targets of S100A4. S100A4 had a greater affinity for wild-type or mutant arg-175-his p53 than for non-muscle myosin. The results suggest that S100A4 might induce metastasis by influencing the function of p53 as well as through its interaction with myosin and that any mechanism is independent of the mutational status of p53.

Original language	English
Pages (from-to)	1212-1217
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	286
Issue number	5
DOIs	https://doi.org/10.1006/bbrc.2001.5517
Publication status	Published - 1 Jan 2001
Externally published	Yes

Keywords

Breast cancer
Metastasis
Myosin
Optical biosensor
P53
P9Ka
S100A4

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1006/bbrc.2001.5517

78 Citations
1 Other contribution

Erratum: "Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)"
Chen, H. L., Fernig, D. G., Rudland, P. S., Sparks, A., Wilkinson, M. & Barraclough, R., 22 Aug 2003, 1 p.
Research output: Other contribution

Open Access

3 Citations (Scopus)

Cite this

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title = "Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)",

abstract = "Experimentally elevated levels of S100A4 induce a metastatic phenotype in benign mammary tumour cells in vivo. In humans, the presence of S100A4 in breast cancer cells correlates strongly with reduced patient survival. Potential interacting binding partners for S100A4 have now been examined using an optical biosensor. There was significant interaction of S100A4 with non-muscle myosin and p53, but not with actin, tropomyosin or tubulin. The results suggest that myosin and p53 are likely to be intracellular targets of S100A4. S100A4 had a greater affinity for wild-type or mutant arg-175-his p53 than for non-muscle myosin. The results suggest that S100A4 might induce metastasis by influencing the function of p53 as well as through its interaction with myosin and that any mechanism is independent of the mutational status of p53.",

keywords = "Breast cancer, Metastasis, Myosin, Optical biosensor, P53, P9Ka, S100A4",

author = "Chen, \{H. I.\} and Fernig, \{D. G.\} and Rudland, \{P. S.\} and A. Sparks and Mark Wilkinson and R. Barraclough",

year = "2001",

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doi = "10.1006/bbrc.2001.5517",

language = "English",

volume = "286",

pages = "1212--1217",

journal = "Biochemical and Biophysical Research Communications",

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TY - JOUR

T1 - Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)

AU - Chen, H. I.

AU - Fernig, D. G.

AU - Rudland, P. S.

AU - Sparks, A.

AU - Wilkinson, Mark

AU - Barraclough, R.

PY - 2001/1/1

Y1 - 2001/1/1

N2 - Experimentally elevated levels of S100A4 induce a metastatic phenotype in benign mammary tumour cells in vivo. In humans, the presence of S100A4 in breast cancer cells correlates strongly with reduced patient survival. Potential interacting binding partners for S100A4 have now been examined using an optical biosensor. There was significant interaction of S100A4 with non-muscle myosin and p53, but not with actin, tropomyosin or tubulin. The results suggest that myosin and p53 are likely to be intracellular targets of S100A4. S100A4 had a greater affinity for wild-type or mutant arg-175-his p53 than for non-muscle myosin. The results suggest that S100A4 might induce metastasis by influencing the function of p53 as well as through its interaction with myosin and that any mechanism is independent of the mutational status of p53.

AB - Experimentally elevated levels of S100A4 induce a metastatic phenotype in benign mammary tumour cells in vivo. In humans, the presence of S100A4 in breast cancer cells correlates strongly with reduced patient survival. Potential interacting binding partners for S100A4 have now been examined using an optical biosensor. There was significant interaction of S100A4 with non-muscle myosin and p53, but not with actin, tropomyosin or tubulin. The results suggest that myosin and p53 are likely to be intracellular targets of S100A4. S100A4 had a greater affinity for wild-type or mutant arg-175-his p53 than for non-muscle myosin. The results suggest that S100A4 might induce metastasis by influencing the function of p53 as well as through its interaction with myosin and that any mechanism is independent of the mutational status of p53.

KW - Breast cancer

KW - Metastasis

KW - Myosin

KW - Optical biosensor

KW - P53

KW - P9Ka

KW - S100A4

U2 - 10.1006/bbrc.2001.5517

DO - 10.1006/bbrc.2001.5517

M3 - Article

SN - 0006-291X

VL - 286

SP - 1212

EP - 1217

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 5

ER -

Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)

Abstract

Keywords

UN SDGs

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Research output

Erratum: "Binding to intracellular targets of the metastasis-inducing protein, S100A4 (p9Ka)"

Cite this